The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems
Open accessAbstract
Summary The evolution of eukaryotes was accompanied by an increased need for intracellular communication and cellular specialization. Thus, a more complex collection of secreted and membrane proteins had to be synthesized, modified, and folded. The endoplasmic reticulum (ER) thereby became equipped with devoted enzymes and associated factors that both catalyze the production of secreted proteins and remove damaged proteins. A means to modify ER function to accommodate and destroy misfolded proteins also evolved. Not surprisingly, a growing number of human diseases are linked to various facets of ER function. Each of these topics will be discussed in this article, with an emphasis on recent reports in the literature that employed diverse models.
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Cites
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
Self-citationBiological and Chemical Approaches to Diseases of Proteostasis Deficiency
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Misfolded proteins partition between two distinct quality control compartments
Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932
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The unfolded protein response signals through high-order assembly of Ire1
Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., Stroud, R. M., & Walter, P. (2009) · Nature · doi:10.1038/nature07661 · Cited by 656
A Stress-Responsive System for Mitochondrial Protein Degradation
Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304
Self-citationProtein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
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The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
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Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation
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Cited by
Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., Yates, J. R., Su, A. I., Kelly, J. W., & Wiseman, R. L. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.024 · Cited by 554
CFTR: folding, misfolding and correcting the ΔF508 conformational defect
Lukacs, G. L., & Verkman, A. S. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.10.003 · Cited by 375
Ubiquitin and membrane protein turnover: from cradle to grave
MacGurn, J. A., Hsu, P.-C., & Emr, S. D. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060210-093619 · Cited by 287
Hughes, A., Oxford, A., Tawara, K., Jorcyk, C., & Oxford, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030665 · Cited by 113
ER stress causes widespread protein aggregation and prion formation
Hamdan, N., Kritsiligkou, P., & Grant, C. M. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612165 · Cited by 85
Metadata
- Authors
- Brodsky, J. L., & Skach, W. R.
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2011-08
- Volume
- 23
- Issue
- 4
- Pages
- 464-475
- ISSN
- 0955-0674 (ISSN-L)
- OpenAlex
- W2082001606
- Cited by
- 242
- References
- 12
- FWCI
- 1.19
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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