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AIMS Biophysics

2016, Volume 3, Issue 4: 456-478. doi: 10.3934/biophy.2016.4.456
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Review

Quality control mechanisms of protein biogenesis: proteostasis dies hard

  • 1.
    Institute for Research in Biomedicine (IRB), Bellinzona, Switzerland
  • 2.
    Università della Svizzera italiana (USI), Lugano, Switzerland
  • 3.
    Eidgenössische technische Hochschule Zürich (ETHZ), Departement Biologie (DBIOL), Zurich, Switzerland
  • 4.
    Ecole polytechnique de Lausanne (EPFL), Lausanne, Switzerland
  • The biosynthesis of proteins entails a complex series of chemical reactions that transform the information stored in the nucleic acid sequence into a polypeptide chain that needs to properly fold and reach its functional location in or outside the cell. It is of no surprise that errors might occur that alter the polypeptide sequence leading to a non-functional proteins or that impede delivery of proteins at the appropriate site of activity. In order to minimize such mistakes and guarantee the synthesis of the correct amount and quality of the proteome, cells have developed folding, quality control, degradation and transport mechanisms that ensure and tightly regulate protein biogenesis. Genetic mutations, harsh environmental conditions or attack by pathogens can subvert the cellular quality control machineries and perturb cellular proteostasis leading to pathological conditions. This review summarizes basic concepts of the flow of information from DNA to folded and active proteins and to the variable fidelity (from incredibly high to quite sloppy) characterizing these processes. We will give particular emphasis on events that maintain or recover the homeostasis of the endoplasmic reticulum (ER), a major site of proteins synthesis and folding in eukaryotic cells. Finally, we will report on how cells can adapt to stressful conditions, how perturbation of ER homeostasis may result in diseases and how these can be treated.

    Citation: Timothy Jan Bergmann, Giorgia Brambilla Pisoni, Maurizio Molinari. Quality control mechanisms of protein biogenesis: proteostasis dies hard[J]. AIMS Biophysics, 2016, 3(4): 456-478. doi: 10.3934/biophy.2016.4.456

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  • The biosynthesis of proteins entails a complex series of chemical reactions that transform the information stored in the nucleic acid sequence into a polypeptide chain that needs to properly fold and reach its functional location in or outside the cell. It is of no surprise that errors might occur that alter the polypeptide sequence leading to a non-functional proteins or that impede delivery of proteins at the appropriate site of activity. In order to minimize such mistakes and guarantee the synthesis of the correct amount and quality of the proteome, cells have developed folding, quality control, degradation and transport mechanisms that ensure and tightly regulate protein biogenesis. Genetic mutations, harsh environmental conditions or attack by pathogens can subvert the cellular quality control machineries and perturb cellular proteostasis leading to pathological conditions. This review summarizes basic concepts of the flow of information from DNA to folded and active proteins and to the variable fidelity (from incredibly high to quite sloppy) characterizing these processes. We will give particular emphasis on events that maintain or recover the homeostasis of the endoplasmic reticulum (ER), a major site of proteins synthesis and folding in eukaryotic cells. Finally, we will report on how cells can adapt to stressful conditions, how perturbation of ER homeostasis may result in diseases and how these can be treated.


    Abbreviations: PAAD: pancreatic adenocarcinoma; GEO: Gene Expression Omnibus; DEGs: differentially expressed genes; STRING: Search Tool for the Retrieval of Interacting Genes; MCODE: Molecular Complex Detection; GO: Gene Ontology; KEGG: Kyoto Encyclopedia of Genes and Genomes; DAVID: Database for Annotation, Visualization, and Integrated Discovery; GEPIA: Gene Expression Profiling Interactive Analysis; TIMER: Tumor Immune Estimation Resource; GSEA: Gene Set Enrichment Analysis; ECM: extracellular matrix; PPI: protein-protein interaction; MF, molecular function; BP: biological process; CC: cellular component; TCGA: The Cancer Genome Atlas; GTEx: genotype-tissue expression.

    1.   Introduction

    Pancreatic adenocarcinoma (PAAD) is the fourth leading cause of cancer deaths due to its high degree of malignancy, high recurrence rate and poor prognosis [1]. According to published statistics, there were nearly 56,770 new cases in the United States in 2019, and the 5-year survival rate is less than 10% [2]. The mechanisms of PAAD involve complex biological processes, including genomic, epigenetic and metabolic changes. The symptoms of PAAD are atypical, the disease develops rapidly, and there are no sensitive early diagnosis biomarkers or appropriate clinical treatments [3]. Potential biomarkers to assist in the diagnosis and treatment of PAAD have long been a research focus [4]. In recent years, many microarray analysis studies have been conducted to identify key genes involved in the progression of PAAD [5]. However, the key drivers of tumorigenesis remain unclear, which limits the early detection and personalized treatment of PAAD. Thus, it is urgent to reveal the underlying molecular pathogenesis of PAAD and identify effective therapeutic targets.

    In this research study, we first used three Gene Expression Synthesis (GEO) datasets (GSE62452, GSE15471 and GSE62165) to obtain differentially expressed genes (DEGs). Next, we constructed a protein-protein interaction (PPI) network using the Search Tool for the Retrieval of Interacting Genes (STRING) database and applied Cytoscape to identify significant modules and hub genes. Subsequently, the Database for Annotation, Visualization, and Integrated Discovery (DAVID) was utilized to perform Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses of the DEGs. We then estimated the prognostic value of the hub genes using the Gene Expression Profiling Interactive Analysis (GEPIA) database. Finally, we identified two genes (MMP14 and COL12A1) that were associated with the prognosis of PAAD patients. We further explored the roles of MMP14 and COL12A1 in tumor-immune interactions and their biological functions in PAAD.

    In summary, the results of this study provide new clues to further our understanding of PAAD development and identify new immune-related biomarkers for personalized therapy and prognostic monitoring of PAAD patients.

    2.   Materials and methods

    2.1.   Identification of differentially expressed genes

    The GEO is a large public genomic database containing array and sequence-based study data. The following keywords were used to search the GEO database: (pancreas OR pancreatic) AND (cancer OR carcinoma OR tumor OR neoplas* OR malignan* OR adenocarcinoma). The inclusion criteria were as follows: (1) patients diagnosed with PAAD; (2) the samples in microarrays were human tissues from patients with PAAD instead of animal tissues and cell lines; (3) the patients with PAAD were not treated with chemotherapy, radiotherapy, or any other methods; and (4) the microarray profiles included PAAD samples and nontumor tissue samples. The exclusion criteria were as follows: (1) cancer or non-cancer groups with small sample sizes (n < 10) and (2) poor‑quality profiling expression data (0, 0.1 or 1) that accounted for > 30% of the total expression data. Three transcriptome expression profiles, GSE62452, GSE15471 and GSE62165, were obtained from the GEO. The GSE62452 dataset included 69 pancreatic cancer samples and 61 normal pancreatic samples. The GSE15471 dataset consisted of 36 pairs of matched pancreatic tumor and nontumor tissues. The GSE62165 dataset contained 118 PAAD samples and 13 control samples. The three datasets were analyzed using the limma package in R software to identify DEGs. |log2FC| > 1 and adjusted P value < 0.05 were set as the cutoffs.

    2.2.   PPI network construction and module analysis

    The STRING [6] database (https://string-db.org/) was utilized to construct a PPI network. A total interaction score > 0.4 was considered statistically significant. Cytoscape [7] is a bioinformatics software used to analyze and visualize the interaction networks between molecules. We used the Molecular Complex Detection (MCODE) plugin to determine the densest and significant module in the PPI network. The criteria were as follows: degree cutoff = 2, node score cutoff = 0.2, max depth = 100 and K-score = 2. We selected the genes with the highest node score and the strongest connectivities as the PAAD hub genes.

    2.3.   GO and KEGG pathway analyses of the DEGs

    DAVID [8] (https://david.ncifcrf.gov/) is an integrated online database that can provide researchers with comprehensive gene functional annotation information to help them understand biological processes. GO analysis annotates genes and analyzes the molecular function (MF), biological process (BP) and cellular component (CC) of these genes [9]. KEGG is another powerful database for the functional interpretation of genomic sequences [10]. We used the DAVID database to analyze the GO and KEGG pathways of the DEGs. All significant GO and KEGG enrichment pathways were visualized with the ggplot package.

    2.4.   Relationship between hub genes and clinical parameters in PAAD patients

    GEPIA [11] (http://gepia.cancer-pku.cn/) is a user-friendly database that can be used to analyze and visualize large The Cancer Genome Atlas (TCGA) and Genotype-Tissue Expression (GTEx) datasets. GEPIA can perform gene expression comparisons between tumor and control samples, gene correlation analysis and survival analysis. The GEPIA database was utilized to explore the prognostic value of PAAD hub genes. In addition, we downloaded the clinical data of PAAD patients from the TCGA database and analyzed the relationship between hub gene expression and different pathological parameters by the chi-square test. A P value < 0.05 was considered statistically significant.

    2.5.   Correlation between MMP14 and COL12A1 and immune molecules

    The Tumor Immune Estimation Resource (TIMER) [12] (https://cistrome.shinyapps.io/timer/) systematically analyzes immune infiltration in cancer samples based on TCGA database data with its own algorithm. We used the TIMER database to explore the correlation between MAD14 and COL12A1 and the infiltration level of 6 types of immune cells; specifically, B cells, CD4+ T cells, CD8+ T cells, neutrophils, macrophages, and dendritic cells. Besides, TISIDB [13] (http://cis.hku.hk/TISIDB/), an online database for exploring tumor-immune system interactions, was used to assess the correlation between MMP14 and COL12A1 and the immune system in PAAD. A P value < 0.05 obtained from the Spearman's test was considered statistically significant.

    2.6.   Functional annotations of MMP14 and COL12A1

    GeneMANIA [14] (http://www.genemania.org), a user-friendly website, can display gene or gene lists that share the same functions as submitted genes and provide a PPI network. The genes interacting with MMP14 and COL12A1, as determined by GeneMANIA, were all input into Metascape [15] for further functional annotations and analyses. Meanwhile, we conducted Gene Set Enrichment Analysis (GSEA) [16] to reveal the functional pathways of MMP14 and COL12A1 in PAAD by using transcription data from the TCGA. A permutation test (1000x) was applied to identify the most significantly involved pathways. NOM p-value < 0.05 and FDR q-value < 0.25 were used as the screening criteria.

    3.   Results

    3.1.   Analysis of DEGs in PAAD

    After standardization of the microarray results, we identified 4063, 1794 and 296 DEGs from GSE62165, GSE15471 and GSE62452 respectively. Figures 1A–1C show the differential expression of genes in the tumor and normal samples in the three microarrays. A total of 209 common DEGs (153 upregulated and 56 downregulated) in the three datasets were obtained through the online tool Venn diagram (http://bioinformatics.psb.ugent.be/webtools/Venn/) (Figure 1D). The PPI network of DEGs was constructed using the STRING database and then visualized by Cytoscape software, as shown in Figure 1E. The most significant module, with 14 nodes and 83 edges, was obtained based on the PPI network of the DEGs. A total of 14 upregulated genes were identified as hub PAAD genes with a high degree of connectivity, FN1, BGN, THSB2, ASPN, COL11A1, FBN1, COL12A1, COL6A3, SPARC, COL1A1, COL3A1, COL5A2, MMP14 and POSTN (Figure 1F).

    Figure 1.  Identification and analysis of DEGs in PAAD. (A)–(C) Differential expression of genes in the tumor and normal sample in GSE62452, GSE62165 and GSE15471. Upregulated genes with adjusted P value < 0.05 and log2FC > 1 were marked in red. Downregulated genes with adjusted P value < 0.05 and log2FC < −1 were marked in green. The gray points represented genes with no significant difference. (D) An overlap of 209 common DEGs were showed in GSE62165, GSE15471 and GSE62452 datasets. (E) The PPI network of DEGs was visualized by Cytoscape. Upregulated genes were marked in red. Downregulated genes were marked in yellow. (F) The most significant module was obtained from PPI network.
    DownLoad: Full-Size Img PowerPoint

    3.2.   GO and KEGG enrichment pathways of DEGs

    The GO analysis results showed that the DEGs were significantly enriched in the biological processes of proteolysis, cell adhesion, skeletal system development, extracellular matrix organization, extracellular matrix disassembly, collagen fibril organization, collagen catabolic process and endodermal cell differentiation (Figure 2A). Changes in cellular components were significantly enriched in extracellular exosomes, extracellular regions, cell surfaces, extracellular space, endoplasmic reticulum lumen, proteinaceous extracellular matrix, collagen trimers and extracellular matrix (Figure 2B). With regard to molecular function, DEGs were mainly enriched in calcium ion binding, serine-type endopeptidase activity, integrin binding, extracellular matrix structural constituent and collagen binding (Figure 2C). KEGG pathway analysis showed that the DEGs were mainly enriched in focal adhesion, protein digestion and absorption and (extracellular matrix) ECM-receptor interaction (Figure 2D).

    Figure 2.  Significant GO and KEGG enrichment pathways of DEGs in PAAD. (A) BP terms of GO. (B) CC terms of GO. (C) MF terms of GO. (D) KEGG pathways.
    DownLoad: Full-Size Img PowerPoint

    3.3.   Clinical value of hub genes in PAAD

    Using GEPIA data, we noted that among the 14 hub genes, only MMP14 and COL12A1 were associated with the prognosis of PAAD patients. Patients with high MMP14 expression had a worse overall (P = 0.033, HR = 1.6) and disease-free survival rates (P = 0.0035, HR = 1.9) (Figure 3A, B). High expression of COL12A1 indicated a poor overall survival outcome (P = 0.0055, HR = 1.8), but it had no effect on the patient's disease-free survival rate (P = 0.057, HR = 1.5) (Figure 3C, D). In addition, as shown in Table 1, MMP14 expression was correlated with tumor grade and M classification, and COL12A1 expression was associated with tumor grade, stage, and T, N and M classification in PAAD (P value < 0.05). Taken together, these results suggested that the hub genes MMP14 and COL12A1 have clinical relevance in PAAD. Thus, we further explored the roles of MMP14 and COL12A1 in tumor-immune interactions and their biological functions in PAAD.

    Figure 3.  Prognostic value of MMP14 and COL12A1 in PAAD patients analyzed by GEPIA. Logrank P < 0.05 was statistically significant. (A)–(B) High MMP14 expression was associated with worse overall and disease-free survival in PAAD. (C)–(D) High expression of COL12A1was significantly associated with worse overall survival while disease-free survival was not statistically significant in PAAD.
    DownLoad: Full-Size Img PowerPoint
    Table 1.  Relationship between MMP14 and COL12A1 expression and clinicopathological parameters of PAAD.
    Parameters Overall(n = 178) COL12A1 expression P MMP14 expression P
    low (89) high (89) high (89) low (89)
    Primary site (%) 0.262 0.295
      Body of Pancreas 14 (7.9) 9 (10.1) 5 (5.6) 9 (10.1) 5 (5.6)
      Head of Pancreas 139 (78.1) 65 (73.0) 74 (83.1) 69 (77.5) 70 (78.7)
      Tail of Pancreas 14 (7.9) 7 (7.9) 7 (7.9) 8 (9.0) 6 (6.7)
      Other 11 (6.2) 8 (9.0) 3 (3.4) 3 (3.4) 8 (9.0)
    Pathological type (%) 0.094 0.094
      Other Type 25 (14.1) 18 (20.2) 7 (8.0) 7 (8.0) 18 (20.2)
      Ductal Type 147 (83.1) 69 (77.5) 78 (88.6) 78 (88.6) 69 (77.5)
      Colloid Carcinoma 4 (2.3) 2 (2.2) 2 (2.3) 2 (2.3) 2 (2.2)
      Undifferentiated Carcinoma 1 (0.6) 0 (0.0) 1 (1.1) 1 (1.1) 0 (0.0)
    Grade (%) 0.044 0.018
      G1 31 (17.4) 22 (24.7) 9 (10.1) 8 (9.0) 23 (25.8)
      G2 95 (53.4) 40 (44.9) 55 (61.8) 51 (57.3) 44 (49.4)
      G3 48 (27.0) 24 (27.0) 24 (27.0) 29 (32.6) 19 (21.3)
      G4 2 (1.1) 1 (1.1) 1 (1.1) 1 (1.1) 1 (1.1)
      GX 2 (1.1) 2 (2.2) 0 (0.0) 0 (0.0) 2 (2.2)
    Tumor stage (%) 0.004 0.28
      Stage Ⅰ 21 (12.0) 18 (20.7) 3 (3.4) 7 (8.0) 14 (16.1)
      Stage Ⅱ 147 (84.0) 66 (75.9) 81 (92.0) 76 (86.4) 71 (81.6)
      Stage Ⅲ 3 (1.7) 2 (2.3) 1 (1.1) 2 (2.3) 1 (1.1)
      Stage Ⅳ 4 (2.3) 1 (1.1) 3 (3.4) 3 (3.4) 1 (1.1)
    T classification (%) 0.004 0.444
      T1 7 (4.0) 7 (8.0) 0 (0.0) 2 (2.2) 5 (5.7)
      T2 24 (13.6) 17 (19.3) 7 (7.9) 10 (11.2) 14 (15.9)
      T3 142 (80.2) 61 (69.3) 81 (91.0) 75 (84.3) 67 (76.1)
      T4 3 (1.7) 2 (2.3) 1 (1.1) 2 (2.2) 1 (1.1)
      TX 1 (0.6) 1 (1.1) 0 (0.0) 0 (0.0) 1 (1.1)
    N classification (%) 0.08 0.977
      N0 49 (27.7) 30 (34.1) 19 (21.3) 24 (27.0) 25 (28.4)
      N1 124 (70.1) 55 (62.5) 69 (77.5) 63 (70.8) 61 (69.3)
      NX 4 (2.3) 3 (3.4) 1 (1.1) 2 (2.2) 2 (2.3)
    M classification (%) 0.022 0.046
      M0 80 (44.9) 32 (36.0) 48 (53.9) 47 (52.8) 33 (37.1)
      M1 4 (2.2) 1 (1.1) 3 (3.4) 3 (3.4) 1 (1.1)
      MX 94 (52.8) 56 (62.9) 38 (42.7) (43.8) (61.8)
     | Show Table
    DownLoad: CSV

    3.4.   Correlation between MMP14 and COL12A1 with immunity

    TIMER analysis revealed that MMP14 had significant positive associations with infiltrating levels of CD8+ T cells (r = 0.251, p = 9.24e−4), macrophages (r = 0.417, p = 1.42e−8), neutrophils (r = 0.46, p = 2.5e−10) and dendritic cells (r = 0.463, p = 1.77e−10) in PAAD (Figure 4A). COL12A1 significantly correlated with B cells (r = 0.183, p = 1.67e−2), CD8+ T cells (r = 0.386, p = 1.87e−7), macrophages (r = 0.537, p = 3.58e−14), neutrophils (r = 0.509, p = 1.24e−12) and dendritic cells (r = 0.526, p = 1.55e−13) in PAAD (Figure 4B). Specifically, both MMP14 and COL12A1 were strongly correlated with macrophage, neutrophil and dendritic cell infiltration.

    Figure 4.  The correlation between MMP14. (A) and COL12A1 (B) with immune cell infiltration levels in PAAD analyzed by TIMER.
    DownLoad: Full-Size Img PowerPoint

    Meanwhile, TISIDB was utilized to comprehensively analyze the relationship between MMP14 and COL12A1 and immune molecules in PAAD. With regard to tumor infiltrating lymphocytes (Figure 5), MMP14 was found to positively correlate with Tcm CD4+ T cells (rho = 0.526, P < 2.26E−16), Act DCs (rho = 0.451, P = 3.6E−10), NK cells (rho = 0.447, P = 5.38E−10) and Tcm CD8+ T cells (rho = 0.432, P = 2.23E−9), while COL12A1 was positively correlated with NK cells (rho = 0.524, P < 2.2E−16), Tcm CD8+ T cells (rho = 0.502, P < 2.2E−16), Treg cells (rho = 0.481, P = 7.19E−12) and Tgd cells (rho = 0.475, P = 2.14E-11). With regard to immunoinhibitors (Figure 6), MMP14 was found to positively correlate with TGFB1 (rho = 0.584, P < 2.26E−16), PDCD1LG2 (rho = 0.366, P = 5.69E−7), HAVCR2 (rho = 0.325, P = 1.01E−5) and TGFBR1 (rho = 0.252, P = 0.000682) while COL12A1 was positively correlated with PDCD1LG2 (rho = 0.583, P < 2.2E−16), TGFBR1 (rho = 0.431, P = 2.46E−9), HAVCR2 (rho = 0.407, P = 2.18E−8) and CD274 (rho = 0.346, P = 2.4E−6). With regard to immunostimulators (Figure 7), MMP14 was strongly positively correlated with CD276 (rho = 0.861, P < 2.2E−16), TNFSF4 (rho = 0.605, P < 2.2E−16), CD70 (rho = 0.573, P < 2.2E−16) and TNFSF9 (rho = 0.426, P = 4.02E−9) while COL12A1 was strongly positively correlated with TNFSF4 (rho = 0.758, P < 2.2E−16), CD276 (rho = 0.594, P < 2.2E−16), ENTPD1 (rho = 0.577, P < 2.2E−16) and CD70 (rho = 0.512, P < 2.2E−16). In conclusion, these results indicate functions in the immune process of PAAD.

    Figure 5.  The correlation between MMP14 (A) and COL12A1 (C) with tumor infiltrating lymphocytes in 30 types of tumors analyzed by TISIDB. The top 4 tumor infiltrating lymphocytes with the strongest positive correlation with MMP14 (B) and COL12A1 (D) in PAAD.
    DownLoad: Full-Size Img PowerPoint
    Figure 6.  The correlation between MMP14 (A) and COL12A1 (C) with immunoinhibitors in 30 types of tumors analyzed by TISIDB. The top 4 immunoinhibitors with the strongest positive correlation with MMP14 (B) and COL12A1 (D) in PAAD.
    DownLoad: Full-Size Img PowerPoint
    Figure 7.  The correlation between MMP14 (A) and COL12A1 (C) with immunostimulators in 30 types of tumors analyzed by TISIDB. The top 4 immunostimulators with the strongest positive correlation with MMP14 (B) and COL12A1 (D) in PAAD.
    DownLoad: Full-Size Img PowerPoint

    3.5.   Functions and mechanisms of MMP14 and COL12A1 in PAAD

    Figure 8A, B shows the interaction network and biological functions of MMP14 and COL12A1 and their related genes, respectively. MMP14 was found to be involved in multiple biological processes in PAAD, such as extracellular structure organization, blood vessel development, negative regulation of metallopeptidase activity and amyloid-beta clearance (Figure 8C). COL12A1 was mainly involved in extracellular matrix organization, the pid integrin1 pathway, integrin cell surface interactions, and MET activated PTK2 signaling in PAAD (Figure 8D). Moreover, GSEA was utilized to conduct hallmark and KEGG analyses for MMP14 and COL12A1 expression. The results indicated that the most significant pathways involving MMP14 included epithelial mesenchymal transition, apical junction, ECM receptor interaction, and focal adhesion (Table 2). The most significant pathways involving COL12A1 included epithelial mesenchymal transition, apical junction, focal adhesion, ECM receptor interaction, and regulation of actin cytoskeleton (Table 3).

    Figure 8.  The interaction network of MMP14 (A) and COL12A1 (B) and their related genes. The biological functions of MMP14 (C) and COL12A1 (D) and their related genes analyzed by Metascape.
    DownLoad: Full-Size Img PowerPoint
    Table 2.  The top 10 significant hallmarks and KEGG pathways in the data sets of high MMP14 expression in PAAD.
    Name ES NES NOM p-value FDR q-value
    Hallmark-epithelial mesenchymal transition 0.76 2.25 ≤ 0.001 ≤ 0.001
    Hallmark-apical junction 0.52 2.24 ≤ 0.001 ≤ 0.001
    Hallmark-apical surface 0.52 1.90 ≤ 0.001 0.04
    Hallmark-mitotic spindle 0.47 1.83 0.01 0.06
    Hallmark-hypoxia 0.47 1.82 0.01 0.06
    Hallmark-TGF-β signaling 0.56 1.82 0.01 0.05
    Hallmark-angiogenesis 0.57 1.80 0.01 0.05
    Hallmark-WNT-β catenin signaling 0.47 1.69 0.02 0.09
    Hallmark-apoptosis 0.41 1.69 0.01 0.08
    Hallmark-coagulation 0.40 1.65 0.01 0.08
    KEGG-ECM receptor interaction 0.69 2.17 ≤ 0.001 ≤ 0.001
    KEGG-focal adhesion 0.58 2.15 ≤ 0.001 ≤ 0.001
    KEGG-pathway in cancer 0.46 1.98 ≤ 0.001 0.03
    KEGG-basal cell carcinoma 0.58 1.96 ≤ 0.001 0.03
    KEGG-glycosaminoglycan biosynthesis chondroitin sulfate 0.71 1.92 ≤ 0.001 0.04
    KEGG-regulation of actin cytoskeleton 0.44 1.91 ≤ 0.001 0.04
    KEGG-small cell lung cancer 0.54 1.90 ≤ 0.001 0.03
    KEGG-pathogenic Escherichia coli infection 0.55 1.83 0.01 0.06
    KEGG-bladder cancer 0.54 1.83 0.01 0.06
    KEGG-axon guidance 0.43 1.75 ≤0.001 0.10
    *Note: ES: enrichment score; NES: normalized enrichment score; NOM: nominal. FDR: false discovery rate.
     | Show Table
    DownLoad: CSV
    Table 3.  The top 10 significant hallmarks and KEGG pathways in the data sets of high COL12A1 expression in PAAD.
    Name ES NES NOM p-value FDR q-value
    Hallmark-epithelial mesenchymal transition 0.78 2.41 ≤ 0.001 ≤ 0.001
    Hallmark-apical junction 0.48 2.10 ≤ 0.001 0.01
    Hallmark-UV response DN 0.58 2.09 ≤ 0.001 0.01
    Hallmark-TGF-β signaling 0.59 1.97 ≤ 0.001 0.02
    Hallmark-angiogenesis 0.61 1.93 0.01 0.02
    Hallmark-inflammatory response 0.53 1.86 0.01 0.04
    Hallmark-coagulation 0.44 1.78 ≤ 0.001 0.05
    Hallmark-apoptosis 0.42 1.78 0.01 0.05
    Hallmark-complement 0.45 1.76 0.01 0.05
    Hallmark-notch signaling 0.52 1.70 0.02 0.07
    KEGG-focal adhesion 0.64 2.33 ≤ 0.001 ≤ 0.001
    KEGG-ECM receptor interaction 0.71 2.20 ≤ 0.001 ≤ 0.001
    KEGG-regulation of actin cytoskeleton 0.50 2.19 ≤ 0.001 ≤ 0.001
    KEGG-pathway in cancer 0.50 2.19 ≤ 0.001 ≤ 0.001
    KEGG-TGF-β signaling 0.55 2.11 ≤ 0.001 ≤ 0.001
    KEGG-glycosaminoglycan biosynthesis chondroitin sulfate 0.77 2.10 ≤ 0.001 ≤ 0.001
    KEGG- small cell lung cancer 0.56 1.99 ≤ 0.001 0.01
    KEGG- basal cell carcinoma 0.57 1.99 ≤ 0.001 0.01
    KEGG- melanoma 0.48 1.88 ≤ 0.001 0.04
    KEGG- adherens junction 0.53 1.87 0.01 0.04
    *Note: ES: enrichment score; NES: normalized enrichment score; NOM: nominal. FDR: false discovery rate.
     | Show Table
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    4.   Discussion

    PAAD is one of the most common digestive system malignancies worldwide. The treatments available for advanced PAAD are limited, and the patient prognosis is poor. The mechanisms leading to malignancy in PAAD remain poorly characterized. Moreover, biomarkers for targeted therapy and prognosis monitoring are still elusive. In many cancers, the level of tumor immune infiltration is closely associated with patient prognosis. Thus, there is an urgent need to identify new immune-associated biomarkers that are associated with prognosis and treatment in PAAD.

    In this study, we identified 209 DEGs in PAAD using three microarray datasets from the GEO database. Through GO and KEGG enrichment analyses, we determined the biological functions and pathways of these DEGs in the development of PAAD. GO functional annotations identified many biological pathways associated with the DEGs in PAAD, including cell adhesion, ECM organization, proteolysis, collagen fibril organization, collagen catabolic process and endodermal cell differentiation. KEGG pathway analysis revealed that the DEGs were strongly associated with focal adhesion, ECM-receptor interaction and protein digestion and absorption. These pathways were found to be the most significant pathways in relation to PAAD occurrence and development. Cell adhesion is known to be a key mediator of invasiveness, metastasis, and immune suppression during malignancy since homeostasis in normal tissues is dependent on cell-to-cell adhesion [17]. Mutations and changes in the expression of cell adhesion molecules cadherins, integrins, selectins, and immunoglobulins have been associated with cancer progression in many studies [18]. The dysregulation of the ECM has recently been recognized as a key driver in the development and progression of cancer, as its organization and disassembly control malignant cell behavior and differentiation [19]. Proteolysis is the most fundamental property of malignancy, and its inhibition may be used to attenuate tumor invasion, angiogenesis and migration [20]. Perumal et al found that proteolysis of collagen fibrils is a key process in normal growth, development, repair, and cell differentiation, and in cancerous tumor progression [21]. Collagen is a major component of the ECM, and increasing evidence suggests that it influences tumor cell progression and metastasis through integrins, discoidin domain receptors, tyrosine kinase receptors, and some signaling pathways [22]. Bastidas-Ponce et al described the cellular process of pancreatic morphogenesis and demonstrated that pancreatic formation and development were closely related to endodermal cell differentiation [23]. The functional enrichment results obtained by analyzing the DEGs identified in this study provided novel insights into the mechanisms of PAAD occurrence and development. Based on the PPI network analyzed by Cytoscape, a total of 14 hub genes involved in PAAD development were identified as follows: FN1, BGN, THSB2, ASPN, COL11A1, FBN1, COL12A1, COL6A3, SPARC, COL1A1, COL3A1, COL5A2, MMP14 and POSTN.

    To determine whether these hub genes have clinical relevance in PAAD, we used GEPIA to analyze their prognostic value. We found that only MMP14 and COL12A1 were significantly associated with the survival outcomes of PAAD patients among the 14 hub genes. Our results revealed that high expression of MMP14 and COL12A1 tended to predict poor PAAD patient prognosis. In addition, MMP14 expression was correlated with tumor grade and M classification, while the expression of COL12A1 was related to tumor grade, stage, and T, N and M classification. Taken together, these results suggested that the hub genes MMP14 and COL12A1 had clinical relevance in PAAD. Thus, we selected MMP14 and COL12A1 as true hub genes for further analysis. Functional enrichment analysis and GSEA showed that MMP14 and COL12A1 significantly were involved in cancer hallmarks and KEGG pathways, including epithelial mesenchymal transition, ECM receptor interaction, apical junction, and focal adhesion. Proteolytic degradation of ECM and epithelial mesenchymal transition are known to be crucial steps in the development and progression of cancer [19,24]. The results of this study further confirmed that MMP14 and COL12A1 play important roles in the tumorigenesis and progression of PAAD.

    MMP14 is a member of the membrane-type matrix metalloprotease (MMP) family with previously known roles in ECM degradation or proteolytic protein processing [25]. Previous studies demonstrated that MMP14 affects cancer cell proliferation and invasion and is usually associated with poor patient prognosis in those with cancers such as bladder cancer, gastric cancer and hepatocellular carcinoma[26,27,28]. A meta-analysis comprehensively evaluated the expression levels of MMP14 and its prognostic value in digestive system carcinomas, such as gastric cancer, esophageal carcinoma, oral cancer and hepatocellular carcinoma [29]. However, there were no data on its prognostic value in PAAD. Previous results indicated that MMP14 mainly exerts its proto-oncogenic functions by regulating processes such as ECM degradation and remodeling, cell invasion, and cancer metastasis [30]. Wei Jiang et al reported that MMP14 expression is required for the induction of epithelial mesenchymal transition and the activation of an invasive program in pancreatic cancer [31]. These results revealed the importance of MMP14 in PAAD and indicated that MMP14 is a potential therapeutic target for PAAD.

    COL12A1 encodes the alpha chain of collagen XII, which is a member of the fibril-associated collagen family with interrupted triple helices [32]. Collage XII is an important dominant component of the ECM and interacts with other ECM molecules to provide structural support for cells [33]. As an ECM-related gene, COL12A1 has received increasing attention due to its critical role in human cancer. Some studies have explored the prognostic value of COL12A1 in different cancer types, such as breast cancer, gastric cancer and colorectal cancer [34,35,36]. IDO1 and COL12A1 synergistically participate in the metastasis of gastric cancer via the MAPK pathway[37]. The expression of COL12A1 was found to be increased in ovarian cancer and associated with the drug resistance of cancer cells[38]. In another study, it was revealed that type Ⅳ collagen promotes pancreatic cancer cell proliferation and migration and inhibits apoptosis through an autocrine loop[39]. The expression of Snail, a well-known regulator of epithelial-mesenchymal transition, was found to increase in pancreatic cancer cells in the presence of a collagen-rich milieu, suggesting that the desmoplastic reaction actively contributes to cancer progression[40]. Taken together, these results indicate that COL12A1 might serve as an effective biomarker and therapeutic target for PAAD.

    Significant progress has been made in the treatment of malignancies, especially via the use of immunotherapies. In this study, we conducted a correlation analysis between MMP14 and COL12A1 and immune-infiltrating cells in PAAD. Our results demonstrated that the expression levels of both MMP14 and COL12A1 were significantly positively associated with the infiltration levels of macrophages, neutrophils, dendritic cells and NK cells in PAAD (all P < 0.05, all cor > 0.4). Strong evidence has indicated that these tumor-infiltrating cells play significant roles in the development and progression of PAAD. Macrophages, which are the main components of the tumor microenvironment, are known to promote the initiation, progression, angiogenesis, invasion and metastasis of PAAD [41]. A meta-analysis of 1699 patients showed that a high infiltration level of macrophages was significantly associated with poor overall and disease-free survival rates in pancreatic cancer patients [42]. Many studies have established that neutrophils also promote the initiation, development and progression of pancreatic cancer and that high levels of neutrophils predict poor patient prognoses [43]. Dendritic cells are professional antigen-presenting cells and are involved in the induction and regulation of antitumor immune responses. The levels of dendritic cells have been found to be a prognostic factor in pancreatic cancer [44]. Recent clinical evidence has shown that NK cells play a critical role in the antigen-independent immune response against malignant cells and that high NK infiltration predicts poor survival in patients with advanced pancreatic cancer [45]. Patients with a high abundance of these tumor-infiltrating cells had poor survival outcomes, which is consistent with the relationship between high expression of MMP14 and COL12A1 and PAAD patient survival. Previous studies have reported that MMPs promote cancer disease progression, new blood vessel formation, invasion, metastasis, the activity of inflammatory cytokines and chemokines, and avoidance of immune surveillance [46]. MMP14 controls macrophage immune function by modulating inflammatory responses, which triggers the activation of PI3Kδ signal cascades and the remodeling of the Mi-2/NuRD nucleosome complex [47]. In addition, the results of other recent studies suggested that high collagen density can modulate the activity and functions of tumor-infiltrating macrophages and T cells to support cancer cell immune escape, which was associated with poor prognosis in patients with several types of tumor[48,49]. Thus, we hypothesize that the MMP14- and COL12A1-regulated changes in the abundance and functions of tumor immune cells, especially macrophages, neutrophils, dendritic cells and NK cells may lead to invasion, immune system avoidance, and metastasis, which is responsible for the poor prognosis of PAAD patients. However, further experiments and prospective studies are warranted to validate the exact link between these tumor-infiltrating cells and MMP14 and COL12A1 in PAAD.

    We also explored the association between MMP14 and COL12A1 and immune markers in PAAD. Among the immunostimulators, there was a high correlation coefficient between the expression of MMP14 and CD276, TNFSF4, CD70, and TNFSF9. There was also a high correlation coefficient between the expression of COL12A1 and TNFSF4, CD276, ENTPD1, and CD70 in PAAD. In terms of immunoinhibitors, MMP14 expression was positively correlated with TGFB1, PDCD1LG2, HAVCR2 and TGFBR1 while COL12A1 was positively correlated with PDCD1LG2, TGFBR1, HAVCR2 and CD274 in PAAD. Macrophages, neutrophils and dendritic cells are an essential component of innate immunity and play a vital role in various inflammatory diseases as well as in tumor progression. Evidence indicates that tumor-infiltrating lymphocytes play a significant role in the promotion or inhibition of tumor growth [50]. Du et al reported that CAR-T cells targeting CD276/B7-H3 effectively controlled the growth of pancreatic ductal adenocarcinoma, ovarian cancer and neuroblastoma in vitro and in mice without obvious toxicity [51]. CD70 is a costimulatory molecule that participates in the survival of regulatory T cells by interacting with its ligand CD27. Many studies have indicated that anti-CD70 therapy is likely beneficial for stimulating antitumor immune responses [52]. TNFSF4 is a costimulatory checkpoint protein that has been proven to enhance the antitumor activity of T cells [53]. TNFSF9 is highly expressed in PAAD tissues and is related to M1 polarization of macrophages [54]. Chen Liang demonstrated that TGFB1 could affect the progression of pancreatic cancer based on the status of SMAD4 [55]. The PD-1 receptor and its ligands PD-L1/CD274 and PD-L2/PDCD1LG2 play key roles in T cell inhibition and exhaustion. Monoclonal antibodies that block the PD-1/PD-L1 pathway have been developed for cancer immunotherapy and enhance T cell function, especially in melanoma, non-small cell lung cancer, renal cell carcinoma and bladder cancer [56]. The interactions between MMP14 and COL12A1 and immune markers have rarely been reported. Our results provide evidence for a strong correlation between MMP14 and COL12A1 and the above immune molecules in PAAD, indicating that MMP14 and COL12A1 may serve as immune-related therapy targets for PAAD.

    Our study has some limitations. This study is based on bulk RNA sequencing data used to identify biomarkers for PAAD and gene expression in rare clonal cells may have been missed. Due to the heterogeneity of cancer cells, multiple research methods are needed to reveal the molecular mechanisms of PAAD development. Emerging single-cell RNA sequencing technology, which can study every individual cell in a tumor, has become an important tool for analyzing cell biology, discovering the evolutionary relationships among cells, and revealing the heterogeneity of tumor cells [57]. Single-cell RNA sequencing technology provides a new perspective on the regulatory relationship between gene expression and the cell microenvironment [58]. Moreover, single-cell RNA sequencing technology helps identify biomarkers for predicting the prognosis and therapeutic response of tumors [59]. Recent studies have revealed the value of the application of single-cell RNA sequencing for characterizing cell heterogeneity and identifying specific cell-type biomarkers in pancreatic cancer [60,61]. In future studies, we will integrate and analyze more available data, including single-cell sequencing genomic, transcriptome and proteomic data, to provide new insights into the mechanisms of PAAD development and diagnostic and therapeutic strategies for PAAD patients.

    5.   Conclusions

    This study identified 14 hub genes and the molecular mechanisms of PAAD development by using bioinformatics analysis. Among the 14 hub genes, we found that overexpression of MMP14 and COL12A1 was significantly correlated with poor PAAD patient prognosis. Furthermore, the expression of MMP14 and COL12A1 is strongly associated with the level of immune cell infiltration and the levels of multiple immunomodulators in PAAD. Our study demonstrates that MMP14 and COL12A1 play an important role in the tumorigenesis and progression of PAAD and might become promising biomarkers and therapeutic targets.

    Acknowledgments

    This work was supported by the Nanning Qingxiu District Science and Technology Project (No.2019026), National Natural Science Foundation of China (No. 81960126), and Guangxi Natural Science Foundation (2018GXNSFBA281154).

    Conflict of interest

    The authors declare there is no conflict of interest.

    [1] Crick FHC (1956) Ideas on protein synthesis. Wellcome Library for the History and Understanding of Medicine. Avaiable from: http://archives.wellcome.ac.uk/.
    [2] Crick FHC (1970) Central Dogma of Molecular Biology. Nature 227: 561–563. doi: 10.1038/227561a0
    [3] Baltimore D (1970) RNA-dependent DNA polymerase in virions of RNA tumour viruses. Nature 226: 1209–1211. doi: 10.1038/2261209a0
    [4] Temin HM, Mizutani S (1970) RNA-dependent DNA polymerase in virions of Rous sarcoma virus. Nature 226: 1211–1213. doi: 10.1038/2261211a0
    [5] Koonin EV (2012) Does the central dogma still stand? Biol Direct 7: 27. doi: 10.1186/1745-6150-7-27
    [6] Melnikov S, Ben-Shem A, Garreau de Loubresse N, et al. (2012) One core, two shells: bacterial and eukaryotic ribosomes. Nat Struct Mol Biol 19: 560–567. doi: 10.1038/nsmb.2313
    [7] Khatter H, Myasnikov AG, Natchiar SK, et al. (2015) Structure of the human 80S ribosome. Nature 520: 640–645. doi: 10.1038/nature14427
    [8] Kolitz SE, Lorsch JR (2010) Eukaryotic initiator tRNA: finely tuned and ready for action. FEBS Lett 584: 396–404. doi: 10.1016/j.febslet.2009.11.047
    [9] Rodnina MV (2016) The ribosome in action: Tuning of translational efficiency and protein folding. Protein Sci 25: 1390–1406. doi: 10.1002/pro.2950
    [10] Dabrowski M, Bukowy-Bieryllo Z, Zietkiewicz E (2015) Translational readthrough potential of natural termination codons in eucaryotes--The impact of RNA sequence. RNA Biol 12: 950–958. doi: 10.1080/15476286.2015.1068497
    [11] Karpinets TV, Greenwood DJ, Sams CE, et al. (2006) RNA:protein ratio of the unicellular organism as a characteristic of phosphorous and nitrogen stoichiometry and of the cellular requirement of ribosomes for protein synthesis. BMC Biol 4: 1–10. doi: 10.1186/1741-7007-4-1
    [12] Ingolia NT, Lareau LF, Weissman JS (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147: 789–802. doi: 10.1016/j.cell.2011.10.002
    [13] Dennis PP, Bremer H (1974) Differential Rate of Ribosomal Protein Synthesis in Escherichia coli B/r. J Mol Biol 84: 407–422. doi: 10.1016/0022-2836(74)90449-5
    [14] Dennis PP, Nomura M (1974) Stringent Control of Ribosomal Protein Gene Expression in Escherichia coli. Proc Nat Acad Sci USA 71: 3819–3823. doi: 10.1073/pnas.71.10.3819
    [15] Young R, Bremer H (1976) Polypeptide-Chain-Elongation Rate in Escherichia coli B/r as a Function ofGrowth Rate. Biochem J 160: 185–194. doi: 10.1042/bj1600185
    [16] Schaaper RM (1993) Base selection, proofreading, and mismatch repair during DNA replication in Escherichia coli. J Biol Chem 268: 23762–23765.
    [17] Drake JW, Charlesworth B, Charlesworth D, et al. (1998) Rates of spontaneous mutation. Genetics 148: 1667–1686.
    [18] Kunkel TA (2004) DNA replication fidelity. J Biol Chem 279: 16895–16898. doi: 10.1074/jbc.R400006200
    [19] Bebenek K, Kunkel TA (2004) Functions of DNA polymerases. Adv Protein Chem 69: 137–165. doi: 10.1016/S0065-3233(04)69005-X
    [20] Kunkel TA (2009) Evolving Views of DNA Replication (In)Fidelity. Cold Spring Harb Sym 74: 91–101. doi: 10.1101/sqb.2009.74.027
    [21] Sainsbury S, Bernecky C, Cramer P (2015) Structural basis of transcription initiation by RNA polymerase II. Nat Rev Mol Cell Biol 16: 129–143. doi: 10.1038/nrm3952
    [22] Sharma N (2016) Regulation of RNA polymerase II-mediated transcriptional elongation: Implications in human disease. IUBMB Life 68: 709–716. doi: 10.1002/iub.1538
    [23] Loya TJ, Reines D (2016) Recent advances in understanding transcription termination by RNA polymerase II. F1000 Res 5: 1478.
    [24] Schwanhausser B, Busse D, Li N, et al. (2011) Global quantification of mammalian gene expression control. Nature 473: 337–342. doi: 10.1038/nature10098
    [25] Imashimizu M, Oshima T, Lubkowska L, et al. (2013) Direct assessment of transcription fidelity by high-resolution RNA sequencing. Nucleic Acids Res 41: 9090–9104. doi: 10.1093/nar/gkt698
    [26] Ninio J (1991) Connections between translation, transcription and replication error-rates. Biochimie 73: 1517–1523. doi: 10.1016/0300-9084(91)90186-5
    [27] Gouta JF, Thomasb WK, Smithc Z, et al. (2013) Large-scale detection of in vivo transcription errors. PNAS 110: 18584–18589. doi: 10.1073/pnas.1309843110
    [28] Cochella L, Green R (2005) Fidelity in protein synthesis. Curr Biol 15: 536–540. doi: 10.1016/j.cub.2005.02.019
    [29] Kramer EB, Farabaugh PJ (2007) The frequency of translational misreading errors in E. coli is largely determined by tRNA competition. RNA 13: 87–96.
    [30] Zaher HS, Green R (2009) Fidelity at the molecular level: lessons from protein synthesis. Cell 136: 746–762. doi: 10.1016/j.cell.2009.01.036
    [31] Gingold H, Pilpel Y (2011) Determinants of translation efficiency and accuracy. Mol Syst Biol 7: 141–150.
    [32] Ribas de Pouplana L, Santos MA, Zhu JH, et al. (2014) Protein mistranslation: friend or foe? Trends Biochem Sci 39: 355–362. doi: 10.1016/j.tibs.2014.06.002
    [33] Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181: 223–230. doi: 10.1126/science.181.4096.223
    [34] Bulik S, Peters B, Holzhutter HG (2005) Quantifying the Contribution of Defective Ribosomal Products to Antigen Production: A Model-Based Computational Analysis. J Immunol 175: 7957–7964. doi: 10.4049/jimmunol.175.12.7957
    [35] Vabulas RM, Hartl FU (2005) Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 310: 1960–1963. doi: 10.1126/science.1121925
    [36] Schubert U, Antón LC, Gibbs J, et al. (2000) Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404: 770–774. doi: 10.1038/35008096
    [37] Vabulas RM, Hartl UF (2005) Protein Synthesis upon Acute Nutrient Restriction Relies on Proteasome Function. Science 310: 1960–1963. doi: 10.1126/science.1121925
    [38] Hung MC, Link W (2011) Protein localization in disease and therapy. J Cell Sci 124: 3381–3392.
    [39] Chacinska A, Koehler CM, Milenkovic D, et al. (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138: 628–644. doi: 10.1016/j.cell.2009.08.005
    [40] Rapoport TA (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450: 663–669. doi: 10.1038/nature06384
    [41] Geva Y, Schuldiner M (2014) The back and forth of cargo exit from the endoplasmic reticulum. Curr Biol 24: 130–136. doi: 10.1016/j.cub.2013.12.008
    [42] Barlowe C, Helenius A (2016) Cargo Capture and Bulk Flow in the Early Secretory Pathway. Annu Rev Cell Dev Biol 32: 197–222. doi: 10.1146/annurev-cellbio-111315-125016
    [43] Herrmann JM, Neupert W (2000) Protein transport into mitochondria. Curr Opin Microbiol 3: 210–214. doi: 10.1016/S1369-5274(00)00077-1
    [44] Zimmermann R, Eyrisch S, Ahmad M, et al. (2011) Protein translocation across the ER membrane. Biochim Biophys Acta 1808: 912–924. doi: 10.1016/j.bbamem.2010.06.015
    [45] Freitas N, Cunha C (2009) Mechanisms and signals for the nuclear import of proteins. Curr Genomics 10: 550–557. doi: 10.2174/138920209789503941
    [46] Nichols WC, Seligsohn U, Zivelin A, et al. (1998) Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII. Cell 93: 61–70. doi: 10.1016/S0092-8674(00)81146-0
    [47] Spreafico M, Peyvandi F (2009) Combined Factor V and Factor VIII Deficiency. Semin Thromb Hemost 35: 390–399. doi: 10.1055/s-0029-1225761
    [48] Rock KL, Gramm C, Rothstein L, et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761–771. doi: 10.1016/S0092-8674(94)90462-6
    [49] Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895–899. doi: 10.1038/nature02263
    [50] Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477–513. doi: 10.1146/annurev.biochem.78.081507.101607
    [51] Rock KL, Farfan-Arribas DJ, Colbert JD, et al. (2014) Re-examining class-I presentation and the DRiP hypothesis. Trends Immunol 35: 144–152. doi: 10.1016/j.it.2014.01.002
    [52] Cohen-Kaplan V, Livneh I, Avni N, et al. (2016) The ubiquitin-proteasome system and autophagy: Coordinated and independent activities. Int J Biochem Cell Biol: In Press.
    [53] Ravikumar B, Sarkar S, Davies JE, et al. (2010) Regulation of mammalian autophagy in physiology and pathophysiology. Physiol Rev 90: 1383–1435. doi: 10.1152/physrev.00030.2009
    [54] Mariappan M, Li X, Stefanovic S, et al. (2010) A ribosome-associating factor chaperones tail-anchored membrane proteins. Nature 466: 1120–1124. doi: 10.1038/nature09296
    [55] Brandman O, Stewart-Ornstein J, Wong D, et al. (2012) A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress. Cell 151: 1042–1054. doi: 10.1016/j.cell.2012.10.044
    [56] Defenouillère Q, Yao Y, Mouaikel J, et al. (2013) Cdc48 associated complex bound to 60s particles is required for the clearance of aberrant translation products. PNAS 110: 5046–5051. doi: 10.1073/pnas.1221724110
    [57] Shao S, von der Malsburg K, Hegde RS (2013) Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation. Mol Cell 50: 637–648. doi: 10.1016/j.molcel.2013.04.015
    [58] Verma R, Oania RS, Kolawa1 NJ, et al. (2013) Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. eLife 2: e00308.
    [59] Shen PS, Park J, Qin Y, et al. (2016) Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains. Science 347: 75–78.
    [60] Ghaemmaghami S, Huh WK, Bower K, et al. (2003) Global analysis of protein expression in yeast. Nature 425: 737–741. doi: 10.1038/nature02046
    [61] Schwarz F, Aebi M (2011) Mechanisms and principles of N-linked protein glycosylation. Curr Opin Struct Biol 21: 576–582. doi: 10.1016/j.sbi.2011.08.005
    [62] Tannous A, Pisoni GB, Hebert DN, et al. (2015) N-linked sugar-regulated protein folding and quality control in the ER. Semin Cell Dev Biol 41: 79–89. doi: 10.1016/j.semcdb.2014.12.001
    [63] Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286: 1882–1888. doi: 10.1126/science.286.5446.1882
    [64] Aebi M, Bernasconi R, Clerc S, et al. (2010) N-glycan structures: recognition and processing in the ER. Trends Biochem Sci 35: 74–82. doi: 10.1016/j.tibs.2009.10.001
    [65] Schallus T, Feher K, Sternberg U, et al. (2010) Analysis of the specific interactions between the lectin domain of malectin and diglucosides. Glycobiology 20: 1010–1020. doi: 10.1093/glycob/cwq059
    [66] Galli C, Bernasconi R, Solda T, et al. (2011) Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER. PLoS One 6: e16304. doi: 10.1371/journal.pone.0016304
    [67] Pisoni GB, Ruddock LW, Bulleid N, et al. (2015) Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides. Mol Biol Cell 26: 3390–3400. doi: 10.1091/mbc.E15-05-0321
    [68] Lamriben L, Graham JB, Adams BM, et al. (2016) N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle. Traffic 17: 308–326. doi: 10.1111/tra.12358
    [69] Cabral CM, Choudhury P, Liu Y, et al. (2000) Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways. J Biol Chem 275: 25015–25022. doi: 10.1074/jbc.M910172199
    [70] Olivari S, Cali T, Salo KE, et al. (2006) EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem Biophys Res Commun 349: 1278–1284. doi: 10.1016/j.bbrc.2006.08.186
    [71] Ninagawa S, Okada T, Sumitomo Y, et al. (2014) EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step. J Cell Biol 206: 347–356. doi: 10.1083/jcb.201404075
    [72] Hirao K, Natsuka Y, Tamura T, et al. (2006) EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming. J Biol Chem 281: 9650–9658. doi: 10.1074/jbc.M512191200
    [73] Olivari S, Molinari M (2007) Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins. FEBS Lett 581: 3658–3664. doi: 10.1016/j.febslet.2007.04.070
    [74] Christianson JC, Shaler TA, Tyler RE, et al. (2008) OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10: 272–282. doi: 10.1038/ncb1689
    [75] Bernasconi R, Galli C, Calanca V, et al. (2010) Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. J Cell Biol 188: 223–235. doi: 10.1083/jcb.200910042
    [76] Vembar SS, Brodsky JL (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9: 944–957. doi: 10.1038/nrm2546
    [77] Merulla J, Solda T, Molinari M (2015) A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue. Mol Biol Cell 26: 1532–1542. doi: 10.1091/mbc.E14-12-1615
    [78] Merulla J, Fasana E, Solda T, et al. (2013) Specificity and regulation of the endoplasmic reticulum-associated degradation machinery. Traffic 14: 767–777. doi: 10.1111/tra.12068
    [79] Bernasconi R, Molinari M (2011) ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr Opin Cell Biol 23: 176–183. doi: 10.1016/j.ceb.2010.10.002
    [80] Koenig PA, Nicholls PK, Schmidt FI, et al. (2014) The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice. J Biol Chem 289: 34490–34502. doi: 10.1074/jbc.M114.604132
    [81] Hagiwara M, Ling J, Koenig PA, et al. (2016) Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e. Mol Cell 63: 753–767. doi: 10.1016/j.molcel.2016.07.014
    [82] Glick D, Barth S, Macleod KF (2010) Autophagy: cellular and molecular mechanisms. J Pathol 221: 3–12. doi: 10.1002/path.2697
    [83] Mizushima N, Ohsumi Y, Yoshimori T (2002) Autophagosome Formation in Mammalian Cells. Cell Struct Funct 27: 421–429. doi: 10.1247/csf.27.421
    [84] Ohsumi Y (2014) Historical landmarks of autophagy research. Cell Res 24: 9–23. doi: 10.1038/cr.2013.169
    [85] Ariosa AR, Klionsky DJ (2016) Autophagy core machinery: overcoming spatial barriers in neurons. J Mol Med (Berl): In Press.
    [86] Ryter SW, Cloonan SM, Choi AM (2013) Autophagy: a critical regulator of cellular metabolism and homeostasis. Mol Cells 36: 7–16. doi: 10.1007/s10059-013-0140-8
    [87] Choi AM, Ryter SW, Levine B (2013) Autophagy in human health and disease. N Engl J Med 368: 1845–1846. doi: 10.1056/NEJMc1303158
    [88] Lin F, Qin ZH (2013) Degradation of misfolded proteins by autophagy: is it a strategy for Huntington's disease treatment? J Huntingtons Dis 2: 149–157.
    [89] Webb JL, Ravikumar B, Atkins J, et al. (2003) Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 278: 25009–25013. doi: 10.1074/jbc.M300227200
    [90] Pickford F, Masliah E, Britschgi M, et al. (2008) The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J Clin Invest 118: 2190–2199.
    [91] Lee MJ, Lee JH, Rubinsztein DC (2013) Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog Neurobiol 105: 49–59. doi: 10.1016/j.pneurobio.2013.03.001
    [92] Perlmutter DH (2011) Alpha-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates. Annu Rev Med 62: 333–345. doi: 10.1146/annurev-med-042409-151920
    [93] Fu L, Sztul E (2009) ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy. Eur J Cell Biol 88: 215–226. doi: 10.1016/j.ejcb.2008.11.003
    [94] Farre JC, Subramani S (2016) Mechanistic insights into selective autophagy pathways: lessons from yeast. Nat Rev Mol Cell Biol 17: 537–552.
    [95] Khaminets A, Heinrich T, Mari M, et al. (2015) Regulation of endoplasmic reticulum turnover by selective autophagy. Nature 522: 354–358. doi: 10.1038/nature14498
    [96] Fumagalli FNJ, Bergmann TJ, Cebollero E, et al. (2016) Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery. Nat Cell Biol: In press.
    [97] Inoue T, Tsai B (2013) How viruses use the endoplasmic reticulum for entry, replication, and assembly. Cold Spring Harb Perspect Biol 5: a013250. doi: 10.1101/cshperspect.a013250
    [98] van den Boomen DJ, Lehner PJ (2015) Identifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class I. Mol Immunol 68: 106–111. doi: 10.1016/j.molimm.2015.07.005
    [99] Gardner BM, Pincus D, Gotthardt K, et al. (2013) Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb Perspect Biol 5: a013169.
    [100] Mori K (2009) Signalling pathways in the unfolded protein response: development from yeast to mammals. J Biochem 146: 743–750. doi: 10.1093/jb/mvp166
    [101] Zhang L, Zhang C, Wang A (2016) Divergence and Conservation of the Major UPR Branch IRE1-bZIP Signaling Pathway across Eukaryotes. Sci Rep 6: 27362. doi: 10.1038/srep27362
    [102] Lee AH, Iwakoshi NN, Glimcher LH (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23: 7448–7459. doi: 10.1128/MCB.23.21.7448-7459.2003
    [103] Hollien J, Weissman JS (2006) Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313: 104–107. doi: 10.1126/science.1129631
    [104] Haze K, Yoshida H, Yanagi H, et al. (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787–3799. doi: 10.1091/mbc.10.11.3787
    [105] Shoulders MD, Ryno LM, Genereux JC, et al. (2013) Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep 3: 1279–1292. doi: 10.1016/j.celrep.2013.03.024
    [106] Bertolotti A, Zhang Y, Hendershot LM, et al. (2000) Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326–332. doi: 10.1038/35014014
    [107] Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271–274. doi: 10.1038/16729
    [108] Vattem KM, Wek RC (2004) Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci U S A 101: 11269–11274. doi: 10.1073/pnas.0400541101
    [109] Lu PD, Harding HP, Ron D (2004) Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 167: 27–33. doi: 10.1083/jcb.200408003
    [110] Jiang HY, Wek SA, McGrath BC, et al. (2004) Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response. Mol Cell Biol 24: 1365–1377. doi: 10.1128/MCB.24.3.1365-1377.2004
    [111] Schroder M, Kaufman RJ (2005) ER stress and the unfolded protein response. Mutat Res 569: 29–63. doi: 10.1016/j.mrfmmm.2004.06.056
    [112] Redler RL, Das J, Diaz JR, et al. (2016) Protein Destabilization as a Common Factor in Diverse Inherited Disorders. J Mol Evol 82: 11–16. doi: 10.1007/s00239-015-9717-5
    [113] Sitia R, Braakman I (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426: 891–894. doi: 10.1038/nature02262
    [114] Bernier V, Lagace M, Bichet DG, et al. (2004) Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocrinol Metab 15: 222–228. doi: 10.1016/j.tem.2004.05.003
    [115] Molinari M (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3: 313–320. doi: 10.1038/nchembio880
    [116] Kopito RR, Ron D (2000) Conformational disease. Nat Cell Biol 2: 207–209. doi: 10.1038/35041139
    [117] Gidalevitz T, Ben-Zvi A, Ho KH, et al. (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311: 1471–1474. doi: 10.1126/science.1124514
    [118] Powers ET, Morimoto RI, Dillin A, et al. (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78: 959–991. doi: 10.1146/annurev.biochem.052308.114844
    [119] Morello JP, Petaja-Repo UE, Bichet DG, et al. (2000) Pharmacological chaperones: a new twist on receptor folding. Trends Pharmacol Sci 21: 466–469. doi: 10.1016/S0165-6147(00)01575-3
    [120] Cohen FE, Kelly JW (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426: 905–909. doi: 10.1038/nature02265
    [121] Convertino M, Das J, Dokholyan NV (2016) Pharmacological Chaperones: Design and Development of New Therapeutic Strategies for the Treatment of Conformational Diseases. ACS Chem Biol 11: 1471–1489. doi: 10.1021/acschembio.6b00195
    [122] Ma Y, Hendershot LM (2004) The role of the unfolded protein response in tumour development: friend or foe? Nat Rev Cancer 4: 966–977. doi: 10.1038/nrc1505
    [123] Fernandez PM, Tabbara SO, Jacobs LK, et al. (2000) Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions. Breast Cancer Res Treat 59: 15–26. doi: 10.1023/A:1006332011207
    [124] Shuda M, Kondoh N, Imazeki N, et al. (2003) Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis. J Hepatol 38: 605–614.
    [125] Song MS, Park YK, Lee JH, et al. (2001) Induction of glucose-regulated protein 78 by chronic hypoxia in human gastric tumor cells through a protein kinase C-epsilon/ERK/AP-1 signaling cascade. Cancer Res 61: 8322–8330.
    [126] Gazit G, Lu J, Lee AS (1999) De-regulation of GRP stress protein expression in human breast cancer cell lines. Breast Cancer Res Treat 54: 135–146. doi: 10.1023/A:1006102411439
    [127] Plate L, Paxman RJ, Wiseman RL, et al. (2016) Modulating protein quality control. Elife 5: e18431.
    [128] Wang X, Venable J, LaPointe P, et al. (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127: 803–815. doi: 10.1016/j.cell.2006.09.043
    [129] Mu TW, Ong DS, Wang YJ, et al. (2008) Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134: 769–781. doi: 10.1016/j.cell.2008.06.037
    [130] Chiang WC, Hiramatsu N, Messah C, et al. (2012) Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation. Invest Ophthalmol Vis Sci 53: 7159–7166. doi: 10.1167/iovs.12-10222
    [131] Luheshi LM, Dobson CM (2009) Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett 583: 2581–2586. doi: 10.1016/j.febslet.2009.06.030
    [132] Braakman I, Bulleid NJ (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem 80: 71–99. doi: 10.1146/annurev-biochem-062209-093836
    [133] Brodsky JL, Skach WR (2011) Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems. Curr Opin Cell Biol 23: 464–475. doi: 10.1016/j.ceb.2011.05.004
    [134] Papa FR, Zhang C, Shokat K, et al. (2003) Bypassing a kinase activity with an ATP-competitive drug. Science 302: 1533–1537. doi: 10.1126/science.1090031
    [135] Wiseman RL, Zhang Y, Lee KP, et al. (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell 38: 291–304. doi: 10.1016/j.molcel.2010.04.001
    [136] Wang L, Perera BG, Hari SB, et al. (2012) Divergent allosteric control of the IRE1alpha endoribonuclease using kinase inhibitors. Nat Chem Biol 8: 982–989. doi: 10.1038/nchembio.1094
    [137] Sidrauski C, Tsai JC, Kampmann M, et al. (2015) Pharmacological dimerization and activation of the exchange factor eIF2B antagonizes the integrated stress response. Elife 4: e07314.
    [138] Robblee MM, Kim CC, Porter Abate J, et al. (2016) Saturated Fatty Acids Engage an IRE1alpha-Dependent Pathway to Activate the NLRP3 Inflammasome in Myeloid Cells. Cell Rep 14: 2611–2623. doi: 10.1016/j.celrep.2016.02.053
    [139] Gallagher CM, Walter P (2016) Ceapins inhibit ATF6alpha signaling by selectively preventing transport of ATF6alpha to the Golgi apparatus during ER stress. Elife 5: e11880.
    [140] Gallagher CM, Garri C, Cain EL, et al. (2016) Ceapins are a new class of unfolded protein response inhibitors, selectively targeting the ATF6alpha branch. Elife 5: e11880.
    [141] Plate L, Cooley CB, Chen JJ, et al. (2016) Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation. Elife 5: e15550.
    [142] Hsu PD, Lander ES, Zhang F (2014) Development and applications of CRISPR-Cas9 for genome engineering. Cell 157: 1262–1278. doi: 10.1016/j.cell.2014.05.010

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    56. Ho Soonmin, The Influence of Concentration on the Formation of Chemical Bath Deposited Copper Tin Sulphide Thin Films: SEM and EDX Studies, 2022, 9, 2409-983X, 22, 10.15377/2409-983X.2022.09.3
    57. Mira Natasha Azman, Nadin Jamal Abualroos, Khatijah Aisha Yaacob, Rafidah Zainon, Feasibility of nanomaterial tungsten carbide as lead-free nanomaterial-based radiation shielding, 2023, 202, 0969806X, 110492, 10.1016/j.radphyschem.2022.110492
    58. Jose Joseph, 2023, 9780128035818, 10.1016/B978-0-12-819728-8.00132-7
    59. Ning Song, Shuo Deng, 2022, 10.5772/intechopen.108026
    60. Abderrahim Moumen, Gayan C. W. Kumarage, Elisabetta Comini, P-Type Metal Oxide Semiconductor Thin Films: Synthesis and Chemical Sensor Applications, 2022, 22, 1424-8220, 1359, 10.3390/s22041359
    61. N. Ariharan, C. G. Sriram, N. Radhika, S. Aswin, S. Haridas, A comprehensive review of vapour deposited coatings for cutting tools: properties and recent advances, 2022, 100, 0020-2967, 262, 10.1080/00202967.2022.2037343
    62. Amir Zelati, Multifractal and optical characterization of silver nanoparticles embedded in carbon films prepared in C2H2 + N2 gas mixtures, 2022, 137, 2190-5444, 10.1140/epjp/s13360-022-03307-0
    63. Olayinka O. Abegunde, Mohammed Makha, Karima Machkih, Hicham Larhlimi, Anas Ghailane, Youssef Samih, Jones Alami, Structural, mechanical and corrosion resistance of phosphorus-doped TiAlN thin film, 2022, 57, 0022-2461, 19107, 10.1007/s10853-022-07785-6
    64. Maria Badiceanu, Sinziana Anghel, Natalia Mihailescu, Anita Ioana Visan, Cristian N. Mihailescu, Ion N. Mihailescu, Coatings Functionalization via Laser versus Other Deposition Techniques for Medical Applications: A Comparative Review, 2022, 12, 2079-6412, 71, 10.3390/coatings12010071
    65. Olayinka O. Abegunde, Mohammed Makha, Hicham Larhlimi, Mohamed Lahouij, Youssef Samih, Heinz Busch, Jones Alami, Effect of bias voltage and nitrogen content on the morphological, structural, mechanical, and corrosion resistance properties of micro-alloyed Ti1−xAl0.8xP0.2XNy films deposited by high power impulse magnetron sputtering, 2023, 41, 0734-2101, 013101, 10.1116/6.0002232
    66. Barbara Popanda, Marcin Środa, 2023, Chapter 9, 978-3-031-20265-0, 319, 10.1007/978-3-031-20266-7_9
    67. Anna Lisa Semrau, Sarah V. Dummert, Christian Eckel, Sonia Mackewicz, R. Thomas Weitz, Gregor Kieslich, Synthetic Approaches Targeting Metal-Free Perovskite [HMDABCO](NH4)I3 Thin Films, 2022, 22, 1528-7483, 406, 10.1021/acs.cgd.1c01042
    68. Pouya Kazemi, Gholamreza Moradi, Dry reforming of methane over Ni/ ZrO 2 and Ni  Cu / ZrO 2 thin layer nanocatalysts in a microchannel reactor: The effect of coating time , 2023, 42, 1944-7442, 10.1002/ep.13996
    69. Gwan Seung Jeong, Yoon-Chae Jung, Na Yeon Park, Young-Jin Yu, Jin Hee Lee, Jung Hwa Seo, Jea-Young Choi, Stoichiometry and Morphology Analysis of Thermally Deposited V2O5−x Thin Films for Si/V2O5−x Heterojunction Solar Cell Applications, 2022, 15, 1996-1944, 5243, 10.3390/ma15155243
    70. Sri Bharani Ghantasala, Sumitra Sharma, Magnetron Sputtered Thin Films Based on Transition Metal Nitride: Structure and Properties, 2023, 220, 1862-6300, 2200229, 10.1002/pssa.202200229
    71. Irina Negut, Bogdan Bita, Andreea Groza, Polymeric Coatings and Antimicrobial Peptides as Efficient Systems for Treating Implantable Medical Devices Associated-Infections, 2022, 14, 2073-4360, 1611, 10.3390/polym14081611
    72. Akinsanya D. Baruwa, Olayinka O. Abegunde, Esther T. Akinlabi, Oluseyi P. Oladijo, Elizabeth M. Makhatha, Omolayo M. Ikumapayi, Shree Krishna, Jyotsna Dutta Majumdar, Radio Frequency Magnetron Sputtering Coatings of Biomedical Implants Using Nanostructured Titanium Carbide Thin films, 2021, 7, 2198-4220, 10.1007/s40735-021-00576-7
    73. Ching Joe Tang, Muhammad Azuddin Hassan, Iskandar Yahya, 2021, Direct Injection Carbon Nanotubes Thin Film Deposition System, 978-1-6654-0193-7, 416, 10.1109/SCOReD53546.2021.9652715
    74. Yogesh Singh, K.K. Maurya, V.N. Singh, A review on properties, applications, and deposition techniques of antimony selenide, 2021, 230, 09270248, 111223, 10.1016/j.solmat.2021.111223
    75. Mingyue Wang, Claire J. Carmalt, Film Fabrication of Perovskites and their Derivatives for Photovoltaic Applications via Chemical Vapor Deposition, 2022, 5, 2574-0962, 5434, 10.1021/acsaem.1c02612
    76. Ozan Aktas, Anna C. Peacock, Laser Thermal Processing of Group IV Semiconductors for Integrated Photonic Systems, 2021, 2, 2699-9293, 2000159, 10.1002/adpr.202000159
    77. Po-Chou Chen, Shu-Mei Chang, Hao-Chung Kuo, Fu-Cheng Chang, Yu-An Li, Chao-Cheng Ting, Reliability Enhancement of 14 nm HPC ASIC Using Al2O3 Thin Film Coated with Room-Temperature Atomic Layer Deposition, 2022, 12, 2079-6412, 1308, 10.3390/coatings12091308
    78. Zhuo Zhao, Fang Fang, Junsheng Wu, Xinru Tong, Yanwen Zhou, Zhe Lv, Jian Wang, David Sawtell, Interfacial Chemical Effects of Amorphous Zinc Oxide/Graphene, 2021, 14, 1996-1944, 2481, 10.3390/ma14102481
    79. Mauricio Isoldi, Edson Moriyoshi Ozono, Ronaldo Domingues Mansano, Replacement of Waveguides by a Resonant Cavity in a Microwave CVD Reactor, 2021, 49, 0093-3813, 2718, 10.1109/TPS.2021.3104748
    80. Charlotte Skjöldebrand, Joanne L. Tipper, Peter Hatto, Michael Bryant, Richard M. Hall, Cecilia Persson, Current status and future potential of wear-resistant coatings and articulating surfaces for hip and knee implants, 2022, 15, 25900064, 100270, 10.1016/j.mtbio.2022.100270
    81. Rajinder Singh Deol, Nitika Batra, Pranjal Rai, Henam Sylvia Devi, Madhusudan Singh, Film densification and electrotransportation of alkali ions in solution-deposited piezoceramic thin films under electric stress, 2022, 759, 00406090, 139469, 10.1016/j.tsf.2022.139469
    82. Ishan Choudhary, , Investigation of time-dependent stability and surface defects in sol–gel derived IGZO and IZO thin films, 2021, 100, 0928-0707, 132, 10.1007/s10971-021-05615-w
    83. Mustafa Uçar, Atilla Evcin, Osman Çelen, Development and characterisation of multifunctional surface coatings for photovoltaic panels, 2022, 11, 2046-0147, 19, 10.1680/jemmr.21.00041
    84. Kisan C. Rathod, Kallappa R. Sanadi, Pradip D. Kamble, Ganesh S. Kamble, Muddsar L. Gaur, Kalyanrao M. Garadkar, Growth Mechanism, Structural and Photoelectrochemical Study of Zinc Tellurium Thin Film, 2022, 34, 0975427X, 715, 10.14233/ajchem.2022.23458
    85. Jyothi Gutpa, Habibuddin Shaik, K. Naveen Kumar, Sheik Abdul Sattar, PVD techniques proffering avenues for fabrication of porous tungsten oxide (WO3) thin films: A review, 2022, 143, 13698001, 106534, 10.1016/j.mssp.2022.106534
    86. ERMAN ERDOGAN, CORONENE ORGANIC FILMS: OPTICAL AND SPECTRAL CHARACTERISTICS UNDER ANNEALING TEMPERATURE INFLUENCES, 2021, 28, 0218-625X, 2150081, 10.1142/S0218625X21500815
    87. Dattatraya G. Subhedar, Kamlesh V. Chauhan, Darshankumar A. Patel, An experimental investigation of TiN coating on cutting force and surface finish in milling of aluminium, 2022, 59, 22147853, 161, 10.1016/j.matpr.2021.10.384
    88. Dapeng Sun, Siying Tian, Chujun Yin, Fengling Chen, Jing Xie, Chun Huang, Chaobo Li, Thin Film Deposition Techniques in Surface Engineering Strategies for Advanced Lithium-Ion Batteries, 2023, 13, 2079-6412, 505, 10.3390/coatings13030505
    89. Meryem Khellouf, Faouzi Metina, Gomotsegang Fred Molelekwa, 2021, 978-1-83916-287-9, 83, 10.1039/9781839165436-00083
    90. Ruixue Wang, Zhangchuan Xia, Xianghao Kong, Shuang Xue, Huiyan Wang, Uniform deposition of silicon oxide film on cylindrical substrate by radially arranged plasma jet array, 2022, 437, 02578972, 128365, 10.1016/j.surfcoat.2022.128365
    91. Uzma Bilal, Muhammad Ramzan, Muhammad Imran, Gul Naz, M. Waqas Mukhtar, Farah Fahim, Hafiz M. N. Iqbal, HfO2-based nanostructured thin-films (i.e., low-e coatings) with robust optical performance and energy efficiency, 2022, 12, 2008-9244, 1131, 10.1007/s40097-022-00485-2
    92. James A. Oke, Tien-Chien Jen, Atomic layer deposition and other thin film deposition techniques: from principles to film properties, 2022, 21, 22387854, 2481, 10.1016/j.jmrt.2022.10.064
    93. Xinlong Huang, Youchao Qi, Tianzhao Bu, Xinrui Li, Guoxu Liu, Jianhua Zeng, Beibei Fan, Chi Zhang, Overview of Advanced Micro-Nano Manufacturing Technologies for Triboelectric Nanogenerators, 2022, 2, 2673-706X, 316, 10.3390/nanoenergyadv2040017
    94. Sudhanshu Dwivedi, 2023, Chapter 6, 978-981-19-8713-7, 101, 10.1007/978-981-19-8714-4_6
    95. Wangyan Wu, Wei Luo, Yunhui Huang, Less is more: a perspective on thinning lithium metal towards high-energy-density rechargeable lithium batteries, 2023, 0306-0012, 10.1039/D2CS00606E
    96. Md Shahjahan Kabir Chowdury, Young Jin Cho, Sung Bum Park, Yong-il Park, Review—Functionalized Graphene Oxide Membranes as Electrolytes, 2023, 170, 0013-4651, 033503, 10.1149/1945-7111/acc35e
    97. Yasmin A. El-Moaz, Wafaa A. Mohamed, Mai M. Rifai, Nasser N. Morgan, Khaled H. Metwally, Nabil A. Abdel Ghany, Fabrication, Characterization, and Corrosion Protection of Siloxane Coating on an Oxygen Plasma Pre-treated Silver-Copper Alloy, 2023, 1059-9495, 10.1007/s11665-023-07990-7
    98. Mahmood K. Modhi, Jamal M. Rzaij, 2023, 2591, 0094-243X, 030066, 10.1063/5.0120468
    99. Zhenhong Ye, Le Zhang, Taiwei Liu, Weicheng Xuan, Xiaodong He, Changhao Hou, Donglin Han, Binbin Yu, Junye Shi, Jie Kang, Jiangping Chen, The effect of surface nucleation modulation on the mechanical and biocompatibility of metal-polymer biomaterials, 2023, 11, 2296-4185, 10.3389/fbioe.2023.1160351
    100. Gwan Seung Jeong, Yoon-Chae Jung, Na Yeon Park, Young-Jin Yu, Jin Hee Lee, Jung Hwa Seo, Jea-Young Choi, Enhanced Passivation Efficiency of Transition Metal Oxide with Low Thermal Budget Deposition for Si/Tmo Heterojunction Solar Cell Applications, 2022, 1556-5068, 10.2139/ssrn.4096623
    101. Xudong Tao, James Dutson, Chongyang Zeng, Ceyla Asker, Sally Luong, Abdallah Reza, Botao Hao, Zheng Zhang, Joshua Ellingford, Ruy Sebastian Bonilla, Oliver Fenwick, Emiliano Bilotti, Felix Hofmann, Mike Thwaites, Hazel E. Assender, Exceptional Performance of Room Temperature Sputtered Flexible Thermoelectric Thin Film Using High Target Utilisation Sputtering Technique, 2024, 9, 2365-709X, 10.1002/admt.202301958
    102. Shariaty Faridoddin, Baranov Maksim Alexandrovich, Tsybin Oleg Yurjevich, Structure of biomolecular films through advanced imaging and statistical analysis, 2024, 702, 09277757, 134920, 10.1016/j.colsurfa.2024.134920
    103. Juan Jesus Rocha-Cuervo, Esmeralda Uribe-Lam, Cecilia Daniela Treviño-Quintanilla, Dulce Viridiana Melo-Maximo, Sputtering Plasma Effect on Zinc Oxide Thin Films Produced on Photopolymer Substrates, 2023, 15, 2073-4360, 2283, 10.3390/polym15102283
    104. Faran Baig, Zeeshan Zaheer, Zahid Khan, Faheem Qasim, A comparative study of optical, reversible wettability and UV light sensitivity of ZnO nano-structures via chemical methods, 2024, 56, 1572-817X, 10.1007/s11082-024-06451-2
    105. M. Lablali, H. Mes-Adi, A. Eddiai, K. Abderrafi, M. Mazroui, Cu thin film growth on stepped Si substrate: Effects of incident energy and thermal annealing, 2024, 637-638, 00220248, 127739, 10.1016/j.jcrysgro.2024.127739
    106. Patta Supraja, Suryasnata Tripathy, Ranjana Singh, Rahul Gangwar, Shiv Govind Singh, A novel cleanroom-free technique for simultaneous electrodeposition of polypyrrole onto array of IDuEs: Towards low-cost, stable and accurate point-of-care TBI diagnosis without trained manpower, 2025, 267, 09565663, 116824, 10.1016/j.bios.2024.116824
    107. Yana Suchikova, Sergii Kovachov, Ihor Bohdanov, Zhakyp T. Karipbaev, Vladimir Pankratov, Anatoli I. Popov, Study of the structural and morphological characteristics of the CdxTeyOz nanocomposite obtained on the surface of the CdS/ZnO heterostructure by the SILAR method, 2023, 129, 0947-8396, 10.1007/s00339-023-06776-x
    108. Wojciech Bulowski, Rafał Knura, Robert P. Socha, Maciej Basiura, Katarzyna Skibińska, Marek Wojnicki, Thin Film Semiconductor Metal Oxide Oxygen Sensors: Limitations, Challenges, and Future Progress, 2024, 13, 2079-9292, 3409, 10.3390/electronics13173409
    109. Edgar Moraru, Grigore Octavian Dontu, Sorin Cananau, Vlad-Andrei Stanescu, 2023, Chapter 29, 978-3-031-40627-0, 345, 10.1007/978-3-031-40628-7_29
    110. Muhammad Zain Ul Abidin, Muhammad Ikram, Sawaira Moeen, Ghazanfar Nazir, Mohammed Benali Kanoun, Souraya Goumri-Said, A comprehensive review on the synthesis of ferrite nanomaterials via bottom-up and top-down approaches advantages, disadvantages, characterizations and computational insights, 2024, 520, 00108545, 216158, 10.1016/j.ccr.2024.216158
    111. R.S. Devika, P. Vengatesh, T.S. Shyju, Review on ternary chalcogenides: Potential photoabsorbers, 2023, 22147853, 10.1016/j.matpr.2023.04.113
    112. Devika R S, Sagaya A. Immanuel, Vengatesh Panneerselvam, Shyju Thankaraj Salammal, Shamima Hussain, 2024, 9780323939416, 547, 10.1016/B978-0-323-93940-9.00112-2
    113. Xingcen Liu, Junbai Li, 2024, 9783527351916, 301, 10.1002/9783527841264.ch14
    114. Aimilia A. Barmpaki, Evangelia E. Zavvou, Charalampos Drivas, Konstantinos Papapetros, Labrini Sygellou, Konstantinos S. Andrikopoulos, Stella Kennou, Nikolaos D. Andritsos, Aris Giannakas, Constantinos E. Salmas, Athanasios Ladavos, Panagiotis Svarnas, Panagiota K. Karahaliou, Christoforos A. Krontiras, Atomic layer deposition of ZnO on PLA/TiO2 bionanocomposites: Evaluation of surface chemistry and physical properties toward food packaging applications, 2023, 140, 0021-8995, 10.1002/app.54465
    115. Robert J. K. Wood, Ping Lu, Coatings and Surface Modification of Alloys for Tribo-Corrosion Applications, 2024, 14, 2079-6412, 99, 10.3390/coatings14010099
    116. Łukasz Łach, Dmytro Svyetlichnyy, Recent Progress in Heat and Mass Transfer Modeling for Chemical Vapor Deposition Processes, 2024, 17, 1996-1073, 3267, 10.3390/en17133267
    117. Кристина Александровна Андрианова, Лилия Миниахмедовна Амирова, Функционально-градиентные материалы: получение, свойства, применение (обзор), 2024, 97, 0044-4618, 10.31857/S0044461824020014
    118. Gaurav Singhal, Sujan Dewanjee, Gwangmin Bae, Youngjin Ham, Danny J. Lohan, Kai‐Wei Lan, Jiaqi Li, Tarek Gebrael, Shailesh N. Joshi, Seokwoo Jeon, Nenad Miljkovic, Paul V. Braun, Interference Lithography‐Based Fabrication of 3D Metallic Mesostructures on Reflective Substrates using Electrodeposition‐Compatible Anti‐Reflection Coatings for Power Electronics Cooling, 2024, 10, 2199-160X, 10.1002/aelm.202300827
    119. Wendy Quilumbaquin, G. Xavier Castillo-Cabrera, Luis J. Borrero-González, Patricio J. Espinoza-Montero, Protocol for the preparation of TiO2-modified boron-doped diamond photoelectrode via electrophoretic deposition and its photoelectrochemical study, 2024, 5, 26661667, 103259, 10.1016/j.xpro.2024.103259
    120. S. Kovalchuk, M. Nowicki, I. Morawski, Low power silicon evaporation source—Construction, performances, and applications, 2024, 42, 2166-2746, 10.1116/6.0003284
    121. Karima Machkih, Rachid Oubaki, Mohammed Makha, A Review of CIGS Thin Film Semiconductor Deposition via Sputtering and Thermal Evaporation for Solar Cell Applications, 2024, 14, 2079-6412, 1088, 10.3390/coatings14091088
    122. Thiago C. Canevari, 2024, 9780443153341, 79, 10.1016/B978-0-443-15334-1.00005-5
    123. Muhammad Yaseen, Muhammad Arif Khan Khattak, Abbas Khan, Shaista Bibi, Mohamed Bououdina, Muhammad Usman, Niaz Ali Khan, Azhar Ali Ayaz Pirzado, Rasha A. Abumousa, Muhammad Humayun, State-of-the-art electrochromic thin films devices, fabrication techniques and applications: a review, 2024, 10, 2055-0324, 1, 10.1080/20550324.2023.2291619
    124. Yulia Eka Putri, Melvi Muharmi, Tio Putra Wendari, Diana Vanda Wellia, Growth of SrTiO3 thin film on a glass substrate by the sol-gel-assisted hydrothermal method, 2023, 40, 24680230, 103026, 10.1016/j.surfin.2023.103026
    125. Olayinka O. Abegunde, Mohamed Lahouij, Nassima Jaghar, Hicham Larhlimi, Mohammed Makha, Jones Alami, Synergistic effect of deposition temperature and substrate bias on structural, mechanical, stability and adhesion of TiN thin film prepared by reactive HiPIMS, 2023, 02728842, 10.1016/j.ceramint.2023.12.371
    126. Tom Birkoben, Hermann Kohlstedt, 2024, Chapter 1, 978-3-031-36704-5, 1, 10.1007/978-3-031-36705-2_1
    127. Xeniya Alexandrovna Leontyeva, Darya Sergeevna Puzikova, Margarita Borisovna Dergacheva, Gulinur Marsovna Khussurova, Polina Vyacheslavovna Panchenko, Synthesis and properties of semiconductor bismuth sulfide iodide for photoelectrochemical applications, 2023, 27, 13196103, 101694, 10.1016/j.jscs.2023.101694
    128. Muhammad Haseeb Nawaz, Aqsa Aizaz, Huzaifa Shafique, Abdul Qadir Ropari, Osama bin Imran, Mohamed Abbas, Muhammad Atiq Ur Rehman, Rosemary loaded Xanthan coatings on surgical grade stainless steel for potential orthopedic applications, 2024, 186, 03009440, 107987, 10.1016/j.porgcoat.2023.107987
    129. M. M. Rampai, C. B. Mtshali, N. S. Seroka, L. Khotseng, Hydrogen production, storage, and transportation: recent advances, 2024, 14, 2046-2069, 6699, 10.1039/D3RA08305E
    130. Manish Singh, Lakshmi Narayanan Ramasubramanian, Raj N. Singh, Influence of processing conditions on the titanium–aluminum contact metallization on a silicon wafer for thermal management, 2023, 41, 2166-2746, 10.1116/6.0002749
    131. Dingyi Zhang, Wenhe Yu, Lu Zhang, Xiangyang Hao, Progress in the Synthesis and Application of Transparent Conducting Film of AZO (ZnO:Al), 2023, 16, 1996-1944, 5537, 10.3390/ma16165537
    132. Mohammed A. Doheim, Fluidized Processing of Surface Engineering of Metallic Components: Problems Encountered and Effects on Design, 2024, 76, 1047-4838, 2079, 10.1007/s11837-024-06410-y
    133. Qayes A. Abbas, Mushtaq Talib Alhelaly, Mohammed A. Hameed, The inter-planner parameter and the blue shift of band gap of titanium dioxide thin films prepared using the DC reactive magnetron sputtering, 2024, 53, 0972-8821, 1516, 10.1007/s12596-023-01275-x
    134. Tanvir M. Mahim, A. H. M. A. Rahim, M. Mosaddequr Rahman, Review of Mono- and Bifacial Photovoltaic Technologies: A Comparative Study, 2024, 14, 2156-3381, 375, 10.1109/JPHOTOV.2024.3366698
    135. Zainab Albaraqaawee, Shaymaa Abbas Abdulsada, Optimisation of surface characteristics of standard duplex stainless for bio-applications by using electrophoretic deposition: A brief review, 2022, 66, 1804-1213, 96, 10.2478/kom-2022-0013
    136. Christina Floraki, Maria Androulidaki, Emmanuel Spanakis, Dimitra Vernardou, Effect of Electrolyte Concentration on the Electrochemical Performance of Spray Deposited LiFePO4, 2023, 13, 2079-4991, 1850, 10.3390/nano13121850
    137. Saumyadeep Bora, Deep Pooja, Hitesh Kulhari, 2024, Chapter 1, 978-981-99-5313-4, 1, 10.1007/978-981-99-5314-1_1
    138. Akula Umamaheswara Rao, Sunil Kumar Tiwari, Manjeet Singh Goyat, Amit Kumar Chawla, Recent developments in magnetron-sputtered silicon nitride coatings of improved mechanical and tribological properties for extreme situations, 2023, 58, 0022-2461, 9755, 10.1007/s10853-023-08575-4
    139. J. B. Roberto, M. Du, J. G. Ezold, S. L. Hogle, J. Moon, K. Myhre, K. P. Rykaczewski, Actinide targets for the synthesis of superheavy nuclei, 2023, 59, 1434-601X, 10.1140/epja/s10050-023-01144-y
    140. Khalid Bouiti, Najoua Labjar, Mohammed Benmessaoud, Anas Chraka, Mohamed Omari, Said Jebbari, Hamid Nasrellah, Souad El Hajjaji, 2024, 1469, 9780841296961, 279, 10.1021/bk-2024-1469.ch013
    141. Kenza Kamli, Zakaria Hadef, Ouarda Kamli, Baghdadi Chouial, Mohamed Salah Aida, Hani Hadjoudja, Samir Labiod, Effect of Deposition Time on the Properties of CuxZnyS Thin Films Synthesized by Ultrasonic Spray Pyrolysis, 2023, 81, 1661-9897, 37, 10.4028/p-DPoy5X
    142. Karolin Pluschke, Aaron Herrmann, Michael Dürr, Soft Deposition of Organic Molecules Based on Cluster-Induced Desorption for the Investigation of On-Surface and Surface-Mediated Reactions, 2023, 8, 2470-1343, 40639, 10.1021/acsomega.3c05518
    143. Silviane C. F. Gorski, Bruno Nunes, Abel A. C. Recco, Cesar E. da Costa, Marcus V. F. Schroeder, Julio C. Giubilei Milan, Tribological and Corrosion Behavior of AISI 1045 Coated with AISI 316 Film Produced By Triode Magnetron Sputtering, 2024, 27, 1980-5373, 10.1590/1980-5373-mr-2023-0359
    144. Yi Ren, Yin Zhang, Yadong Zhou, Shangzhong Jin, Nianbing Zhong, Yang Yue, 2024, Design of filament-type auxiliary ion source and study on its improvement of thin film parameters, 9781510674509, 33, 10.1117/12.3025158
    145. Dehen Cao, Shimin Yu, Zili Chen, Yu Wang, Hongyu Wang, Zhipeng Chen, Wei Jiang, Ya Zhang, Optimizing impedance matching parameters for single-frequency capacitively coupled plasma via machine learning, 2024, 42, 0734-2101, 10.1116/5.0173921
    146. Naiara P. V. Sebbe, Filipe Fernandes, Franciso J. G. Silva, André F. V. Pedroso, Rita C. M. Sales-Contini, Marta L. S. Barbosa, Luis M. Durão, Luis L. Magalhães, Wear Behavior of TiAlVN-Coated Tools in Milling Operations of INCONEL® 718, 2024, 14, 2079-6412, 311, 10.3390/coatings14030311
    147. Santosh Kumar, Comprehensive review on high entropy alloy-based coating, 2024, 477, 02578972, 130327, 10.1016/j.surfcoat.2023.130327
    148. G. Xavier Castillo-Cabrera, Patricio J. Espinoza-Montero, Novel trends in mixed oxide electrodes for photoelectrocatalytic wastewater treatment, 2024, 44, 24519103, 101448, 10.1016/j.coelec.2024.101448
    149. Bilisuma Fekadu Finina, Anteneh Kindu Mersha, Nano-enabled antimicrobial thin films: design and mechanism of action, 2024, 14, 2046-2069, 5290, 10.1039/D3RA07884A
    150. I. I. Vinogradov, N. A. Drozhzhin, L. I. Kravets, A. Rossouw, T. N. Vershinina, A. N. Nechaev, Formation of Hybrid Membranes for Water Desalination by Membrane Distillation, 2024, 86, 1061-933X, 667, 10.1134/S1061933X24600519
    151. Hálice de Oliveira Xavier Silva, Thales Alves Faraco, Indhira Oliveira Maciel, Welber Gianini Quirino, Benjamin Fragneaud, Paula Gomes Pereira, Cristiano Legnani, High optoelectronic quality of AZO films grown by RF-magnetron sputtering for organic electronics applications, 2023, 38, 0268-1242, 065004, 10.1088/1361-6641/acd13d
    152. Jaeho Choi, Deb Kumar Shah, M. Shaheer Akhtar, Ahmad Umar, Hassan Fouad, In-Sung Jung, Fabrication of Double Antireflection Layer of SiO2/SiNx via Spin Coating and Brush Painting for Enhanced Performance of Silicon Solar Cells, 2024, 16, 1947-2935, 18, 10.1166/sam.2024.4623
    153. Seung-Min Lee, Ju-Yong Lee, Seung-Kyun Kang, 2024, 9780323991476, 155, 10.1016/B978-0-323-99147-6.00007-7
    154. Fatemeh Seyedpour, Javad Farahbakhsh, Zoheir Dabaghian, Wafa Suwaileh, Masoumeh Zargar, Ahmad Rahimpour, Mohtada Sadrzadeh, Mathias Ulbricht, Yaghoub Mansourpanah, Advances and challenges in tailoring antibacterial polyamide thin film composite membranes for water treatment and desalination: A critical review, 2024, 581, 00119164, 117614, 10.1016/j.desal.2024.117614
    155. Khurshed Alam, Woohyung Jang, Geonwoo Jeong, Jinhui Ser, Doori Kang, Tae-Hoon Kim, Hoonsung Cho, Synthesis of High-Entropy Alloys with a Tailored Composition and Phase Structure Using a Single Configurable Target, 2024, 9, 2470-1343, 1362, 10.1021/acsomega.3c07721
    156. M.M. Osman, Zeyad Almutairi, Redhwan Almuzaiqer, Effect of spin coating speeds on electrical and optical characteristic of perovskite SrTiO3 thin films prepared by sol-gel method, 2024, 24, 25901230, 103046, 10.1016/j.rineng.2024.103046
    157. Boxuan Hu, Xiao-Lei Shi, Tianyi Cao, Meng Li, Wenyi Chen, Wei-Di Liu, Wanyu Lyu, Tuquabo Tesfamichael, Zhi-Gang Chen, Advances in Flexible Thermoelectric Materials and Devices Fabricated by Magnetron Sputtering, 2023, 2688-4046, 10.1002/smsc.202300061
    158. Sachin V. Mukhamale, Moses J. Kartha, Pankaj P. Khirade, Experimental, theoretical and numerical simulation-based investigations on the fabricated Cu2ZnSn thin-film-based Schottky diodes with enhanced electron transport for solar cell, 2024, 14, 2045-2322, 10.1038/s41598-024-63857-4
    159. Alessio Bosio, Gianluca Foti, Stefano Pasini, Donato Spoltore, A Review on the Fundamental Properties of Sb2Se3-Based Thin Film Solar Cells, 2023, 16, 1996-1073, 6862, 10.3390/en16196862
    160. Mohit Teacher, Rajkumar Velu, Additive Manufacturing of Functionally Graded Materials: A Comprehensive Review, 2024, 25, 2234-7593, 165, 10.1007/s12541-023-00864-x
    161. Yuya Asamoto, Keiichiro Urabe, Takayuki Matsuda, Takashi Hamano, Masao Noma, Michiru Yamashita, Shigehiko Hasegawa, Koji Eriguchi, Study on Ion Flux From Magnetically Confined Low-Pressure Arc Discharge With a Thermionic Cathode to Substrate for High-Throughput Film Deposition Processes, 2024, 52, 0093-3813, 2333, 10.1109/TPS.2024.3417896
    162. Anusha Dinakar Rao, Raghavendra Bairy, Pawan Nayak N, Suresh D Kulkarni, Neelamma Gummagol, Effect of Cr-doping on third-order nonlinear optical properties of nanostructured Zn1-xCrxO thin films for Opto-Electronic device applications, 2024, 130, 0947-8396, 10.1007/s00339-024-07736-9
    163. M. Lablali, H. Mes-adi, M. Mazroui, Effect of deposition rate and annealing on Nb thin film growth on Cu substrate: Molecular dynamics simulation, 2024, 229, 0042207X, 113548, 10.1016/j.vacuum.2024.113548
    164. Anita Ioana Visan, Rodica Cristescu, Polysaccharide-Based Coatings as Drug Delivery Systems, 2023, 15, 1999-4923, 2227, 10.3390/pharmaceutics15092227
    165. Shiyao Gu, Saad Ullah, Firoz Khan, Xiaoxia Wang, Ping Liu, Shi-e Yang, Yongsheng Chen, Recent advances and perspectives on Sb2S3 thin-film solar cells, 2024, 28, 25892347, 101019, 10.1016/j.mtsust.2024.101019
    166. Jyothi Gupta, Habibuddin Shaik, Sheik Abdul Sattar, A review on perspective of spin coating technique towards profound electrochromism of tungsten oxide thin films, 2024, 0973-1458, 10.1007/s12648-024-03199-z
    167. Jessica Willkommen, Amin Bahrami, Nicolas Perez Rodriguez, Angelika Wrzesinska-Lashkova, Yana Vaynzof, Kornelius Nielsch, Sebastian Lehmann, Room Temperature Synthesis of Tellurium by Solution Atomic Layer Deposition, 2024, 24, 1528-7483, 8056, 10.1021/acs.cgd.4c00987
    168. Asif Rasool, Shahnaz Kossar, R. Amiruddin, 2024, Chapter 14, 978-981-99-6648-6, 165, 10.1007/978-981-99-6649-3_14
    169. Saurabh Sharma, Kuldeep Kumar, Naveen Thakur, A comprehensive review on analysis of functionalization techniques and techno-innovative uses of nano-cellulosic materials, 2023, 206, 09266690, 117632, 10.1016/j.indcrop.2023.117632
    170. Abraham Encinas-Terán, Horacio A. Pineda-León, María R. Gómez-Colín, Laura R. Márquez-Alvarez, Ramón Ochoa-Landín, Alejandro Apolinar-Iribe, Sandra L. Gastélum-Acuña, Temístocles Mendívil-Reynoso, Santos J. Castillo, Synthesis and Characterization of a Semiconductor Diodic Bilayer PbS/CdS Made by the Chemical Bath Deposition Technique, 2024, 9, 2470-1343, 24321, 10.1021/acsomega.3c10051
    171. I. I. Vinogradov, N. A. Drozhzhin, L. I. Kravets, A. Rossouw, T. N. Vershinina, A. N. Nechaev, Formation of Hybrid Membranes for Water Desalination by the Method of Membrane Distillation, 2024, 86, 0023-2912, 533, 10.31857/S0023291224050029
    172. Alejandra López-Suárez, Yaser D. Cruz-Delgado, Dwight R. Acosta, Juan López-Patiño, Beatriz E. Fuentes, The Effect of H+ Fluence Irradiation on the Optical, Structural, and Morphological Properties of ZnO Thin Films, 2024, 17, 1996-1944, 6095, 10.3390/ma17246095
    173. Astha Singh, Aakriti Patel, Hema Chaudhary, Kiran Yadav, Neha Minocha, Nanotheranostics: The Fabrication of Theranostics with Nanoparticles and their Application to Treat the Neurological Disorders, 2025, 19, 18722105, 17, 10.2174/1872210517666230718115651
    174. Mohammad Nur‐E‐Alam, Mohammad Tanvirul Ferdaous, Abdullah Alghafis, Mikhail Vasiliev, Boon Kar Yap, Tiong Sieh Kiong, Megat Mohd Izhar Sapeli, Nowshad Amin, Mohd Adib Ibrahim, Md Khan Sobayel Bin Rafiq, Tailoring Ga‐Doped ZnO Thin Film Properties for Enhanced Optoelectric Device Performance: Argon Flow Rate Modulation and Dynamic Sputtering Geometry Analysis, 2024, 2367-198X, 10.1002/solr.202400353
    175. Tahir Iqbal Awan, Sumera Afsheen, Sabah Kausar, 2025, Chapter 1, 978-981-96-1363-2, 1, 10.1007/978-981-96-1364-9_1
    176. N. P. V. Sebbe, F. J. G. Silva, L. M. Durão, A. Jesus, R. C. M. Sales-Contini, Comparative Analysis of the Wear Behavior of TiN/TiAlN-, TiAlVN-, and TiAlYN-Coated Tools in Milling Operations of Inconel 718, 2025, 147, 0742-4787, 10.1115/1.4066954
    177. Melania Suweni Muntini, Nabiha Rassya Islamy Satrio Putri, Mekala Insawang, Sarawoot Boonkirdram, Mati Horprathum, Tosawat Seetawan, Athorn Vora-ud, Thermoelectricity of Iron-Antimony-Titanium Thin Films Fabricated Through DC Magnetron Sputtering, 2024, 0361-5235, 10.1007/s11664-024-11695-5
    178. 2025, 9781119713067, 137, 10.1002/9781119713128.ch3
    179. Siphelo Ngqoloda, Thelma Ngwenya, Mpfunzeni Raphulu, 2025, 10.5772/intechopen.1008691
    180. Jaideep Adhikari, Prerona Saha, Pritam Mandal, Sudip Kumar Sinha, Asiful H. Seikh, Jabair A. Mohammed, Manojit Ghosh, A Review on High Entropy Alloys as Metallic Biomaterials: Fabrication, Properties, Applications, Challenges, and Future Prospects, 2025, 2731-4812, 10.1007/s44174-025-00314-4
    181. Ashok Adhikari, Dwight Roberto Acosta Najarro, José Reyes-Gasga, Enrique Camarillo Garcia, Tommy Kevin Merino Alama, Odín Reyes Vallejo, Francisco Javier Cano, Maria de la Luz Olvera Amador, Preparation and characterization of vanadium-titanium oxide thin films via the evaporation technique followed by the post-annealing treatment, 2025, 340, 02540584, 130644, 10.1016/j.matchemphys.2025.130644
    182. Jiale Chai, Yuanyuan Gao, Kun Zhou, Xiangfei Kong, Exploiting third-generation radiative cooling for energy applications, 2025, 26663864, 102542, 10.1016/j.xcrp.2025.102542
    183. Isha Arora, Rishi Kant, 2025, 9781394287277, 205, 10.1002/9781394287307.ch9
    184. R. Kemparaju, Akila Prabhudesai, S. Charan Prasanth, M. Madesh Kumar, K. Ramesh, Electrical switching and phase change properties of GeTe-Al2Te3 chalcogenide alloys, 2025, 02728842, 10.1016/j.ceramint.2025.04.110
    185. Ksenia B. Kim, Alexander S. Lenshin, Sergei S. Chernenko, Sabukhi Ilich ogly Niftaliev, Andrey I. Chukavin, Examining the morphology and surface composition of a nanostructured tin film on porous silicon, 2024, 91, 1070-9762, 675, 10.1364/JOT.91.000675
    186. H. Al Amouri, S. Shehayeb, L. Ghannam, P. Trens, I. Karame, X. Deschanels, G. Toquer, Solar selective absorbers via electrophoretic deposition: A comparative and critical review of the method, 2025, 46, 23524928, 112621, 10.1016/j.mtcomm.2025.112621
    187. Danielle N. Alverson, Daniel Olds, Megan M. Butala, Distinguishing isotropic and anisotropic signals for X-ray total scattering using machine learning, 2025, 81, 2053-2733, 175, 10.1107/S2053273325002438
    188. Liubov Kravets, Iliya Vinogradov, Arnoux Rossouw, Boris Gorberg, Alexander Nechaev, Pavel Apel, Functionalization of PET track-etched membranes with electrospun PVDF nanofibers for hybrid membranes fabrication in water desalination, 2025, 371, 13835866, 133395, 10.1016/j.seppur.2025.133395
    189. Jing Xu, Kang Li, Hang Yin, Axial compression–induced post-buckling of nanotube films on copper nanopillars: a molecular dynamics study, 2025, 31, 1610-2940, 10.1007/s00894-025-06377-w
    190. Liubov I. Kravets, Maxim A. Yarmolenko, A. V. Rogachev, Radmir V. Gainutdinov, M. A. Kuvaitseva, Vladimir A. Altynov, Nikolay E. Lizunov, ANALYSIS OF LONG-TERM HYDROPHOBIC PROPERTIES STABILITY OF THE TEXTURED POLYMER COATINGS PRODUCED VIA ELECTRON-BEAM DEPOSITION OF POLYMERS ON THE TRACK-ETCHED MEMBRANE SURFACE , 2025, 29, 1093-3611, 57, 10.1615/HighTempMatProc.2025057717
    191. Saki Murotani, Sakura Uehara, Jianbo Liang, Eiji Shikoh, Yoshihisa Kaneko, Naoteru Shigekawa, Fabrication and electrical characterization of thick-metal-film coplanar waveguides on silicon oxide films by directly bonding Al foils, 2025, 64, 0021-4922, 05SP21, 10.35848/1347-4065/add167
    192. Daniela Santo, José D. Castro, Sandra Cruz, Isabel Carvalho, Albano Cavaleiro, Sandra Carvalho, Customisation of PVD coatings for biomedical devices, 2025, 02578972, 132277, 10.1016/j.surfcoat.2025.132277
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    194. C. Durga Prasad, H. R. Manjunath, Mahantesh S. Matur, H. B. Shivaprasad, C. Solaimuthu, M. Haridass, Shrishail B. Sollapur, Saravana Bavan, T. A. Sudarshan, Investigation of Microstructural and Hot Corrosion Behaviour of CoMoCrSi/WC–12Co Microwave Cladding on Titanium Substrate, 2025, 11, 2198-4220, 10.1007/s40735-025-00997-8
    195. Yawen Yang, Hexi Li, Dandan Liu, Wei Hu, Ruixue Wang, Zhihao Yi, Anna Zhu, A critical review on integrated fabric-based functionalized composites for protection and decontamination of chemical and biological warfare agents, 2025, 543, 00108545, 216905, 10.1016/j.ccr.2025.216905
    196. A. S. Mokrushin, S. A. Dmitrieva, Y. M. Gorban, A. R. Stroikova, N. P. Simonenko, A. A. Averin, E. P. Simonenko, AACVD Synthesis of Bilayer Thin-Film ZnO/Cr2O3 Nanocomposites for Chemoresistive Gas Sensors, 2025, 70, 0036-0236, 624, 10.1134/S0036023624603763
    197. A. Ashok, D. Acosta, M. De la L. Olvera, A. Maldonado, Sustainable synthesis and analysis of MO3 (M=Mo, W) nanoparticles obtained from the thermo-mechanical process for CO gas sensing applications, 2025, 02728842, 10.1016/j.ceramint.2025.06.386
    198. Anthunes Íkaro de Araújo, Igor Oliveira Nascimento, Michelle Cequeira Feitor, Maxwell Santana Libório, Álvaro Albueno da Silva Linhares, Pâmala Samara Vieira, Salete Martins Alves, Rômulo Ribeiro Magalhães de Sousa, Cleânio da Luz Lima, Ediones Maciel de Sousa, Thercio Henrique de Carvalho Costa, A Novel Technology to Deposition Diamond-Like Carbon Thin Films: Cathodic Cylinder Plasma Deposition, 2025, 1047-4838, 10.1007/s11837-025-07572-z
    199. Kamlendra Vikram, Sumit Pramanik, Shubrajit Bhaumik, 2025, 9780443298929, 37, 10.1016/B978-0-443-29892-9.00002-2
    200. Anita Ioana Visan, Irina Negut, Polymeric Composite Thin Films Deposited by Laser Techniques for Antimicrobial Applications—A Short Overview, 2025, 17, 2073-4360, 2020, 10.3390/polym17152020
    201. Eugene Bortchagovsky, Alla Bogoslovska, Dmytro Grynko, Oleksandr Selyshchev, Dietrich R.T. Zahn, Continuous ultrathin layers of ZnS produced by the successive ionic layer adsorption and reaction technique, 2025, 00406090, 140754, 10.1016/j.tsf.2025.140754
    202. Hao Du, Ke Zhang, Debin Liu, Wenchang Lang, Progress in the Circular Arc Source Structure and Magnetic Field Arc Control Technology for Arc Ion Plating, 2025, 18, 1996-1944, 3498, 10.3390/ma18153498
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