Allosteric Conformation
Allosteric Conformation is a structural state of a protein characterized by a functional change in shape induced at one site due to the binding of a ligand at a distinct, spatially separated site, thereby modulating the protein's activity through conformational transmission.
116
Publications
6K
Citations
532
Authors
202
Institutions
Publications per year
2017–2026
24
Parents
116
Allosteric initiation and regulation of catalysis with a molecular knot
Vanesa Marcos, Alexander J. Stephens, Javier Jaramillo-García et al. · Science · 2016 · 254 citations · Full text
Molecular glue CELMoD compounds are regulators of cereblon conformation
Edmond R. Watson, Scott J. Novick, Mary E. Matyskiela et al. · Science · 2022 · 197 citations · Full text
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202

Centre National de la Recherche Scientifique
Paris, France
7 h-index
32 publications
1K citations
Institut Pasteur
Paris, France
4 h-index
20 publications
939 citations
Inserm
Paris, France
4 h-index
7 publications
553 citations
University of Washington
Seattle, United States
4 h-index
24 publications
707 citations

Chinese Academy of Sciences
Beijing, China
4 h-index
16 publications
686 citations
University of Cambridge
Cambridge, United Kingdom
3 h-index
5 publications
672 citations

McMaster University
Hamilton, Canada
3 h-index
7 publications
271 citations
Harvard University
Cambridge, United States
3 h-index
23 publications
2.1K citations
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16 publications · 645 citations
14
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JBC · 11 publications · 542 citations
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PNAS · 10 publications · 626 citations
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JMB · 6 publications · 744 citations
6
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5 publications · 276 citations
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