Mechanism of Phosphorylation-Induced Folding of 4E-BP2 Revealed by Molecular Dynamics Simulations-Reference-Cited by-同舟云学术

Mechanism of Phosphorylation-Induced Folding of 4E-BP2 Revealed by Molecular Dynamics Simulations

Published:2016-12-05 Issue:1 Volume:13 Page:320-328
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Zeng Juan¹^ORCID,Jiang Fan¹,Wu Yun-Dong¹²

Affiliation:

1. Laboratory of Computational Chemistry and Drug Design, Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen 518055, China

2. College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China

Funder

Shenzhen Graduate School, Peking University

National Natural Science Foundation of China

Shenzhen Science and Technology Innovation Committee

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.6b00848

Reference73 articles.

1. Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling

2. Post-translational modifications induce significant yet not extreme changes to protein structure

3. Exploring the conformational and binding properties of unphosphorylated/phosphorylated monomeric and trimeric Bcl-2 through docking and molecular dynamics simulations

4. Tandem phosphorylation within an intrinsically disordered region regulates ACTN4 function

5. A New Twist on Clock Protein Phosphorylation: A Conformational Change Leads to Protein Degradation

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