Influenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitors

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Influenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitors is …
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scholarly articleQ13442814

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P819ADS bibcode2013NatCo...4.1491V
P6179Dimensions Publication ID1002009031
P356DOI10.1038/NCOMMS2487
P698PubMed publication ID23422659

P50authorGeorge F. GaoQ16260071
Jinghua YanQ88146803
Jianxun QiQ90990686
P2093author name stringYan Wu
Qing Li
Yan Li
Christopher J Vavricka
Yasuo Suzuki
Yue Liu
Kosuke Tanaka
Hiromasa Kiyota
Nongluk Sriwilaijaroen
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Mutagenesis of the Conserved Active-Site Tyrosine Changes a Retaining Sialidase into an Inverting SialidaseQ30882880
Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virusQ31018417
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Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activityQ34565520
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Mechanisms of the action of povidone-iodine against human and avian influenza A viruses: its effects on hemagglutination and sialidase activities.Q37337761
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P407language of work or nameEnglishQ1860
P304page(s)1491
P577publication date2013-01-01
P1433published inNature CommunicationsQ573880
P1476titleInfluenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitors
P478volume4

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