Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease-Reference-Cited by-同舟云学术

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Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease

Published:2016-05 Issue:4 Volume:62 Page:572-585
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Békés Miklós,van der Heden van Noort Gerbrand J.,Ekkebus Reggy,Ovaa Huib,Huang Tony T.,Lima Christopher D.

Funder

National Institutes of Health (NIH) National Institute of General Medical Sciences

Department of Energy Office of Science by Argonne National Laboratory

NIH/NIGMS

NIH National Cancer Institute

NYU Laura & Isaac Perlmutter Cancer Center

NWO-VENI

NOW-VICI

ERC

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference37 articles.

1. Catalytic function and substrate specificity of the papain-like protease domain of nsp3 from the Middle East respiratory syndrome coronavirus;Báez-Santos;J. Virol.,2014

2. Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression;Bailey-Elkin;J. Biol. Chem.,2014

3. Viral OTU deubiquitinases: a structural and functional comparison;Bailey-Elkin;PLoS Pathog.,2014

4. SARS hCoV papain-like protease is a unique Lys48 linkage-specific di-distributive deubiquitinating enzyme;Békés;Biochem. J.,2015

5. Mapping the active site of papain with the aid of peptide substrates and inhibitors;Berger;Philos. Trans. R. Soc. Lond. B Biol. Sci.,1970

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