Chaperone-substrate Recognition
Chaperone-Substrate Recognition is a molecular interaction mechanism by which chaperone proteins selectively identify and bind non-native or misfolded protein substrates through exposed hydrophobic regions or specific sequence motifs, thereby initiating proper folding, preventing aggregation, or targeting for degradation.
875
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Citations
3.6K
Authors
945
Institutions
Publications per year
2017–2026
141
Parents
875
Proteins as molecular chaperones
John Ellis · Nature · 1987 · 916 citations
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Mikko Taipale, Irina Krykbaeva, Martina Koeva et al. · Cell · 2012 · 903 citations · Full text
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Howard Hughes Medical Institute
Chevy Chase, United States
34 h-index
98 publications
10.9K citations
National Institutes of Health
Bethesda, United States
29 h-index
137 publications
11.6K citations
University of Michigan
Ann Arbor, United States
25 h-index
127 publications
11.8K citations
Heidelberg University
Heidelberg, Germany
25 h-index
127 publications
20.2K citations
Technical University of Munich
Munich, Germany
20 h-index
114 publications
9.1K citations

University of Toronto
Toronto, Canada
20 h-index
88 publications
15.8K citations

Centre National de la Recherche Scientifique
Paris, France
18 h-index
109 publications
5.1K citations
Max Planck Institute of Biochemistry
Martinsried, Germany
16 h-index
39 publications
9.1K citations
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JBC · 137 publications · 9.5K citations
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JMB · 58 publications · 3.5K citations
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PNAS · 41 publications · 4.2K citations
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27 publications · 5.5K citations
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BBRC · 26 publications · 1K citations
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