Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering - Test2 - elhamkhani - TriplyDB

Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering

Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering

http://www.wikidata.org/entity/Q27704051

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RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments.Nucleocapsid protein-dependent assembly of the RNA packaging signal of Middle East respiratory syndrome coronavirus.Overexpression of the nucleocapsid protein of Middle East respiratory syndrome coronavirus up-regulates CXCL10

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Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering

http://www.wikidata.org/entity/Q27704051

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2016 nî lūn-bûn

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2016 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2016 թվականի փետրվարին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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Structural characterization of ...... d small-angle X-ray scattering

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Structural characterization of ...... d small-angle X-ray scattering

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Structural characterization of ...... d small-angle X-ray scattering

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Acta crystallographica. Section D, Structural biology

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Structural characterization of ...... d small-angle X-ray scattering

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Amal Baklouti

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Marion Sévajol

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Nicolas Papageorgiou

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P2860

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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

The Crystal Structures of Chikungunya and Venezuelan Equine Encephalitis Virus nsP3 Macro Domains Define a Conserved Adenosine Binding Pocket

Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N Protein

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

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

Coronavirus N Protein N-Terminal Domain (NTD) Specifically Binds the Transcriptional Regulatory Sequence (TRS) and Melts TRS-cTRS RNA Duplexes

Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein

Structural Basis for the Identification of the N-Terminal Domain of Coronavirus Nucleocapsid Protein as an Antiviral Target

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192-202

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10.1107/S2059798315024328

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Pt 2

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72

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Julie Lichière

François Ferron

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2016-02-01T00:00:00Z

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26894667

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X-ray diffraction

Middle East respiratory syndrome coronavirus