Species-Specific Inhibition of Homologous Enzymes by Modification of Nonconserved Amino Acids Residues. The cysteine residues of triosephosphate isomerase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.0114t.x/fullpdf
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1. Protein crystallography and infectious diseases
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4. Selective Inhibition of Trypanosomal Glyceraldehyde-3-phosphate Dehydrogenase by Protein Structure-Based Design: Toward New Drugs for the Treatment of Sleeping Sickness
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1. Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes;PLOS ONE;2018-01-17
2. A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease;Proteins: Structure, Function, and Bioinformatics;2017-04-27
3. Identification of the critical residues responsible for differential reactivation of the triosephosphate isomerases of two trypanosomes;Open Biology;2016-10
4. The E104D mutation increases the susceptibility of human triosephosphate isomerase to proteolysis. Asymmetric cleavage of the two monomers of the homodimeric enzyme;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2013-12
5. Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies;International Journal of Molecular Sciences;2012-10-12
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