Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides
Open Access
- 10 July 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 501 (1) , 19-23
- https://doi.org/10.1016/s0014-5793(01)02606-0
Abstract
Synthetic peptides corresponding to two distinct segments of the subunit interface of the homodimeric enzyme triosephosphate isomerase (residues 9–18, ANWKCNGTLE, peptide I; residues 68–79, KFGNGSYTG...Keywords
This publication has 41 references indexed in Scilit:
- Synthetic Interface Peptides as Inactivators of Multimeric Enzymes: Inhibitory and Conformational Properties of Three Fragments fromLactobacilluscaseiThymidylate SynthaseBiochemistry, 1998
- Crystal Structure of Fructose-1,6-bisphosphate Aldolase from the Human Malaria Parasite Plasmodium falciparum,Biochemistry, 1998
- Inhibiting the assembly of protein—protein interfacesCurrent Opinion in Chemical Biology, 1998
- Triosephosphate isomerase from Plasmodium falciparum:. the crystal structure provides insights into antimalarial drug designStructure, 1997
- The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial designNature Structural & Molecular Biology, 1996
- The inhibition of human immunodeficiency virus proteases by ‘interface peptides’Antiviral Research, 1996
- The Inhibition of HIV-1 Protease by Interface PeptidesBiochemical and Biophysical Research Communications, 1993
- Synthetic “interface” peptides alter dimeric assembly of the HIV 1 and 2 proteasesProtein Science, 1992
- The use of enzymopathic human red cells in the study of malarial parasite glucose metabolismBlood, 1988
- Protein Crystallography and Computer Graphics—toward Rational Drug DesignAngewandte Chemie International Edition in English, 1986