Understanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorArcuri, H. A.
dc.creatorPalma, Mario Sergio
dc.date2014-05-20T13:55:06Z
dc.date2016-10-25T17:04:56Z
dc.date2014-05-20T13:55:06Z
dc.date2016-10-25T17:04:56Z
dc.date2011-03-01
dc.date.accessioned2017-04-05T21:12:09Z
dc.date.available2017-04-05T21:12:09Z
dc.identifierCurrent Medicinal Chemistry. Sharjah: Bentham Science Publ Ltd, v. 18, n. 9, p. 1311-1317, 2011.
dc.identifier0929-8673
dc.identifierhttp://hdl.handle.net/11449/19711
dc.identifierhttp://acervodigital.unesp.br/handle/11449/19711
dc.identifier10.2174/092986711795029528
dc.identifierWOS:000288986300006
dc.identifierhttp://dx.doi.org/10.2174/092986711795029528
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/865509
dc.descriptionTuberculosis 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.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationCurrent Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectChorismate synthase
dc.subjectMycobacterium tuberculosis
dc.subjectshikimate pathway
dc.titleUnderstanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis
dc.typeOtro


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