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dc.contributor.authorOppenheimer, Michelle
dc.contributor.authorValenciano, Ana L.
dc.contributor.authorSobrado, Pablo
dc.identifier.citationMichelle Oppenheimer, Ana L. Valenciano, and Pablo Sobrado, “Biosynthesis of Galactofuranose in Kinetoplastids: Novel Therapeutic Targets for Treating Leishmaniasis and Chagas' Disease,” Enzyme Research, vol. 2011, Article ID 415976, 13 pages, 2011. doi:10.4061/2011/415976
dc.description.abstractCell surface proteins of parasites play a role in pathogenesis by modulating mammalian cell recognition and cell adhesion during infection. β-Galactofuranose (Galf) is an important component of glycoproteins and glycolipids found on the cell surface of Leishmania spp. and Trypanosoma cruzi. β-Galf-containing glycans have been shown to be important in parasite-cell interaction and protection against oxidative stress. Here, we discuss the role of β-Galf in pathogenesis and recent studies on the Galf-biosynthetic enzymes: UDP-galactose 4′ epimerase (GalE), UDP-galactopyranose mutase (UGM), and UDP-galactofuranosyl transferase (GalfT). The central role in Galf formation, its unique chemical mechanism, and the absence of a homologous enzyme in humans identify UGM as the most attractive drug target in the β-Galf-biosynthetic pathway in protozoan parasites.
dc.rightsCreative Commons Attribution 4.0 International
dc.titleBiosynthesis of Galactofuranose in Kinetoplastids: Novel Therapeutic Targets for Treating Leishmaniasis and Chagas' Diseaseen_US
dc.typeArticle - Refereed
dc.description.versionPeer Reviewed
dc.rights.holderCopyright © 2011 Michelle Oppenheimer et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Creative Commons Attribution 4.0 International
License: Creative Commons Attribution 4.0 International