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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/19711
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dc.contributor.authorArcuri, H. A.-
dc.contributor.authorPalma, Mario Sergio-
dc.date.accessioned2014-05-20T13:55:06Z-
dc.date.accessioned2016-10-25T17:04:56Z-
dc.date.available2014-05-20T13:55:06Z-
dc.date.available2016-10-25T17:04:56Z-
dc.date.issued2011-03-01-
dc.identifierhttp://dx.doi.org/10.2174/092986711795029528-
dc.identifier.citationCurrent Medicinal Chemistry. Sharjah: Bentham Science Publ Ltd, v. 18, n. 9, p. 1311-1317, 2011.-
dc.identifier.issn0929-8673-
dc.identifier.urihttp://hdl.handle.net/11449/19711-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/19711-
dc.description.abstractTuberculosis is considered a worldwide health problem mainly due to co-infection with HIV and proliferation of multi-drug-resistant strains. The enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria, but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate. The aim of this article is to review the available information on chorismate synthase from Mycobacterium tuberculosis.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.description.sponsorshipINCT-TB-
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)-
dc.format.extent1311-1317-
dc.language.isoeng-
dc.publisherBentham Science Publ Ltd-
dc.sourceWeb of Science-
dc.subjectChorismate synthaseen
dc.subjectMycobacterium tuberculosisen
dc.subjectshikimate pathwayen
dc.titleUnderstanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosisen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionNatl Inst Sci & Technol Immunol INCT III-
dc.description.affiliationSão Paulo State Univ UNESP, CEIS, Dept Biol, Inst Biosci Rio Claro, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationHC FMUSP, INCor, Discipline Allergy & Immunol, São Paulo, Brazil-
dc.description.affiliationNatl Inst Sci & Technol Immunol INCT III, Alegre, RS, Brazil-
dc.description.affiliationUnespSão Paulo State Univ UNESP, CEIS, Dept Biol, Inst Biosci Rio Claro, BR-13506900 Rio Claro, SP, Brazil-
dc.description.sponsorshipIdFAPESP: 06/57122-7-
dc.identifier.doi10.2174/092986711795029528-
dc.identifier.wosWOS:000288986300006-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofCurrent Medicinal Chemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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