Allostery
Allostery is a regulatory mechanism in which the binding of a ligand at one site of a protein induces a conformational or dynamic change that alters the functional activity at a distinct, distant site within the same protein.
196
Publications
12.2K
Citations
937
Authors
372
Institutions
Publications per year
2017–2026
85
196
Allostery without conformational change
Alan Cooper, David T. F. Dryden · European Biophysics Journal · 1984 · 745 citations
Cucurbit[n]urils: from mechanism to structure and function
Lyle Isaacs · Chemical Communications · 2008 · 427 citations
Pharmacy, Biochemistry, Chemistry +13
A Unified View of “How Allostery Works”
Chung‐Jung Tsai, Ruth Nussinov · PLoS Computational Biology · 2014 · 415 citations · Full text
Structural basis for allosteric PARP-1 retention on DNA breaks
Levani Zandarashvili, Marie-France Langelier, Uday Kiran Velagapudi et al. · Science · 2020 · 331 citations · Full text
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372

Howard Hughes Medical Institute
Chevy Chase, United States
7 h-index
12 publications
1.4K citations
University of Pennsylvania
Philadelphia, United States
7 h-index
24 publications
4.7K citations
University of California San Diego
San Diego, United States
6 h-index
16 publications
1.1K citations
University of Maryland, College Park
College Park, United States
5 h-index
9 publications
897 citations
University of California, San Francisco
San Francisco, United States
5 h-index
19 publications
788 citations
ETH Zurich
Zurich, Switzerland
5 h-index
14 publications
478 citations
Columbia University
New York, United States
5 h-index
13 publications
1.4K citations
Harvard University
Cambridge, United States
5 h-index
26 publications
5.1K citations
1–8 of 372
PNAS · 24 publications · 1.7K citations
21
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JMB · 10 publications · 390 citations
10
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8 publications · 523 citations
8
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8 publications · 260 citations
8
h-index
8 publications · 615 citations
8
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