Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging. - Wikidata - wikimedia - TriplyDB

Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

http://www.wikidata.org/entity/Q34746639

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Structural Basis for the Identification of the N-Terminal Domain of Coronavirus Nucleocapsid Protein as an Antiviral Target Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).The coronavirus nucleocapsid is a multifunctional protein.SHAPE analysis of the RNA secondary structure of the Mouse Hepatitis Virus 5' untranslated region and N-terminal nsp1 coding sequences A key role for the carboxy-terminal tail of the murine coronavirus nucleocapsid protein in coordination of genome packaging Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein Chimeras

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Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

http://www.wikidata.org/entity/Q34746639

description

2013 nî lūn-bûn

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2013 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2013 թվականի մայիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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Transient oligomerization of t ...... s ribonucleoprotein packaging.

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Transient oligomerization of t ...... s ribonucleoprotein packaging.

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JOURNAL.PONE.0065045

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Chia-Min Michael Chen

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Ming-hui Chiang

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Tai-huang Huang

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Yen-lan Hsu

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P2860

X-Ray Structures of the N- and C-Terminal Domains of a Coronavirus Nucleocapsid Protein: Implications for Nucleocapsid Formation

Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA

Nuclear Magnetic Resonance Structure of the N-Terminal Domain of Nonstructural Protein 3 from the Severe Acute Respiratory Syndrome Coronavirus

Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method

Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.

The coronavirus nucleocapsid protein is dynamically associated with the replication-transcription complexes.

Testing the balanced electrostatic interaction hypothesis of hepatitis B virus DNA synthesis by using an in vivo charge rebalance approach

The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.

The SARS-CoV nucleocapsid protein: a protein with multifarious activities.

Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.

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severe acute respiratory syndrome-related coronavirus

ribonucleoprotein

molecular biology

severe acute respiratory syndrome coronavirus

betacoronaviruses nucleocapsid protein family

nucleoprotein [SARS-Cov]

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3662775

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