About: Viruses and viral proteins

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Viruses and viral proteins
Creator	Ferrero, Diego Verdaguer, Nuria Murthy, Mathur
Source	Medline; PMC
abstract	For more than 30 years X-ray crystallography has been by far the most powerful approach for determining the structures of viruses and viral proteins at atomic resolution. The information provided by these structures, which covers many important aspects of the viral life cycle such as cell-receptor recognition, viral entry, nucleic acid transfer and genome replication, has extensively enriched our vision of the virus world. Many of the structures available correspond to potential targets for antiviral drugs against important human pathogens. This article provides an overview of the current knowledge of different structural aspects of the above-mentioned processes.
has issue date	2014-10-14(xsd:dateTime)
bibo:doi	10.1107/s205225251402003x
bibo:pmid	25485129
has license	cc-by
sha1sum (hex)	9484a7c6359d1364cd37bb1d80bdefd118d7ffe6
schema:url	https://doi.org/10.1107/s205225251402003x
resource representing a document's title	Viruses and viral proteins
has PubMed Central identifier	PMC4224467
has PubMed identifier	25485129
schema:publication	IUCrJ
resource representing a document's body	covid:9484a7c6359d1364cd37bb1d80bdefd118d7ffe6#body_text
is schema:about of	named entity 'acid' named entity 'VIRUSES' named entity 'VIRAL PROTEINS' named entity 'X-RAY CRYSTALLOGRAPHY' named entity 'VIRAL PROTEINS' named entity 'INFORMATION' named entity 'OVERVIEW' named entity 'ATOMIC' named entity 'GENOME' named entity 'RECEPTOR RECOGNITION' named entity 'STRUCTURAL' named entity 'PATHOGENS' named entity 'DIFFERENT' named entity 'HUMAN' named entity 'STRUCTURES' named entity 'THESE' named entity 'CURRENT' named entity 'IMPORTANT' named entity 'COVERS' named entity 'YEARS' named entity 'ANTIVIRAL DRUGS' named entity 'PROVIDES' named entity 'POWERFUL' named entity 'NUCLEIC ACID' named entity 'ARTICLE' named entity 'ENRICHED' named entity 'VISION' named entity 'KNOWLEDGE' named entity 'OUR' named entity 'TARGETS' named entity 'PROCESSES' named entity 'APPROACH' named entity 'CELL' named entity 'AVAILABLE' named entity 'VIRAL LIFE CYCLE' named entity 'RESOLUTION' named entity 'WORLD' named entity 'VIRAL ENTRY' named entity 'FAR' named entity 'PROVIDED' named entity 'REPLICATION' named entity 'TRANSFER' named entity 'POTENTIAL' named entity 'MORE THAN' named entity 'VIRUS' named entity 'VIRUSES' named entity 'aspects' named entity 'potential' named entity 'proteins' named entity 'powerful' named entity 'genome replication' named entity 'virus' named entity 'antiviral drugs' named entity 'viruses' named entity 'viral tropism' named entity 'core protein' named entity 'N-terminus' named entity 'active site' named entity 'cations' named entity 'phages' named entity 'trimer' named entity 'CD46' named entity 'affinity tags' named entity 'RNA' named entity 'dengue virus' named entity 'aspartyl protease' named entity 'proteolytically cleaved' named entity 'RNA' named entity 'dsDNA' named entity 'Haemagglutinin' named entity 'IUCrJ' named entity 'binding proteins' named entity 'phages' named entity 'protein' named entity 'cryoelectron microscopy' named entity 'virion' named entity 'host cells' named entity 'toxicity' named entity 'VPg'

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