The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Open accessAbstract
Molecular chaperones are known to facilitate cellular protein folding. They bind non‐native proteins and orchestrate the folding process in conjunction with regulatory cofactors that modulate the affinity of the chaperone for its substrate. However, not every attempt to fold a protein is successful and chaperones can direct misfolded proteins to the cellular degradation machinery for destruction. Protein quality control thus appears to involve close cooperation between molecular chaperones and energy‐dependent proteases. Molecular mechanisms underlying this interplay have been largely enigmatic so far. Here we present a novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation.
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Cites
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Takayama, S., Sato, T., Krajewski, S., Kochel, K., Irie, S., Milian, J. A., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90410-7 · Cited by 857
The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A., & Cyr, D. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1492 · Cited by 335
Self-citation
Cited by
Rosenzweig, R., Nillegoda, N. B., Mayer, M. P., & Bukau, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0133-3 · Cited by 1,285
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423
Chaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260
“HSC70 is a multifunctional chaperone that also contributes to the disassembly of clathrin from endocytic pits, folding of newly synthesized proteins, refolding of unfolded proteins and, as a partner of HSP90, to the stabilization of proteins in transient unstable conformations [14].”
BackgroundDomain Interdependence in the Biosynthetic Assembly of CFTR
Cui, L., Aleksandrov, L., Chang, X.-B., Hou, Y.-X., He, L., Hegedus, T., Gentzsch, M., Aleksandrov, A., Balch, W. E., & Riordan, J. R. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.086 · Cited by 216
AI-Based Protein Structure Prediction in Drug Discovery: Impacts and Challenges
Schauperl, M., & Denny, R. A. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00026 · Cited by 122
Metadata
- Authors
- Höhfeld, J., Cyr, D. M., & Patterson, C.
- Venue
- EMBO reports
- Published
- 2001-10
- Volume
- 2
- Issue
- 10
- Pages
- 885-890
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- OpenAlex
- W2126581529
- Cited by
- 338
- References
- 3
- FWCI
- 6.95
- Type
- journal article
- Language
- en
- Open access
- green
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