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In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
Open accessAbstract
A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter cotranslationally in the ER lumen, which contains resident molecular chaperones and folding factors that assist their maturation. Native proteins are released from the ER lumen and are transported through the secretory pathway to their final intra- or extracellular destination. Folding-defective polypeptides are exported across the ER membrane into the cytosol and destroyed. Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099
Hammond, C., Braakman, I., & Helenius, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.913 · Cited by 841
Progressive disruption of cellular protein folding in models of polyglutamine diseases
Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643
The frequency of errors in protein biosynthesis
Loftfield, R. B., & Vanderjagt, D. (1972) · Biochemical Journal · doi:10.1042/bj1281353 · Cited by 399
Jakob, C. A., Burda, P., Roth, J., & Aebi, M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.5.1223 · Cited by 338
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Mechanisms, regulation and functions of the unfolded protein response
Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications
Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Yin, J., Huang, L., Wu, L., Li, J., James, T. D., & Lin, W. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00645b · Cited by 549
Amm, I., Sommer, T., & Wolf, D. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493
Structural and Mechanistic Insights into STIM1-Mediated Initiation of Store-Operated Calcium Entry
Stathopulos, P. B., Zheng, L., Li, G.-Y., Plevin, M. J., & Ikura, M. (2008) · Cell · doi:10.1016/j.cell.2008.08.006 · Cited by 469
Peripheral Protein Quality Control Removes Unfolded CFTR from the Plasma Membrane
Okiyoneda, T., Barrière, H., Bagdány, M., Rabeh, W. M., Du, K., Höhfeld, J., Young, J. C., & Lukacs, G. L. (2010) · Science · doi:10.1126/science.1191542 · Cited by 408
ER and aging—Protein folding and the ER stress response
Naidoo, N. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.001 · Cited by 280
Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation
Quan, E. M., Kamiya, Y., Kamiya, D., Denic, V., Weibezahn, J., Kato, K., & Weissman, J. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.017 · Cited by 242
Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology
Di Jeso, B., & Arvan, P. (2016) · Endocrine Reviews · doi:10.1210/er.2015-1090 · Cited by 184
Chen, Y.-A., Peng, Y.-J., Hu, M.-C., Huang, J.-J., Chien, Y.-C., Wu, J.-T., Chen, T.-Y., & Tang, C.-Y. (2015) · Scientific Reports · doi:10.1038/srep10667 · Cited by 61
The Role of the Hypoxia-Related Unfolded Protein Response (UPR) in the Tumor Microenvironment
Bartoszewska, S., Collawn, J. F., & Bartoszewski, R. (2022) · Cancers · doi:10.3390/cancers14194870 · Cited by 43
Vanoni, O., Paganetti, P., & Molinari, M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0459 · Cited by 28
Self-citationMannan, M. A.-U., Shadrick, W. R., Biener, G., Shin, B.-S., Anshu, A., Raicu, V., Frick, D. N., & Dey, M. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.036 · Cited by 18
Chaperoning the Mononegavirales: Current Knowledge and Future Directions
Latorre, V., Mattenberger, F., & Geller, R. (2018) · Viruses · doi:10.3390/v10120699 · Cited by 14
Metadata
- Authors
- Hebert, D. N., & Molinari, M.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2007-10
- Volume
- 87
- Issue
- 4
- Pages
- 1377-1408
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2071767667
- Cited by
- 671
- References
- 20
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- green
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