Molecular Chaperones
Molecular Chaperones is a class of specialized proteins that facilitate the proper folding of other proteins by binding to non-native polypeptides and preventing misfolding or aggregation, thereby ensuring conformational maturation without being part of the final functional structure.
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2017–2026
1.7K
8.9K
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Martin Schröder, Randal J. Kaufman · Annual Review of Biochemistry · 2005 · 3K citations · Full text
Umut Özcan, Erkan Yılmaz, Lale Özcan et al. · Science · 2006 · 2.4K citations · Full text
A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
Adeela Kamal, Lia Thao, John Sensintaffar et al. · Nature · 2003 · 1.4K citations
Medicine, Oncology, Pharmacology +10
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Howard Hughes Medical Institute
Chevy Chase, United States
119 h-index
704 publications
147.4K citations
University of Michigan
Ann Arbor, United States
81 h-index
732 publications
79.5K citations
National Institutes of Health
Bethesda, United States
80 h-index
786 publications
76.3K citations
Heidelberg University
Heidelberg, Germany
79 h-index
582 publications
77.4K citations
Max Planck Institute of Biochemistry
Martinsried, Germany
73 h-index
528 publications
83.7K citations
Stanford University
Stanford, United States
70 h-index
431 publications
43.3K citations
University of Cambridge
Cambridge, United Kingdom
69 h-index
553 publications
53.6K citations

Centre National de la Recherche Scientifique
Paris, France
68 h-index
1.1K publications
62.1K citations
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JBC · 1.2K publications · 106.1K citations
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PNAS · 468 publications · 55.2K citations
132
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150 publications · 28.3K citations
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114 publications · 19.8K citations
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93 publications · 30.7K citations
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