The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes

10.1371/journal.ppat.1002030

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Main Authors:	Ferron F., Li Z., Danek E.I., Luo D., Wong Y., Coutard B., Lantez V., Charrel R., Canard B., Walz T., Lescar J.
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	Public Library of Science 2020
Subjects:	guanine nucleotide binding protein nucleoprotein oligomer ribonucleoprotein RNA complementary DNA hybrid protein nucleocapsid protein virus RNA amino terminal sequence article binding site Bunyavirus crystal structure crystallization crystallography electron microscopy hydrophobicity in vivo study molecular interaction mutagenesis nonhuman nucleotide sequence protein assembly protein conformation protein multimerization Rift Valley fever bunyavirus RNA binding amino acid sequence animal chemical structure chemistry genetics human isolation and purification metabolism methodology physiology protein domain sequence alignment site directed mutagenesis surface plasmon resonance ultrastructure virus assembly X ray crystallography Bunyaviridae Phlebovirus Rift Valley fever virus Amino Acid Sequence Animals Crystallography, X-Ray DNA, Complementary Humans Microscopy, Electron Models, Molecular Mutagenesis, Site-Directed Nucleocapsid Proteins Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Ribonucleoproteins RNA, Viral Sequence Alignment Surface Plasmon Resonance Virus Assembly
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/165414
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1654142024-11-14T04:05:32Z The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes Ferron F. Li Z. Danek E.I. Luo D. Wong Y. Coutard B. Lantez V. Charrel R. Canard B. Walz T. Lescar J. DUKE-NUS MEDICAL SCHOOL guanine nucleotide binding protein nucleoprotein oligomer ribonucleoprotein RNA complementary DNA hybrid protein nucleocapsid protein ribonucleoprotein virus RNA amino terminal sequence article binding site Bunyavirus crystal structure crystallization crystallography electron microscopy hydrophobicity in vivo study molecular interaction mutagenesis nonhuman nucleotide sequence protein assembly protein conformation protein multimerization Rift Valley fever bunyavirus RNA binding amino acid sequence animal chemical structure chemistry genetics human isolation and purification metabolism methodology physiology protein domain protein multimerization sequence alignment site directed mutagenesis surface plasmon resonance ultrastructure virus assembly X ray crystallography Bunyaviridae Phlebovirus Rift Valley fever virus Amino Acid Sequence Animals Crystallography, X-Ray DNA, Complementary Humans Microscopy, Electron Models, Molecular Mutagenesis, Site-Directed Nucleocapsid Proteins Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Ribonucleoproteins Rift Valley fever virus RNA, Viral Sequence Alignment Surface Plasmon Resonance Virus Assembly 10.1371/journal.ppat.1002030 PLoS Pathogens 7 5 e1002030 2020-03-13T05:26:47Z 2020-03-13T05:26:47Z 2011 Article Ferron F., Li Z., Danek E.I., Luo D., Wong Y., Coutard B., Lantez V., Charrel R., Canard B., Walz T., Lescar J. (2011). The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes. PLoS Pathogens 7 (5) : e1002030. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.ppat.1002030 15537366 https://scholarbank.nus.edu.sg/handle/10635/165414 Public Library of Science Unpaywall 20200320
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	guanine nucleotide binding protein nucleoprotein oligomer ribonucleoprotein RNA complementary DNA hybrid protein nucleocapsid protein ribonucleoprotein virus RNA amino terminal sequence article binding site Bunyavirus crystal structure crystallization crystallography electron microscopy hydrophobicity in vivo study molecular interaction mutagenesis nonhuman nucleotide sequence protein assembly protein conformation protein multimerization Rift Valley fever bunyavirus RNA binding amino acid sequence animal chemical structure chemistry genetics human isolation and purification metabolism methodology physiology protein domain protein multimerization sequence alignment site directed mutagenesis surface plasmon resonance ultrastructure virus assembly X ray crystallography Bunyaviridae Phlebovirus Rift Valley fever virus Amino Acid Sequence Animals Crystallography, X-Ray DNA, Complementary Humans Microscopy, Electron Models, Molecular Mutagenesis, Site-Directed Nucleocapsid Proteins Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Ribonucleoproteins Rift Valley fever virus RNA, Viral Sequence Alignment Surface Plasmon Resonance Virus Assembly
spellingShingle	guanine nucleotide binding protein nucleoprotein oligomer ribonucleoprotein RNA complementary DNA hybrid protein nucleocapsid protein ribonucleoprotein virus RNA amino terminal sequence article binding site Bunyavirus crystal structure crystallization crystallography electron microscopy hydrophobicity in vivo study molecular interaction mutagenesis nonhuman nucleotide sequence protein assembly protein conformation protein multimerization Rift Valley fever bunyavirus RNA binding amino acid sequence animal chemical structure chemistry genetics human isolation and purification metabolism methodology physiology protein domain protein multimerization sequence alignment site directed mutagenesis surface plasmon resonance ultrastructure virus assembly X ray crystallography Bunyaviridae Phlebovirus Rift Valley fever virus Amino Acid Sequence Animals Crystallography, X-Ray DNA, Complementary Humans Microscopy, Electron Models, Molecular Mutagenesis, Site-Directed Nucleocapsid Proteins Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Ribonucleoproteins Rift Valley fever virus RNA, Viral Sequence Alignment Surface Plasmon Resonance Virus Assembly Ferron F. Li Z. Danek E.I. Luo D. Wong Y. Coutard B. Lantez V. Charrel R. Canard B. Walz T. Lescar J. The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
description	10.1371/journal.ppat.1002030
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL Ferron F. Li Z. Danek E.I. Luo D. Wong Y. Coutard B. Lantez V. Charrel R. Canard B. Walz T. Lescar J.
format	Article
author	Ferron F. Li Z. Danek E.I. Luo D. Wong Y. Coutard B. Lantez V. Charrel R. Canard B. Walz T. Lescar J.
author_sort	Ferron F.
title	The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
title_short	The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
title_full	The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
title_fullStr	The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
title_full_unstemmed	The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
title_sort	hexamer structure of the rift valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
publisher	Public Library of Science
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/165414
_version_	1821215607143530496

The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes

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