An alanine residue in human parainfluenza virus type 3 phosphoprotein is critical for restricting excessive N0-P interaction and maintaining N solubility-Reference-Cited by-同舟云学术

An alanine residue in human parainfluenza virus type 3 phosphoprotein is critical for restricting excessive N0-P interaction and maintaining N solubility

Published:2018-05 Issue: Volume:518 Page:64-76
ISSN:0042-6822
Container-title:Virology
language:en
Short-container-title:Virology

Author:

Zhang Shengwei,Cheng Qi,Luo Chenxi,Yin Lei,Qin Yali,Chen Mingzhou

Funder

China Natural Science Foundation

State Key Laboratory of Virology of China

Publisher

Elsevier BV

Subject

Virology

Reference36 articles.

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5. Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity;Castel;J. Virol.,2009

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1. Structural Basis of Human Parainfluenza Virus 3 Unassembled Nucleoprotein in Complex with Its Viral Chaperone;Journal of Virology;2022-01-26

2. Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35;Biomolecules;2021-10-29

3. Sumoylation of Human Parainfluenza Virus Type 3 Phosphoprotein Correlates with A Reduction in Viral Replication;Virologica Sinica;2020-11-16