Chaperone-Assisted Assembly is a molecular mechanism in which molecular chaperones selectively stabilize nascent or misfolded subunits and facilitate their correct oligomeric organization into a functional quaternary structure through transient, ATP-regulated interactions.
171
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2017–2026
26
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171
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
Sean M. Hemmingsen, Carol A. Woolford, Saskia M. van der Vies et al. · Nature · 1988 · 1.3K citations
Structural Basis of Chaperone Function and Pilus Biogenesis
Frederic G. Sauer, Klaus Fütterer, Jerome S. Pinkner et al. · Science · 1999 · 415 citations
1–5 of 171
Authors
810
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12
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7
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7
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5
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5
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1–5 of 810
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295
Washington University in St. Louis
St Louis, United States
12 h-index
39 publications
5.4K citations
Birkbeck, University of London
London, United Kingdom
6 h-index
13 publications
1.1K citations
University College London
London, United Kingdom
6 h-index
12 publications
807 citations
The University of Tokyo
Tokyo, Japan
6 h-index
25 publications
2K citations
Max Planck Institute of Biochemistry
Martinsried, Germany
5 h-index
23 publications
3K citations
National Institutes of Health
Bethesda, United States
5 h-index
17 publications
2.7K citations
Institute of Structural and Molecular Biology
London, United Kingdom
5 h-index
14 publications
600 citations
Swedish University of Agricultural Sciences
Uppsala, Sweden
5 h-index
11 publications
594 citations
1–8 of 295
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- Journal of Biological Chemistry
JBC · 28 publications · 2.3K citations
22
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- Proceedings of the National Academy of Sciences
PNAS · 12 publications · 1.2K citations
12
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- Journal of Molecular Biology
JMB · 9 publications · 442 citations
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- Nature
7 publications · 2.1K citations
7
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- Cell
6 publications · 1.3K citations
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