Chaperone-bound Intermediates
Chaperone-Bound Intermediates is a folding intermediate that is transiently associated with molecular chaperones during protein folding, distinguishing it from other folding intermediates by its specific stabilization and regulation through chaperone binding to prevent misfolding or aggregation.
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4K
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156
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58
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2017–2026
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Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Michael J. Kerner, Dean J. Naylor, Yasushi Ishihama et al. · Cell · 2005 · 666 citations · Full text
Residues in chaperonin GroEL required for polypeptide binding and release
Wayne A. Fenton, Yechezkel Kashi, Krystyna Furtak et al. · Nature · 1994 · 642 citations
Thomas Langer, Günter Pfeifer, Jörg Martin et al. · The EMBO Journal · 1992 · 417 citations · Full text
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding
Achim Brinker, Guenther Pfeifer, Michael J. Kerner et al. · Cell · 2001 · 300 citations · Full text
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Howard Hughes Medical Institute
Chevy Chase, United States
4 h-index
10 publications
2.2K citations
Max Planck Institute of Biochemistry
Martinsried, Germany
4 h-index
17 publications
5.7K citations
Case Western Reserve University
Cleveland, United States
3 h-index
8 publications
369 citations
Stanford University
Stanford, United States
3 h-index
8 publications
822 citations
Yale University
New Haven, United States
3 h-index
7 publications
2.2K citations
Harvard University
Cambridge, United States
2 h-index
7 publications
256 citations
Max Planck Society
Munich, Germany
2 h-index
5 publications
513 citations
Institute of Structural and Molecular Biology
London, United Kingdom
2 h-index
5 publications
478 citations
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JMB · 8 publications · 420 citations
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JBC · 6 publications · 239 citations
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3 publications · 790 citations
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2 publications · 966 citations
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2 publications · 108 citations
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