Using evolutionary changes to achieve species-specific inhibition of enzyme action — studies with triosephosphate isomerase
- 1 December 1995
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 2 (12) , 847-855
- https://doi.org/10.1016/1074-5521(95)90091-8
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- Water Requirements in Monomer Folding and Dimerization of Triosephosphate Isomerase in Reverse Micelles. Intrinsic Fluorescence of Conformers Related to ReactivationBiochemistry, 1995
- Selective Inhibition of Trypanosomal Glyceraldehyde-3-phosphate Dehydrogenase by Protein Structure-Based Design: Toward New Drugs for the Treatment of Sleeping SicknessJournal of Medicinal Chemistry, 1994
- Protein crystallography and infectious diseasesProtein Science, 1994
- Inhibition of triosephosphate isomerase from Trypanosoma brucei with cyclic hexapeptidesEuropean Journal of Biochemistry, 1992
- Enzyme catalysis: not different, just betterNature, 1991
- Evolution and the Tertiary Structure of ProteinsAnnual Review of Biophysics and Bioengineering, 1984
- On the three-dimensional structure and catalytic mechanism of triose phosphate isomerasePhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981
- Evolution of enzyme function and the development of catalytic efficiencyBiochemistry, 1976
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975
- Refolding of triose phosphate isomeraseBiochemical Journal, 1973