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dc.contributor.authorJamabo, Miebaka-
dc.description.abstractAfrican Trypanosomiasis is a neglected tropical disease caused by Trypanosoma brucei (T. brucei) and is spread by the tsetse fly in sub-Saharan Africa. The disease is fatal if left untreated and the currently approved drugs for treatment are toxic and difficult to administer. The trypanosome must survive in the insect vector and its mammalian host, and to adapt to these different conditions, the parasite relies on molecular chaperones called heat shock proteins. Heat shock proteins mediate the folding of newly synthesized proteins as well as prevent misfolding of proteins under normal conditions and during stressful conditions. Heat shock protein 90 (Hsp90) is one of the major molecular chaperones of the stress response at the cellular level. It functions with other chaperones and co-chaperones and inhibition of its interactions is being explored as a potential therapeutic target for numerous diseases. This study provides an in-silico overview of Hsp90 and its co-chaperones in both T. brucei brucei and T. brucei gambiense in relation to human and other kinetoplastid
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.subjectTrypanosoma bruceivi
dc.subjectsinh hóavi
dc.titleThe Hsp90 chaperone system from the African trypanosome, Trypanosoma bruceivi
dc.typeJournal articlevi
dc.description.noteCC BY 4.0vi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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