A point mutation at the subunit interface of hypoxanthine-guanine-xanthine phosphoribosyltransferase impairs activity: role of oligomerization in catalysis
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(02)02826-0/fullpdf
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1. Allopurinol ribonucleoside as an antileishmanial agent. Biological effects, metabolism, and enzymatic phosphorylation.
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1. Role of W181 in modulating kinetic properties of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase;Proteins: Structure, Function, and Bioinformatics;2016-08-13
2. Product Release Pathways in Human and Plasmodium falciparum Phosphoribosyltransferase;Journal of Chemical Information and Modeling;2016-07-21
3. Structural and dynamical correlations in PfHGXPRT oligomers: A molecular dynamics simulation study;Journal of Biomolecular Structure and Dynamics;2016-04-25
4. Slow ligand-induced conformational switch increases the catalytic rate in Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase;Molecular BioSystems;2015
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