Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1-Reference-Cited by-同舟云学术

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Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1

Published:2018-01-23 Issue:21 Volume:122 Page:5623-5629
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Campitelli Paul¹,Guo Jingjing²^ORCID,Zhou Huan-Xiang³^ORCID,Ozkan S. Banu¹^ORCID

Affiliation:

1. Department of Physics and Center for Biological Physics, Arizona State University, Tempe, Arizona 85287, United States

2. School of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, China

3. Department of Chemistry and Department of Physics, University of Illinois at Chicago, Chicago, Illinois 60607, United States

Funder

Division of Molecular and Cellular Biosciences

Gordon and Betty Moore Foundation

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.7b11971

Reference42 articles.

1. On the nature of allosteric transitions: A plausible model

2. Unsuspected pathway of the allosteric transition in hemoglobin

3. Allostery without conformational change

4. Hidden dynamic allostery in a PDZ domain

5. Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?

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