Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1485
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dc.contributor.authorNandurdikar, Rahul S.en_US
dc.contributor.authorMaciag, Anna E.en_US
dc.contributor.authorHong, Sam Y.en_US
dc.contributor.authorCHAKRAPANI, HARINATHen_US
dc.contributor.authorCitro, Michael L.en_US
dc.contributor.authorKeefer, Larry K.en_US
dc.contributor.authorSaavedra, Joseph E.en_US
dc.date.accessioned2019-01-21T10:29:25Z
dc.date.available2019-01-21T10:29:25Z
dc.date.issued2009-12en_US
dc.identifier.citationOrganic Letters, 12(1), 56-59.en_US
dc.identifier.issn1523-7060en_US
dc.identifier.issn1523-7052en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1485-
dc.identifier.urihttps://doi.org/10.1021/ol902481sen_US
dc.description.abstractGlcNAc-PROLI/NO prodrugs that are activated by N-acetylglucosaminidase to release nitric oxide (NO) are described. A classical acid-amine coupling is used to bifunctionalize these PROLI/NO prodrugs, which on activation generate up to 4 mol of NO, a peptide residue, and an N-acetylglucosamine residue. Many of the prodrugs synthesized are efficient sources of intracellular NO.en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectPROLI/NOen_US
dc.subjectlysine methylen_US
dc.subjectGlycosidaseen_US
dc.subjectPeptide residueen_US
dc.subject2010en_US
dc.titleGlycosylated PROLI/NO Derivatives as Nitric Oxide Prodrugsen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleOrganic Lettersen_US
dc.publication.originofpublisherForeignen_US
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