About: A structural analysis of M protein in coronavirus assembly and morphology

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	A structural analysis of M protein in coronavirus assembly and morphology
Creator	Makino, Shinji Siddell, Stuart Kuhn, Peter Kiss, Gabriella Bhella, David Neuman, Benjamin Connelly, Stephen Droese, Ben Buchmeier, Michael Fazil Baksh, M Klaus, Joseph Kunding, Andreas Sawicki, Stanley Stamou, Dimitrios Wilson, Ian
source	Elsevier; Medline; PMC
abstract	The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.
has issue date	2011-04-01(xsd:dateTime)
bibo:doi	10.1016/j.jsb.2010.11.021
bibo:pmid	21130884
has license	bronze-oa
sha1sum (hex)	bd51ebd1d7d5c9161290c1a89d4e3fb7434db6b5
schema:url	https://doi.org/10.1016/j.jsb.2010.11.021
resource representing a document's title	A structural analysis of M protein in coronavirus assembly and morphology
has PubMed Central identifier	PMC4486061
has PubMed identifier	21130884
schema:publication	Journal of Structural Biology
resource representing a document's body	covid:bd51ebd1d7d5c9161290c1a89d4e3fb7434db6b5#body_text
is schema:about of	named entity 'M PROTEIN' named entity 'assembly' named entity 'RNA' named entity 'M protein' named entity 'host' named entity 'organization' named entity 'structure' named entity 'particles' named entity 'regulate' named entity 'investigated' named entity 'PROTEIN ' named entity 'ORGANIZATION' named entity 'ASSOCIATED WITH' named entity 'FUNCTIONS' named entity 'WHERE' named entity 'ANALYSIS' named entity 'M PROTEIN' named entity 'INTERACTIONS' named entity 'CONFORMER' named entity 'PROTEIN ' named entity 'HOST' named entity 'CENTRAL' named entity 'N PROTEIN' named entity 'NEW' named entity 'STATISTICAL ANALYSIS' named entity 'NARROW' named entity 'VIRUS-LIKE PARTICLES' named entity 'COMPACT' named entity 'INSIGHT' named entity 'PRESENT' named entity 'LOW' named entity 'CLUSTERS' named entity 'VIRUS' named entity 'RIGIDITY' named entity 'MAKE' named entity 'HOW' named entity 'COME' named entity 'FINDINGS' named entity 'VIRUS ASSEMBLY' named entity 'TYPES' named entity 'VIRION' named entity 'ADOPT' named entity 'CRYOELECTRON MICROSCOPY' named entity 'S PROTEIN' named entity 'ELONGATED' named entity 'RANGE' named entity 'PLAYS' named entity 'STRUCTURE' named entity 'ACCESS' named entity 'ASSEMBLY' named entity 'MEMBRANES' named entity 'PROMOTE' named entity 'SIZE' named entity 'TOMOGRAPHY' named entity 'EVIDENCE' named entity 'ROLE' named entity 'CELLULAR' named entity 'USING' named entity 'THESE' named entity 'HELP' named entity 'CORONAVIRUS' named entity 'VIRIONS' named entity 'VIRUS PARTICLES' named entity 'SPIKE DENSITY' named entity 'HHS' named entity 'MORPHOLOGY' named entity 'STRUCTURAL ANALYSIS'

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