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Article: Investigation of the binding and cleavage characteristics of N1 neuraminidases from avian, seasonal, and pandemic influenza viruses using saturation transfer difference nuclear magnetic resonance

TitleInvestigation of the binding and cleavage characteristics of N1 neuraminidases from avian, seasonal, and pandemic influenza viruses using saturation transfer difference nuclear magnetic resonance
Authors
Issue Date2014
Citation
Influenza and other respiratory viruses, 2014, v. 8 n. 2, p. 235-242 How to Cite?
AbstractThe main function of influenza neuraminidase (NA) involves enzymatic cleavage of sialic acid from the surface of host cells resulting in the release of the newly produced virions from infected cells, as well as aiding the movement of virions through sialylated mucus present in the respiratory tract. However, there has previously been little information on the binding affinity of different forms of sialylated glycan with NA. Our objectives were then to investigate both sialic acid binding and cleavage of neuraminidase at an atomic resolution level.
Persistent Identifierhttp://hdl.handle.net/10722/199809
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorGarcia, JCen_US
dc.contributor.authorLai, JCCen_US
dc.contributor.authorHaselhorst, Ten_US
dc.contributor.authorChoy, KTen_US
dc.contributor.authorYen, Hen_US
dc.contributor.authorPeiris, JSMen_US
dc.contributor.authorItzstein, MVen_US
dc.contributor.authorNicholls, JMen_US
dc.date.accessioned2014-07-22T01:38:32Z-
dc.date.available2014-07-22T01:38:32Z-
dc.date.issued2014en_US
dc.identifier.citationInfluenza and other respiratory viruses, 2014, v. 8 n. 2, p. 235-242en_US
dc.identifier.urihttp://hdl.handle.net/10722/199809-
dc.description.abstractThe main function of influenza neuraminidase (NA) involves enzymatic cleavage of sialic acid from the surface of host cells resulting in the release of the newly produced virions from infected cells, as well as aiding the movement of virions through sialylated mucus present in the respiratory tract. However, there has previously been little information on the binding affinity of different forms of sialylated glycan with NA. Our objectives were then to investigate both sialic acid binding and cleavage of neuraminidase at an atomic resolution level.en_US
dc.languageengen_US
dc.relation.ispartofInfluenza and other respiratory virusesen_US
dc.titleInvestigation of the binding and cleavage characteristics of N1 neuraminidases from avian, seasonal, and pandemic influenza viruses using saturation transfer difference nuclear magnetic resonanceen_US
dc.typeArticleen_US
dc.identifier.emailGarcia, JC: jmgarcia@hku.hken_US
dc.identifier.emailLai, JCC: jimmylcc@connect.hku.hken_US
dc.identifier.emailChoy, KT: ktchoy@hku.hken_US
dc.identifier.emailYen, H: hyen@hku.hken_US
dc.identifier.emailPeiris, JSM: malik@hkucc.hku.hken_US
dc.identifier.emailNicholls, JM: jmnichol@hkucc.hku.hken_US
dc.identifier.authorityYen, H=rp00304en_US
dc.identifier.authorityPeiris, JSM=rp00410en_US
dc.identifier.authorityNicholls, JM=rp00364en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1111/irv.12184en_US
dc.identifier.pmid24118862-
dc.identifier.pmcidPMC4186472-
dc.identifier.hkuros231877en_US
dc.identifier.volume8en_US
dc.identifier.issue2en_US
dc.identifier.spage235en_US
dc.identifier.epage242en_US

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