The role of dynamics in allosteric regulation.
By Dorothee Kern, E. Zuiderweg. Current Opinion in Structural Biology, 2003
642 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/232c63e11b01290bad4e035a0a20ceea1b90d1f7
How researchers see this paper
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In Materials Chemistry
- Martin Karplus
- Qiang Cui
- Carolina Brito
- Le Yan
- Riccardo Ravasio
- N. V. Dokholyan
- Matthieu Wyart
- Lucy J. Colwell
In Molecular Biology
- Qiang Cui
- Martin Karplus
- Dima Kozakov
- Junseock Koh
- Ivet Bahar
- N. V. Dokholyan
- John Karanicolas
- H. Youn
In Spectroscopy
- Martin Karplus
- Qiang Cui
- Ivet Bahar
- M. Grimaldo
- F. Roosen‐Runge
- Dima Kozakov
- P. Hamm
- Olivier Michielin
Citations in the corpus
- Protein Sectors: Statistical Coupling Analysis versus Conservation (2014, background): “An experimental test for such inhomogeneities inside proteins could employ NMR spectroscopy to follow the dynamics of specific atoms while the protein is undergoing conformational change [14, 26].”
- On the accuracy of inferring energetic coupling between distant sites in protein families from evolutionary imprints: Illustrations using lattice model (2009, background): “6 Given the ubiquitous nature of allosteric control in a number of biological processes (movements of motors on polar tracks,7 domain movements in molecular chaperones,8 and enzyme catalysis9), it is important to determine the key residues that are involved in the signalling pathways.”
- Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, background): “with current views about allosteric proteins (4, 18, 25), and”
- Functional dynamics of PDZ binding domains: a normal-mode analysis. (2005, background): “Flexibility and internal mobility of proteins have been recognized as fundamental to their biological functions (Berendsen and Hayward 2000; Frauenfelder and others 2001; Kern and Zuiderweg 2003), since most of the biological activity occurs close to the native state.”
- Allostery in Its Many Disguises: From Theory to Applications (2019, background): “They also acknowledge the role of dynamics, but argue against the concept of dynamic allostery discussed above, which involves no changes between distinct conformational states (see also Kern and Zuiderweg, 2003).”
- Dynamically driven protein allostery (2006, background): “Although there is increasing evidence suggesting a role of conformational dynamics in cooperative ligand-binding processe”
- Allostery and cooperativity revisited (2008, background): “…of small- to medium-sized proteins, a ‘‘new view’’ of allosteric transitions, often referred to as the ‘‘population-shift’’ model, has become very popular (Kern and Zuiderweg 2003; Gunasekaran et al. 2004; Swain and Gierasch 2006; Bahar et al. 2007; see also an earlier review, Jardetzky 1996).”
- Dynamics of proteins in solution (2019, background): “For further reading on this topic, we refer the reader to Kern and Zuiderweg (2003); Tzeng and Kalodimos (2011); Motlagh et al. (2014); Kornev and Taylor (2015); Papaleo et al. (2016).”