Effect of Ser392 Phosphorylation on the Structure and Dynamics of the Polybasic Domain of ADP Ribosylation Factor Nucleotide Site Opener Protein: A Molecular Simulation Study-Reference-Cited by-同舟云学术

Effect of Ser392 Phosphorylation on the Structure and Dynamics of the Polybasic Domain of ADP Ribosylation Factor Nucleotide Site Opener Protein: A Molecular Simulation Study

Published:2013-10-01 Issue:41 Volume:52 Page:7339-7349
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Srinivasaraghavan Kannan¹²,Nacro Kassoum²,Grüber Gerhard¹³,Verma Chandra S.¹³⁴

Affiliation:

1. Bioinformatics Institute (A*STAR), 30 Biopolis Street, 07-01 Matrix, Singapore 138671

2. Experimental Therapeutics Centre (A*STAR), 31 Biopolis Street, 03-01 Nanos, Singapore 138669

3. School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551

4. Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi400912e

Reference37 articles.

1. Regulation of Arf Activation: the Sec7 Family of Guanine Nucleotide Exchange Factors

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4. ARF proteins: roles in membrane traffic and beyond

5. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway

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