Figure 1.
The acidity of fresh-cut mangosteen during cold storage.
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
| [1] | Luh Suriati, I Made Supartha Utama, Bambang Admadi Harsojuwono, Ida Bagus Wayan Gunam . Incorporating additives for stability of Aloe gel potentially as an edible coating. AIMS Agriculture and Food, 2020, 5(3): 327-336. doi: 10.3934/agrfood.2020.3.327 |
| [2] | Nafi Ananda Utama, Yulianti, Putrika Citta Pramesi . The effects of alginate-based edible coating enriched with green grass jelly and vanilla essential oils for controlling bacterial growth and shelf life of water apples. AIMS Agriculture and Food, 2020, 5(4): 756-768. doi: 10.3934/agrfood.2020.4.756 |
| [3] | Ilenia Tinebra, Roberta Passafiume, Alessandra Culmone, Eristanna Palazzolo, Giuliana Garofalo, Vincenzo Naselli, Antonio Alfonzo, Raimondo Gaglio, Vittorio Farina . Boosting post-harvest quality of 'Coscia' pears: Antioxidant-enriched coating and MAP storage. AIMS Agriculture and Food, 2024, 9(4): 1151-1172. doi: 10.3934/agrfood.2024060 |
| [4] | Hayriye Fatma Kibar, Ferhan K. Sabir . Chitosan coating for extending postharvest quality of tomatoes (Lycopersicon esculentum Mill.) maintained at different storage temperatures. AIMS Agriculture and Food, 2018, 3(2): 97-108. doi: 10.3934/agrfood.2018.2.97 |
| [5] | Valentina M. Merlino, Danielle Borra, Aurora Bargetto, Simone Blanc, Stefano Massaglia . Innovation towards sustainable fresh-cut salad production: Are Italian consumers receptive?. AIMS Agriculture and Food, 2020, 5(3): 365-386. doi: 10.3934/agrfood.2020.3.365 |
| [6] | Thi-Van Nguyen, Tom Ross, Hoang Van Chuyen . Evaluating the efficacy of three sanitizing agents for extending the shelf life of fresh-cut baby spinach: food safety and quality aspects. AIMS Agriculture and Food, 2019, 4(2): 320-339. doi: 10.3934/agrfood.2019.2.320 |
| [7] | Jeffrey A. Clark, Hillary E. Norwood, Jack A. Neal, Sujata A. Sirsat . Quantification of pathogen cross-contamination during fresh and fresh-cut produce handling in a simulated foodservice environment. AIMS Agriculture and Food, 2018, 3(4): 467-480. doi: 10.3934/agrfood.2018.4.467 |
| [8] | Alaika Kassim, Tilahun S. Workneh, Mark D. Laing . A review of the postharvest characteristics and pre-packaging treatments of citrus fruit. AIMS Agriculture and Food, 2020, 5(3): 337-364. doi: 10.3934/agrfood.2020.3.337 |
| [9] | Soukaina Ouansafi, Fahde Abdelilah, Mostafa Kabine, Hind Maaghloud, Fatima Bellali, Karima El Bouqdaoui . The effects of soil proprieties on the yield and the growth of tomato plants and fruits irrigated by treated wastewater. AIMS Agriculture and Food, 2019, 4(4): 921-938. doi: 10.3934/agrfood.2019.4.921 |
| [10] | Luana Muniz de Oliveira, Ágda Malany Forte de Oliveira, Railene Hérica Carlos Rocha Araújo, George Alves Dias, Albert Einstein Mathias de Medeiros Teodósio, José Franciraldo de Lima, Luana da Silva Barbosa, Wellinghton Alves Guedes . Spirulina platensis coating for the conservation of pomegranate. AIMS Agriculture and Food, 2020, 5(1): 76-85. doi: 10.3934/agrfood.2020.1.76 |
Mangosteen is a tropical fruit that is currently popular. The mangosteen fruit has a delicious taste and contains vitamins, minerals, and antioxidants that are beneficial for health [1,2]. Mangosteen is perishable. Although edible parts are still suitable for consumption, damage to nonedible parts, such as skin, determines consumer preferences. The number of nonedible parts of the mangosteen fruit (around 63%–75%) is relatively high and contributes to household waste [3,4], causing a growth in the sales of edible parts, i.e., fresh-cut fruits. The fresh-cut selection is also driven by consumer demand for quality products and a lack of preparation time [5,6,7].
Fresh cuts are products with minimal processing steps to get maximum quality. Processing includes stripping, cutting, slicing, pith removal, washing, and packaging [8]. Some of the advantages of minimally processed products include providing consumers with a variety of choices in one package, enabling consumers to get the required fresh quantity, easy assessment of quality, and reducing the volume and transport costs [4]. Fresh-cut fruit has the disadvantages of perishability and shorter shelf-life than the whole fruit [5,9]. Tissue injury causes the fruit to undergo physicochemical changes, which induce deterioration [10,11].
According to [5] and [12], the application of 1% CaCl2 combined with cold storage enhances the firmness of fresh-cut and prevents browning. The application of the edible coating helps maintain the freshness of fresh-cut products [13], as a barrier against mass transfer and gas exchange [14]. According to [15], edible coatings improve appearance (bright and shiny colors), retain moisture, prevent weight loss and protect against microorganisms. However, there has been no previous research on the application of the edible coating on fresh-cut mangosteen. Therefore, it is important to study and know the coating method and extend shelf life.
Aloe vera gel has potential as an edible coating (ecogel) because it consists of polysaccharides containing more than 75 functional chemical compounds, such as saponins, sterols, acemannan, vitamins, and folic acid [16]. The advantages of using ecogel are biodegradability, permeable oxygen, antioxidant activity, low toxicity, low cost, and ease of application [17]. The concentration of additives determines the consistency of the ecogel. The optimal concentration of citric acid, ascorbic acid, and potassium sorbate additives is 0.15% [18]. The obstacle in applying ecogel to fresh-cut fruit is the difficulty of adhesion on the surface of hydrophilic fruit slices [5].
The adhesion ability of the ecogel is influenced by the structure, size, and chemical constituents. The small size of the particle improves solubility, absorption of active compounds, and controlled release. The nano-ecogel is one of the applications of nanotechnology in the postharvest handling of fresh-cut fruit. There are many reports of aloe vera for coating fruits and vegetables, but the application of nano-ecogel is a new study. The advantages obtained from the use of nano-ecogel include a barrier, mechanical properties, emulsion system, and bioavailability [19]. The ecogel application is influenced by composition, time, method, and layer thickness. The use of nano-ecogel is an effort to maintain the physicochemical change in fresh-cut mangosteen [19,20]. However, to the best of the authors' knowledge, no information is available on the concentration of nano-ecogel and the best immersion time of fresh-cut mangosteen. Therefore, research is needed to determine the concentration of nano-ecogel and immersion time to maintain the physicochemical characteristics of fresh-cut mangosteen.
Preparation of nano-ecogel using the method invented by [18]. The first step of ecogel production is sorting 1-year-old aloe leaves (Aloe barbadense. Miller). Leaves were left for 24 h at room temperature to remove yellow mucus. Aloe leaves were washed with water to remove the yellow mucus residue and unpleasant odors that could reduce the quality of the gel. Tripping and filleting were to produce gel fillets by using a stainless knife. Gel filets were homogenized for 5 min and heated at 70 ± 1 ℃ for 5 min [21]. The gel was cooled for 1 h at 27 ℃ and filtered with the Rocker 300 vacuum pump, 5340FK1000R flash filter, and Whatman filter paper no. 42. Aloe gel was added with a mixture of citric acid, ascorbic acid, and potassium sorbate with concentrations of 0.15% (w/v). The agitation process used the sonicate masonic Q125 to obtain the nanostructures, with a 59-time delay pulse of 30 seconds for 50 min. The size of ecogel nanoparticles was determined using the UV–vis spectrophotometer. The maximum absorbance indicated a particle size of 20–110 nm [22].
Fresh and ripe mangosteen fruits aged 105 days since flowering were collected from a garden in Panji Village, Sukasada District, Buleleng Regency, Bali Province, Indonesia. The criteria of mangosteen fruit included greenish-yellow skin color with 50% pink spots spreading on the skin, round like a compressed ball, flesh consisting of 5–8 segments, fresh green petals, and fruit weight of 130–180 g. The mangosteen fruit was precooled by washing with water and stored in a clean tissue paper to drain excess water. The mangosteen fruit was peeled carefully to obtain a fruit without skin (fresh-cut fruit) and left with fused segments.
Peeled fresh-cut mangosteen was first dipped into 1% CaCl2 solution for 10 min and dried using a blower for 20 min. Fresh-cut mangosteen was applied with 100%, 75%, 50% and 25% nano-ecogel. A concentration of 100% nano-ecogel meant pure nano-ecogel, whereas 75% concentration indicated 75 mL nano-ecogel and 25 ml water. The immersion time of fresh-cut mangosteen in the nano-ecogel was 1, 2 and 3 min. This study was repeated three times. Fresh-cut fruits coated with nano-ecogel was drained and dried using a blower for 20 min. Furthermore, fresh-cut mangosteen was packaged in a 10 cm × 20 cm × 5 cm plastic box equipped with two holes with a diameter of 0.5 cm on the lid and stored at a cold temperature (7 ± 1 ℃). During storage for 3, 6 and 9 days, acidity [30], vitamin C [31], water content [34], total dissolved solids (TDS) [30], weight loss [23], texture [32], and browning index [33] were evaluated.
This study used a completely randomized design factorial pattern. Statistical analysis was performed using SPSS to measure the variance of all observed variables through analysis of variance. The significant value obtained using Duncan, p < 0.05 shows a noticeable difference.
Immature fruits contain some organic acids, which tend to degrade during ripening. A decrease in acidity changes the acidity of the fruit. The acidity of fresh-cut mangosteen after nano-ecogel application on day 3 is on average higher than before application which is 3.06. A high concentration of nano-ecogel results in an increased ability to cover the surface pores of the fruit, thereby inhibiting the process of converting sugar into organic acids [35]. The taste of fruits is mostly influenced by the contents of sugar, organic acids, phenolics, and volatile compounds.
High nano-ecogel concentrations caused the fresh-cut surface to close, thus delaying the conversion of sugar into organic acids. In line with the results of the study [35], that the application of nanoparticles chitosan inhibits the conversion of starch to sugar and sugar to organic acid, due to the ability of this coating as a barrier in the surface of fresh-cut. The nanostructured edible coating on minimally processed foods effectively controlled moisture loss and retained the color and extend shelf-life of apple slices [36]. Following the opinion of [23], aloe vera gel contains many functional components, and antimicrobials and antioxidants can inhibit postharvest damage.
Fresh-cut mangosteen stored for nine days and treated with 50% nano-ecogel has the highest vitamin C content. Figure 2 shows that the fresh-cut mangosteen fruit on day 3 was treated with 50% nano-ecogel, the highest vitamin C content (2.79 mg/100 g), 25% ecogel the lowest vitamin C content (2.27 mg/100 g). This means 50% is the most ideal concentration of nano-ecogel coating solution to cover the pores of the fresh-cut surface so that the vitamin C oxidation process can be avoided. The vitamin C content of fresh-cut mangosteen on days 6 and 9 ranges from 1.68 mg/100 g to 2.22 mg/100 g and from 1.55 mg/100 g to 1.89 mg/100 g, respectively. The mangosteen fruit contains several important nutrients, including xanthones and vitamin C [24,25], and their amounts are remarkably influenced by many factors, e. g. variety, environment, and maturity. Vitamin C levels in fresh-cut mangosteen are relatively stable, indicating that the application of nano-ecogel can maintain the vitamin C levels of fresh-cut mangosteen. The loss of vitamin C in the material is due to the oxidation process [26]. Aloe vera gel has antioxidant abilities that can inhibit postharvest damage [27].
The decrease in the water content of fresh-cut mangosteen is unavoidable. Mangosteen is a climacteric fruit that still undergoes respiration, i. e. carbohydrates are broken down into simple sugars, water, and energy [1]. Increasing the concentration of nano-ecogel can suppress water loss. A previous study [5] showed that the application of edible coating retains water and results in bright and shiny colors. Edible coatings on the fruit surface tissue aim to modify the environment, inhibit gas transfer, reduce water and aroma loss, change color and improve the appearance [28]. Fresh-cut mangosteen has the highest water content on the ninth day by a nano-ecogel concentration of 100% for 3 minutes, and the lowest on 25% nano-ecogel for 3 minutes. Water loss can be suppressed by increasing the concentration of nano-ecogel. [28] stated that edible coating on the surface of fresh-cut fruit aims to modify the atmosphere, inhibit gas transfer, lose water and aroma, delay color change, and improve appearance. Aloe vera gel consists of polysaccharides glucomannan and acemannan which have potential as edible coatings on fruits [18]
Table 1 shows no significant result in terms of different days at various treatments. The moisture contents of fresh-cut mangosteen fruit are 80.43%–84.45%, 80.82%–83.63%, and 80.47−87.10% on days 3, 6, and 9, respectively. The high concentration of nano-ecogel delays the loss of water of fresh-cut mangosteen. Aloe vera gel consists of glucomannan and acemannan polysaccharides, which have the potential as edible coatings and prevent water loss in fruits [27].
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 81.45 | 82.91 | 82.35 | |
| 100% | 1 | 82.73 b | 81.57 f | 81.93 g |
| 75% | 1 | 82.16 g | 81.10 i | 80.47 i |
| 50% | 1 | 81.72 i | 81.32 h | 82.02 f |
| 25% | 1 | 81.96 h | 81.73 e | 81.95 g |
| 100% | 2 | 84.45 a | 83.63 a | 85.15 b |
| 75% | 2 | 82.64 c | 81.80 d | 83.33 c |
| 50% | 2 | 82.33 f | 82.46 c | 81.15 h |
| 25% | 2 | 81.54 j | 81.57 f | 82.30 e |
| 100% | 3 | 82.46 d | 83.40 b | 87.10 a |
| 75% | 3 | 80.43 e | 81.60 f | 83.62 c |
| 50% | 3 | 82.64 c | 79.50 g | 82.41 d |
| 25% | 3 | 81.12 k | 80.82 i | 79.98 j |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
The application of nano-ecogel at a high concentration on day 3 leads to increased TDS of fresh-cut mangosteen because mangosteen is a climacteric fruit and still ripens during storage. Several types of sugar glucose, fructose, and sucrose in climacteric fruits, such as mangosteen, tend to increase during cell maturation [29]. The nano-ecogel concentration of 50% can maintain the TDS of fresh-cut mangosteen fruit on days 6 and 9. Table 2 shows that the highest total soluble solids of fresh-cut mangosteen fruit (24.82 °Brix) is obtained at immersion in 50% ecogel for 3 min. The nano-ecogel concentration of 50% produces a solution that is not too thick and also does not dilute. In line with the opinion [13] that a good coating solution is non-sticky and easily dry. TDS remain stable because the application of nanoparticles inhibits the conversion of sugar to organic acid, due to the ability as a barrier in the surface of fresh-cut [35]. The lowest TDS is 23.42 °Brix and observed at immersion in 25% ecogel for 1 min. Fresh-cut mangosteen fruit on day 6, a TDS value between 22.22 °Brix and 23.82 °Brix. On the ninth day of storage, fresh-cut mangosteen immersed at 50% ecogel for 3 min has the highest TDS (24.02 °Brix), and that immersed at 100% ecogel for 2 min has the lowest TDS (20.02 °Brix). The application of ecogel on the fruit surface has the advantage of several active ingredients that can be inserted into the polymer matrix for the maintenance of freshness and sensory attributes [30]. Results from a previous study [17], showed that aloe vera gel can be used to extend shelf life and maintain freshness at cold temperatures.
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 23.50 | 22.70 | 22.60 | |
| 100% | 1 | 23.62 de | 22.32 d | 22.02 c |
| 75% | 1 | 24.12 cd | 23.12 b | 21.42 f |
| 50% | 1 | 24.12 cd | 23.12 b | 21.92 cd |
| 25% | 1 | 23.42 e | 22.42 cd | 21.72 e |
| 100% | 2 | 23.82 de | 22.22 e | 20.02 h |
| 75% | 2 | 24.82 a | 22.22 e | 21.82 de |
| 50% | 2 | 23.52 e | 21.32 d | 20.72 g |
| 25% | 2 | 23.82 de | 22.72 c | 21.82 de |
| 100% | 3 | 24.52 ab | 23.82 a | 21.82 de |
| 75% | 3 | 24.22 bc | 22.52 cd | 22.32 b |
| 50% | 3 | 24.62 ab | 23.82 a | 24.02 a |
| 25% | 3 | 24.32 bc | 22.42 cd | 21.82 de |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
A high concentration of nano-ecogel and long immersion on days 3, 6, and 9 results in a high possibility of closing the pores of the fresh-cut mangosteen surface, thereby suppressing transpiration and decreasing weight loss. Following the opinion of [31], edible coatings can retain moisture and prevent weight loss. The highest fresh-cut mangosteen weight loss at immersion in 25% nano-ecogel for 3 min is significantly different from those at other treatments. The lowest weight loss is observed at immersion in 100% nano-ecogel for 3 min. Figure 3 shows that the highest weight loss of fresh-cut mangosteen 3.83% (FW) is obtained at immersion in 25% ecogel for 3 min and that the lowest weight loss of fresh-cut mangosteen 0.51% (FW) is observed at immersion in 100% ecogel for 3 min. The fresh-cut mangosteen fruits on days 6 and 9 have weight loss values of 0.52%–6.54% and 0.52%–6.54% (FW), respectively. Aloe vera gel, as a protector against physical and chemical biological changes, is reported to form a thin layer, improve appearance, and retain moisture [17]. The weight loss of fresh-cut mangosteen increases until the end of storage, which is day 9. Given that fresh-cut mangosteen has a climacteric pattern, the respiration rate still increases during storage [4]. Fresh-cut mangosteen after the nano-ecogel application shows a lower weight loss than that before the nano-ecogel application.
The texture of fresh-cut mangosteen was measured using a texture analyzer at a speed: distance of 10:8. Texture changes during the storage period of fresh-cut mangosteen occur due to the ripening process, and the fruit that is stored for a long time softens because of the influence of pectolytic enzymes. The highest texture value of fresh-cut mangosteen until day 9 is obtained at immersion in 50% nano-ecogel for 1 min. The lowest texture is obtained at immersion in 25% nano-ecogel for 1 min. Table 3 shows that the texture values of fresh-cut mangosteen on days 3 and 6 are 1.58–3.56 and 1.51–3.07 N/m, respectively. The highest texture of fresh-cut mangosteen on day 9 (2.89 N/m) is obtained at immersion in 50% ecogel for 1 min. The lowest texture of 1.38 N/m is obtained at immersion in 25% ecogel for 1 min. This result shows that immersion in 50% nano-ecogel for 1 min can maintain the fresh-cut texture of mangosteen. [2] stated that fruit texture decreases during storage. The activity of pectinase during storage automatically causes loss of rigidity in the fruit tissue [14]. The nano-ecogel interacts with pectin polymers to form crosslinking networks that increase mechanical strength, which delays senescence and controls physiological damage of fresh-cut mangosteen.
| Concentration of Ecogel |
Immersion time (minutes) |
Day | ||
| 3 | 6 | 9 | ||
| Control | 1.20 | 0.83 | 0.60 | |
| 100% | 1 | 3.01 a | 2.76 a | 2.65 ab |
| 75% | 1 | 2.44 a | 2.15 a | 1.66 cd |
| 50% | 1 | 3.08 a | 3.00 a | 2.89 a |
| 25% | 1 | 3.25 a | 3.07 a | 1.38 d |
| 100% | 2 | 3.56 a | 1.94 a | 1.83 cd |
| 75% | 2 | 2.49 a | 2.80 a | 2.79 a |
| 50% | 2 | 2.53 a | 1.95 a | 2.19 cd |
| 25% | 2 | 1.59 a | 1.88 a | 1.86 cd |
| 100% | 3 | 2.15 a | 1.51 a | 1.42 d |
| 75% | 3 | 2.60 a | 2.78 a | 2.36 bc |
| 50% | 3 | 1.84 a | 1.62 a | 1.77 cd |
| 25% | 3 | 1.58 a | 1.70 a | 1.78 cd |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
The lowest browning index of fresh-cut mangosteen on day 3 of 1.99 is observed at immersion in 100% nano-ecogel for 3 min. Figure 4 shows that the highest browning index of fresh-cut mangosteen on day 3 is 8.18, which is obtained at immersion in 25% ecogel for 3 min. The highest browning index on day 6 ranges from 1.01 to 8.34. Observations on day 9 show that the highest browning index is 32.62 and observed at immersion in 100% ecogel for 3 min and that the lowest browning index is 9.88 and observed at immersion in 50% ecogel for 1 min. This result indicates that increasing the concentration of nano-ecogel at the same immersion time results in reduced browning of fresh-cut mangosteen. Nano-ecogel at the right concentration and immersion time will produce a layer that can cover the fresh-cut surface perfectly and contact with oxygen was avoided. Thus, the browning reaction can be prevented. If the fresh-cut surface is tightly closed, the addition of immersion has no effect. [28] stated that edible coating on the surface of fresh-cut fruit aims to modify the atmosphere, inhibit gas transfer, delay color change, and improve appearance.
The enzymatic oxidation of monophenols produces o-diphenols, which are converted into quinones. Nonenzymatic polymerization forms the brown or melanin color [9]. The ability of nano-ecogel as an antioxidant can inhibit the oxidation process of phenol compounds and postharvest damage [27]. Day 6 also shows the same results as day 3, the immersion of fresh-cut mangosteen in 50% nano-ecogel for 1 min has provided a low browning index of 4.87 than control of 8.30. On day 9, the treatment of 50% nano-ecogel for 1 min has provided a low browning index of 27.83 than control 29.10. Several researchers applied aloe vera gel with concentrations ranging from 50% to 100% as an edible coating to preserve whole fruits, such as table grapes [32], mango [33,37], blueberries [34], and apricot [35,38].
The effects of nano-ecogel concentration, immersion time, and their interaction on the degree of acidity were investigated. In addition, the water content, TDS, weight loss, and browning index of fresh-cut mangosteen were studied. In conclusion, immersion in 50% nano-ecogel for 1 min maintained the freshness of fresh-cut mangosteen. Compared with the initial fruit, the fresh-cut mangosteen after nano-ecogel application was more attractive, whiter, juicy, and shiny until the ninth day of storage.
The author would like to thank the rector of the University of Warmadewa and the chairman of the KORPRI Welfare Foundation for their support in this research and all colleagues who helped with this project.
| [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
|
| 1. | Nabeela Haneef, Yvan Garièpy, Vijaya Raghavan, Jiby Kudakasseril Kurian, Najma Hanif, Tahira Hanif, Effects of Aloe-pectin coatings and osmotic dehydration on storage stability of mango slices, 2022, 25, 1981-6723, 10.1590/1981-6723.02822 | |
| 2. | Luh Suriati, I. Made Supartha Utama, Bambang Admadi Harsojuwono, Ida Bagus Wayan Gunam, Effect of Additives on Surface Tension, Viscosity, Transparency and Morphology Structure of Aloe vera Gel-Based Coating, 2022, 6, 2571-581X, 10.3389/fsufs.2022.831671 | |
| 3. | Luh Suriati, Nano Coating of Aloe-Gel Incorporation Additives to Maintain the Quality of Freshly Cut Fruits, 2022, 6, 2571-581X, 10.3389/fsufs.2022.914254 | |
| 4. | A. Soltani, K. Benfreha, K. Hamraoui, Analysis of Physico-chemical Properties, and Antimicrobial Activity of Aloe vera (Aloe barbadensis Miller), 2022, 1624-8597, 10.3166/phyto-2022-0349 | |
| 5. | Luh Suriati, Nanocoating-konjac application as postharvest handling to extend the shelf life of Siamese oranges, 2023, 7, 2571-581X, 10.3389/fsufs.2023.1104498 | |
| 6. | Luh Suriati, Ni Made Ayu Suardani Singapurwa, Aida Firdaus Muhamad Nurul Azmi, Rovina Kobun, I Wayan Widiantara Putra, Putu Ajus Raditya Putra, I.B.W. Gunam, N.S. Antara, A.K. Anal, P.J. Batt, T. Sone, I N.K. Putra, G.P.G. Putra, P. Hariyadi, A.B. Sitanggang, K.A. Nocianitri, I D.G.M. Permana, I W.R. Widarta, N.N. Puspawati, I.B.A. Yogeswara, I D.P.K. Pratiwa, The Effect of Porang Coating Application and Storage Time on The Characteristics of Kintamani Siamese Oranges, 2024, 98, 2117-4458, 06011, 10.1051/bioconf/20249806011 | |
| 7. | Luh Suriati, I Gede Pasek Mangku, Luh Kade Datrini, Hanilyn A. Hidalgo, Josephine Red, Serviana Wunda, Anak Agung Sagung Manik Cindrawat, Ni Luh Putu Sulis Dewi Damayanti, The effect of maltodextrin and drying temperature on the characteristics of Aloe-bignay instant drink, 2023, 3, 27725022, 100359, 10.1016/j.afres.2023.100359 |
Figures(5)
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
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 81.45 | 82.91 | 82.35 | |
| 100% | 1 | 82.73 b | 81.57 f | 81.93 g |
| 75% | 1 | 82.16 g | 81.10 i | 80.47 i |
| 50% | 1 | 81.72 i | 81.32 h | 82.02 f |
| 25% | 1 | 81.96 h | 81.73 e | 81.95 g |
| 100% | 2 | 84.45 a | 83.63 a | 85.15 b |
| 75% | 2 | 82.64 c | 81.80 d | 83.33 c |
| 50% | 2 | 82.33 f | 82.46 c | 81.15 h |
| 25% | 2 | 81.54 j | 81.57 f | 82.30 e |
| 100% | 3 | 82.46 d | 83.40 b | 87.10 a |
| 75% | 3 | 80.43 e | 81.60 f | 83.62 c |
| 50% | 3 | 82.64 c | 79.50 g | 82.41 d |
| 25% | 3 | 81.12 k | 80.82 i | 79.98 j |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 23.50 | 22.70 | 22.60 | |
| 100% | 1 | 23.62 de | 22.32 d | 22.02 c |
| 75% | 1 | 24.12 cd | 23.12 b | 21.42 f |
| 50% | 1 | 24.12 cd | 23.12 b | 21.92 cd |
| 25% | 1 | 23.42 e | 22.42 cd | 21.72 e |
| 100% | 2 | 23.82 de | 22.22 e | 20.02 h |
| 75% | 2 | 24.82 a | 22.22 e | 21.82 de |
| 50% | 2 | 23.52 e | 21.32 d | 20.72 g |
| 25% | 2 | 23.82 de | 22.72 c | 21.82 de |
| 100% | 3 | 24.52 ab | 23.82 a | 21.82 de |
| 75% | 3 | 24.22 bc | 22.52 cd | 22.32 b |
| 50% | 3 | 24.62 ab | 23.82 a | 24.02 a |
| 25% | 3 | 24.32 bc | 22.42 cd | 21.82 de |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
| Concentration of Ecogel |
Immersion time (minutes) |
Day | ||
| 3 | 6 | 9 | ||
| Control | 1.20 | 0.83 | 0.60 | |
| 100% | 1 | 3.01 a | 2.76 a | 2.65 ab |
| 75% | 1 | 2.44 a | 2.15 a | 1.66 cd |
| 50% | 1 | 3.08 a | 3.00 a | 2.89 a |
| 25% | 1 | 3.25 a | 3.07 a | 1.38 d |
| 100% | 2 | 3.56 a | 1.94 a | 1.83 cd |
| 75% | 2 | 2.49 a | 2.80 a | 2.79 a |
| 50% | 2 | 2.53 a | 1.95 a | 2.19 cd |
| 25% | 2 | 1.59 a | 1.88 a | 1.86 cd |
| 100% | 3 | 2.15 a | 1.51 a | 1.42 d |
| 75% | 3 | 2.60 a | 2.78 a | 2.36 bc |
| 50% | 3 | 1.84 a | 1.62 a | 1.77 cd |
| 25% | 3 | 1.58 a | 1.70 a | 1.78 cd |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
DownLoad:
CSV
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 81.45 | 82.91 | 82.35 | |
| 100% | 1 | 82.73 b | 81.57 f | 81.93 g |
| 75% | 1 | 82.16 g | 81.10 i | 80.47 i |
| 50% | 1 | 81.72 i | 81.32 h | 82.02 f |
| 25% | 1 | 81.96 h | 81.73 e | 81.95 g |
| 100% | 2 | 84.45 a | 83.63 a | 85.15 b |
| 75% | 2 | 82.64 c | 81.80 d | 83.33 c |
| 50% | 2 | 82.33 f | 82.46 c | 81.15 h |
| 25% | 2 | 81.54 j | 81.57 f | 82.30 e |
| 100% | 3 | 82.46 d | 83.40 b | 87.10 a |
| 75% | 3 | 80.43 e | 81.60 f | 83.62 c |
| 50% | 3 | 82.64 c | 79.50 g | 82.41 d |
| 25% | 3 | 81.12 k | 80.82 i | 79.98 j |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
| Concentration of Ecogel | Immersion time (minutes) | Day | ||
| 3 | 6 | 9 | ||
| Control | 23.50 | 22.70 | 22.60 | |
| 100% | 1 | 23.62 de | 22.32 d | 22.02 c |
| 75% | 1 | 24.12 cd | 23.12 b | 21.42 f |
| 50% | 1 | 24.12 cd | 23.12 b | 21.92 cd |
| 25% | 1 | 23.42 e | 22.42 cd | 21.72 e |
| 100% | 2 | 23.82 de | 22.22 e | 20.02 h |
| 75% | 2 | 24.82 a | 22.22 e | 21.82 de |
| 50% | 2 | 23.52 e | 21.32 d | 20.72 g |
| 25% | 2 | 23.82 de | 22.72 c | 21.82 de |
| 100% | 3 | 24.52 ab | 23.82 a | 21.82 de |
| 75% | 3 | 24.22 bc | 22.52 cd | 22.32 b |
| 50% | 3 | 24.62 ab | 23.82 a | 24.02 a |
| 25% | 3 | 24.32 bc | 22.42 cd | 21.82 de |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
| Concentration of Ecogel |
Immersion time (minutes) |
Day | ||
| 3 | 6 | 9 | ||
| Control | 1.20 | 0.83 | 0.60 | |
| 100% | 1 | 3.01 a | 2.76 a | 2.65 ab |
| 75% | 1 | 2.44 a | 2.15 a | 1.66 cd |
| 50% | 1 | 3.08 a | 3.00 a | 2.89 a |
| 25% | 1 | 3.25 a | 3.07 a | 1.38 d |
| 100% | 2 | 3.56 a | 1.94 a | 1.83 cd |
| 75% | 2 | 2.49 a | 2.80 a | 2.79 a |
| 50% | 2 | 2.53 a | 1.95 a | 2.19 cd |
| 25% | 2 | 1.59 a | 1.88 a | 1.86 cd |
| 100% | 3 | 2.15 a | 1.51 a | 1.42 d |
| 75% | 3 | 2.60 a | 2.78 a | 2.36 bc |
| 50% | 3 | 1.84 a | 1.62 a | 1.77 cd |
| 25% | 3 | 1.58 a | 1.70 a | 1.78 cd |
| Note: Different letters behind the average value in the same column showed a significant difference with Duncan's test 5% | ||||
