Probing the reactivation process of sarin-inhibited acetylcholinesterase with α-nucleophiles: Hydroxylamine anion is predicted to be a better antidote with DFT calculations

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dc.contributor.authorKhan, M. A. S.
dc.contributor.authorLo, R.
dc.contributor.authorBandyopadhyay, T.
dc.contributor.authorGanguly, B.
dc.date.accessioned2011-12-23T09:15:37Z
dc.date.available2011-12-23T09:15:37Z
dc.date.issued2011
dc.format.extent5045 bytes
dc.format.mimetypetext/html
dc.identifier.sourceJournal of Molecular Graphics & Modelling, 2011. Vol. 29 (8): pp. 1039-1046en
dc.identifier.urihttp://hdl.handle.net/123456789/5532
dc.language.isoenen
dc.subjectReactivationen
dc.subjectOP-inihited AChEen
dc.subjectAlpha-nucleophilesen
dc.subjectDensity functional calculationsen
dc.subjectHydroxylamine anionen
dc.titleProbing the reactivation process of sarin-inhibited acetylcholinesterase with α-nucleophiles: Hydroxylamine anion is predicted to be a better antidote with DFT calculationsen
dc.typeArticleen

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