SrasV1, Main, Exploration, bibRecord, 002F88

The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.

Identifieur interne : 002F88 ( Main/Exploration ); précédent : 002F87; suivant : 002F89

The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.

Auteurs : Yingchun Zeng [République populaire de Chine] ; Linbai Ye ; Shengli Zhu ; Hong Zheng ; Peng Zhao ; Weijia Cai ; Liya Su ; Yinglong She ; Zhenghui Wu

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2008.

RBID : pubmed:18243139

Descripteurs français

KwdFr :
- Cellules HeLa, Humains, Liaison aux protéines, Phosphorylation, Protéines nucléaires (), Protéines nucléaires (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Sites de fixation, Virus du SRAS (), Virus du SRAS (métabolisme).
MESH :
- métabolisme : Protéines nucléaires, Protéines nucléocapside, Virus du SRAS.
- Cellules HeLa, Humains, Liaison aux protéines, Phosphorylation, Protéines nucléaires, Protéines nucléocapside, Sites de fixation, Virus du SRAS.

English descriptors

KwdEn :
- Binding Sites, HeLa Cells, Humans, Nuclear Proteins (chemistry), Nuclear Proteins (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Phosphorylation, Protein Binding, SARS Virus (chemistry), SARS Virus (metabolism).
MESH :
- chemical , chemistry : Nuclear Proteins, Nucleocapsid Proteins.
- chemical , metabolism : Nuclear Proteins, Nucleocapsid Proteins.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- Binding Sites, HeLa Cells, Humans, Phosphorylation, Protein Binding.

Abstract

Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.

DOI: 10.1016/j.bbrc.2008.01.096
PubMed: 18243139

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.</div>
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The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.

The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.

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

Pour générer des pages wiki

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