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dc.contributor.authorKankanamalage, Anushka C. Galasiti
dc.contributor.authorKim, Yunjeong
dc.contributor.authorRathnayake, Athri D.
dc.contributor.authorDamalanka, Vishnu C.
dc.contributor.authorWeerawarna, Pathum M.
dc.contributor.authorDoyle, Sean T.
dc.contributor.authorAlsoudi, Amer F.
dc.contributor.authorDissanayake, D. M. Padmasankha
dc.contributor.authorLushington, Gerald H.
dc.contributor.authorMehzabeen, Nurjahan
dc.contributor.authorBattaile, Kevin P.
dc.contributor.authorLovell, Scott
dc.contributor.authorChang, Kyeong-Ok
dc.contributor.authorGroutas, William C.
dc.date.accessioned2017-04-10T01:38:53Z
dc.date.available2017-04-10T01:38:53Z
dc.date.issued2017-01-27
dc.identifier.citationKankanamalage, Anushka C. Galasiti; Yunjeong, Kim; Rathnayake, Athri D.; Damalanka, Vishnu C.; Weerawarna, Pathum M.; Doyle, Sean T.; Alsoudi, Amer F.; Dissanayake, D. M. Padmasankha; Lushington, Gerald H.; Mehzabeen, Nurjahan; Battaile, Kevin P.; Lovell, Scott; Chang, Kyeong-Ok; Groutas, William C. 2017. Structure-based exploration and exploitation of the S-4 subsite of norovirus 3CL protease in the design of potent and permeable inhibitors. European Journal of Medicinal Chemistry, vol. 126:pp 502–516en_US
dc.identifier.issn0223-5234
dc.identifier.otherWOS:000396804600040
dc.identifier.urihttp://dx.doi.org/10.1016/j.ejmech.2016.11.027
dc.identifier.urihttp://hdl.handle.net/10057/12920
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractHuman noroviruses are the primary cause of epidemic and sporadic acute gastroenteritis. The worldwide high morbidity and mortality associated with norovirus infections, particularly among the elderly, immunocompromised patients and children, constitute a serious public health concern. There are currently no approved human vaccines or norovirus-specific small-molecule therapeutics or prophylactics. Norovirus 3CL protease has recently emerged as a potential therapeutic target for the development of anti-norovirus agents. We hypothesized that the S4 subsite of the enzyme may provide an effective means of designing potent and cell permeable inhibitors of the enzyme. We report herein the structure-guided exploration and exploitation of the S4 subsite of norovirus 3CL protease in the design and synthesis of effective inhibitors of the protease.en_US
dc.description.sponsorshipNational Institutes of Health (AI109039) is gratefully acknowledged. Use of the University of Kansas Protein Structure Laboratory was supported by a grant from the National Institute of General Medical Sciences (P30GM110761) from the National Institutes of Health. Use of the IMCA-CAT beamline 17 -ID at the Advanced Photon Source was supported by the companies of the Industrial Macromolecular Crystallography Association through a contract with Hauptman Woodward Medical Research Institute. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under contract no. DEACO2-06CH11357.en_US
dc.language.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.relation.ispartofseriesEuropean Journal of Medicinal Chemistry;v.126
dc.subjectNorovirusen_US
dc.subject3CL proteaseen_US
dc.subjectS4 subsiteen_US
dc.subjectOptimizationen_US
dc.titleStructure-based exploration and exploitation of the S-4 subsite of norovirus 3CL protease in the design of potent and permeable inhibitorsen_US
dc.typeArticleen_US
dc.rights.holderCopyright © 2017 Elsevier B.V. or its licensors or contributorsen_US


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