Chaperone-mediated Folding
Chaperone-Mediated Folding is a protein folding mechanism in which molecular chaperones selectively bind to nascent or misfolded polypeptides to prevent aggregation and facilitate proper folding through transient, non-covalent interactions, distinguishing it from spontaneous or co-translational folding pathways.
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2017–2026
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Chaperone-assisted Protein Folding
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THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Martin Schröder, Randal J. Kaufman · Annual Review of Biochemistry · 2005 · 3K citations · Full text
Small heat shock proteins are molecular chaperones.
Ursula Jakob, Matthias Gaestel, Katrin Engel et al. · Journal of Biological Chemistry · 1993 · 1.4K citations · Full text
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Howard Hughes Medical Institute
Chevy Chase, United States
97 h-index
455 publications
107.1K citations
University of Michigan
Ann Arbor, United States
64 h-index
413 publications
46.9K citations
Heidelberg University
Heidelberg, Germany
62 h-index
376 publications
51.3K citations
Max Planck Institute of Biochemistry
Martinsried, Germany
60 h-index
357 publications
54K citations
National Institutes of Health
Bethesda, United States
58 h-index
355 publications
36.3K citations
Stanford University
Stanford, United States
56 h-index
314 publications
34.7K citations
Technical University of Munich
Munich, Germany
52 h-index
398 publications
38.8K citations
Yale University
New Haven, United States
52 h-index
208 publications
43.4K citations
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JBC · 712 publications · 58.1K citations
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PNAS · 246 publications · 28.7K citations
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