Effect of T68A/N126Y mutations on the conformational and ligand binding landscape of Coxsackievirus B3 3C protease-Reference-Cited by-同舟云学术

Effect of T68A/N126Y mutations on the conformational and ligand binding landscape of Coxsackievirus B3 3C protease

Published:2015 Issue:8 Volume:11 Page:2303-2311
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Bhakat Soumendranath¹²³⁴

Affiliation:

1. Division of Biophysical Chemistry

2. Lund University

3. SE-22100 Lund

4. Sweden

Abstract

3C protease of Coxsackievirus B3 (CVB3) plays an essential role in the viral replication cycle, and therefore, emerged as an attractive therapeutic target for the treatment of human diseases caused by CVB3 infection.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2015/MB/C5MB00262A

Reference33 articles.

1. Rapid detection of respiratory picornaviruses in nasopharyngeal aspirates by immunofluorescence assay

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