About: Chapter 11 Rhinovirus RNA Polymerase Structure, Function, and Inhibitors

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Chapter 11 Rhinovirus RNA Polymerase Structure, Function, and Inhibitors
Creator	Kakkar, Rita Nirwan, Sonam
Source	Elsevier; PMC
abstract	Abstract Human rhinovirus is responsible for causing 50% of common cold infections in infants and adults. It belongs to the picornavirus family of nonenveloped positive-strand RNA viruses. The RNA synthesis of rhinovirus is carried out by RNA-dependent RNA polymerase, also known as 3DPol. It catalyzes the synthesis of negative-strand RNA using a positive-strand template. The structure of the enzyme consists of three domains: palm, fingers, and thumb domains and Mg2+ in the active site. These conserved structural features of the enzyme help in catalyzing phosphodiester bond formation between the two consecutive nucleotide units complimentary to the template RNA using a VPg primer. Owing to the presence of over 100 serotypes of the enzyme, designing specific inhibitors targeting the polymerase is a challenging task and until now no clinically approved antirhino viral drug is reported. In this review, we have given detailed information about the structure and function of the enzyme and also discussed some of the inhibitors and their in vivo activity against 3DPol.
has issue date	2019-12-31(xsd:dateTime)
bibo:doi	10.1016/b978-0-12-815422-9.00011-5
has license	els-covid
sha1sum (hex)	3a35087a01d75bd91c32477cd56781eec397f979
schema:url	https://doi.org/10.1016/b978-0-12-815422-9.00011-5
resource representing a document's title	Chapter 11 Rhinovirus RNA Polymerase Structure, Function, and Inhibitors
has PubMed Central identifier	PMC7173612
schema:publication	Viral Polymerases
resource representing a document's body	covid:3a35087a01d75bd91c32477cd56781eec397f979#body_text
is schema:about of	named entity 'Polymerase' named entity 'Structure' named entity 'RNA Polymerase' named entity 'Rhinovirus' named entity 'INHIBITORS' named entity 'STRUCTURE' named entity 'RNA POLYMERASE' named entity 'RNA' named entity 'Rhinovirus' named entity 'Inhibitors' named entity 'Function' named entity 'FUNCTION' named entity 'RHINOVIRUS RNA'
is part of of	Chapter 11 Rhinovirus RNA Polymerase Structure, Function, and Inhibitors Abstract Human rhinovirus is responsible for causing 50% of common cold infections in infants and adults. It belongs to the picornavirus family of nonenveloped positive-strand RNA viruses. The RNA synthesis of rhinovirus is carried out by RNA-dependent RNA polymerase, also known as 3DPol. It catalyzes the synthesis of negative-strand RNA using a positive-strand template. The structure of the enzyme consists of three domains: palm, fingers, and thumb domains and Mg2+ in the active site. These conserved structural features of the enzyme help in catalyzing phosphodiester bond formation between the two consecutive nucleotide units complimentary to the template RNA using a VPg primer. Owing to the presence of over 100 serotypes of the enzyme, designing specific inhibitors targeting the polymerase is a challenging task and until now no clinically approved antirhino viral drug is reported. In this review, we have given detailed information about the structure and function of the enzyme and also discussed some of the inhibitors and their in vivo activity against 3DPol. covid:3a35087a01d75bd91c32477cd56781eec397f979#body_text

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