@article {Guido:2009:1570-1808:210,
title = "Kinetic and Crystallographic Studies on Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in Complex with Iodoacetate",
journal = "Letters in Drug Design & Discovery",
parent_itemid = "infobike://ben/lddd",
publishercode ="ben",
year = "2009",
volume = "6",
number = "3",
publication date ="2009-04-01T00:00:00",
pages = "210-214",
itemtype = "ARTICLE",
issn = "1570-1808",
url = "https://www.ingentaconnect.com/content/ben/lddd/2009/00000006/00000003/008aj",
doi = "doi:10.2174/157018009787847774",
keyword = "X-ray crystallography, Trypanosoma cruzi, Parasitic infections, Enzyme, Inhibitors, Glyceraldehyde-3-phosphate dehydrogenase",
author = "Guido, Rafael V.C. and Balliano, Tatiane L. and Andricopulo, Adriano D. and Oliva, Glaucius",
abstract = "Kinetic and crystallographic studies on the formation of the complex between iodoacetate and the enzyme glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi were conducted in order to investigate the mechanistic and structural basis underlying enzyme inactivation. The crystallographic complex reveal important structural features useful for the design of novel inhibitors. ",
}