| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10915282 | Mutation Research/Reviews in Mutation Research | 2013 | 16 Pages |
Abstract
Structural basis for destabilization of human inosine triphosphate pyrophosphatase (ITPA) polymorphic variant Pro32Thr. The cavities in the hydrophobic core (wild-type is red and P32T mutant is blue) are shown relative to the enzyme active site (indicated with the nucleotide position).
Keywords
SSBXTPBase analogsHGPRTDSBITPATPMTMEFInosine triphosphateinosine triphosphate pyrophosphataseNucleotide poolThiopurine S-methyltransferaseSaccharomyces cerevisiaedouble-strand breaksingle-strand breakdominant negativePharmacogeneticsmouse embryonic fibroblastshypoxanthine-guanine phosphoribosyltransferaseITPProtein stabilityHAp
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Cancer Research
Authors
Peter D. Simone, Youri I. Pavlov, Gloria E.O. Borgstahl,