SrasV1, Main, Exploration, bibRecord, 001699

Atlas of coronavirus replicase structure.

Identifieur interne : 001699 ( Main/Exploration ); précédent : 001698; suivant : 001700

Atlas of coronavirus replicase structure.

Auteurs : Benjamin W. Neuman [Royaume-Uni] ; Peter Chamberlain [Royaume-Uni] ; Fern Bowden [Royaume-Uni] ; Jeremiah Joseph [États-Unis]

Source :

Virus research [ 1872-7492 ] ; 2014.

RBID : pubmed:24355834

Descripteurs français

KwdFr :
- Complexes multienzymatiques (), Complexes multienzymatiques (métabolisme), Coronavirus (), Coronavirus (enzymologie), Coronavirus (physiologie), Cristallographie aux rayons X, Cryomicroscopie électronique, Diffusion aux petits angles, RNA replicase (), RNA replicase (métabolisme), Spectroscopie par résonance magnétique.
MESH :
- enzymologie : Coronavirus.
- métabolisme : Complexes multienzymatiques, RNA replicase.
- physiologie : Coronavirus.
- Complexes multienzymatiques, Coronavirus, Cristallographie aux rayons X, Cryomicroscopie électronique, Diffusion aux petits angles, RNA replicase, Spectroscopie par résonance magnétique.

English descriptors

KwdEn :
- Coronavirus (chemistry), Coronavirus (enzymology), Coronavirus (physiology), Cryoelectron Microscopy, Crystallography, X-Ray, Magnetic Resonance Spectroscopy, Multienzyme Complexes (chemistry), Multienzyme Complexes (metabolism), RNA Replicase (chemistry), RNA Replicase (metabolism), Scattering, Small Angle.
MESH :
- chemical , chemistry : Multienzyme Complexes, RNA Replicase.
- chemistry : Coronavirus.
- enzymology : Coronavirus.
- chemical , metabolism : Multienzyme Complexes, RNA Replicase.
- physiology : Coronavirus.
- Cryoelectron Microscopy, Crystallography, X-Ray, Magnetic Resonance Spectroscopy, Scattering, Small Angle.

Abstract

The international response to SARS-CoV has produced an outstanding number of protein structures in a very short time. This review summarizes the findings of functional and structural studies including those derived from cryoelectron microscopy, small angle X-ray scattering, NMR spectroscopy, and X-ray crystallography, and incorporates bioinformatics predictions where no structural data is available. Structures that shed light on the function and biological roles of the proteins in viral replication and pathogenesis are highlighted. The high percentage of novel protein folds identified among SARS-CoV proteins is discussed.

DOI: 10.1016/j.virusres.2013.12.004
PubMed: 24355834

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">The international response to SARS-CoV has produced an outstanding number of protein structures in a very short time. This review summarizes the findings of functional and structural studies including those derived from cryoelectron microscopy, small angle X-ray scattering, NMR spectroscopy, and X-ray crystallography, and incorporates bioinformatics predictions where no structural data is available. Structures that shed light on the function and biological roles of the proteins in viral replication and pathogenesis are highlighted. The high percentage of novel protein folds identified among SARS-CoV proteins is discussed. </div>
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Serveur d'exploration SRAS

Atlas of coronavirus replicase structure.

Atlas of coronavirus replicase structure.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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