pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and uncoating-Reference-Cited by-同舟云学术

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pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and uncoating

Published:2016-09-01 Issue:9 Volume:97 Page:2149-2156
ISSN:0022-1317
Container-title:Journal of General Virology
language:en
Short-container-title:

Author:

Yang Mingrui¹²,Feng Feng²,Liu Yingfang¹²,Wang Hui³,Yang Zhanqiu¹,Hou Wei¹,Liang Huanhuan²

Affiliation:

1. State Key Laboratory of Virology/Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan 430071, PR China

2. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China

3. Department of Pharmacology, School of Basic Medical Sciences, Wuhan University, Wuhan 430071, PR China

Publisher

Microbiology Society

Subject

Virology

Reference31 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution

2. Combined Results from Solution Studies on Intact Influenza Virus M1 Protein and from a New Crystal Form of Its N-Terminal Domain Show That M1 Is an Elongated Monomer

3. Thogoto virus ML protein is a potent inhibitor of the interferon regulatory factor-7 transcription factor

4. Role of the Influenza Virus M1 Protein in Nuclear Export of Viral Ribonucleoproteins

5. The Structure of a Biologically Active Influenza Virus Ribonucleoprotein Complex

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2. Bourbon virus, a newly discovered zoonotic thogotovirus;Journal of General Virology;2023-08-30

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4. Structure of Pseudomonas aeruginosa spermidine dehydrogenase: a polyamine oxidase with a novel heme‐binding fold;The FEBS Journal;2021-11-16

5. Histidine-Mediated Intramolecular Electrostatic Repulsion for Controlling pH-Dependent Protein–Protein Interaction;ACS Chemical Biology;2019-10-09

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