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Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interfaceStructural and biochemical characterization of a recombinant triosephosphate isomerase from Rhipicephalus (Boophilus) microplusIdentification of Amino Acids that Account for Long-Range Interactions in Two Triosephosphate Isomerases from Pathogenic TrypanosomesDifferent contribution of conserved amino acids to the global properties of triosephosphate isomerasesDifferences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomesThe stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteinsA ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populationsIdentification of the critical residues responsible for differential reactivation of the triosephosphate isomerases of two trypanosomesThe importance of arginine codons AGA and AGG for the expression in E. coli of triosephosphate isomerase from seven different species.Massive screening yields novel and selective Trypanosoma cruzi triosephosphate isomerase dimer-interface-irreversible inhibitors with anti-trypanosomal activity.Insular cortex lesions impair the acquisition of conditioned immunosuppression.The interfaces of oligomeric proteins as targets for drug design against enzymes from parasites.Modeling the interaction between quinolinate and the receptor for advanced glycation end products (RAGE): relevance for early neuropathological processes3-H-[1,2]Dithiole as a New Anti-Trypanosoma cruzi Chemotype: Biological and Mechanism of Action Studies.Development of bis-thiazoles as inhibitors of triosephosphate isomerase from Trypanosoma cruzi. Identification of new non-mutagenic agents that are active in vivo.Potent and Selective Inhibitors of Trypanosoma cruzi Triosephosphate Isomerase with Concomitant Inhibition of Cruzipain: Inhibition of Parasite Growth through Multitarget Activity.The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Multi-Anti-Parasitic Activity of Arylidene Ketones and Thiazolidene Hydrazines against Trypanosoma cruzi and Leishmania spp.Causes of the decrease in fluorescence due to proteolysis of alpha-casein.Early expression of the receptor for advanced glycation end products in a toxic model produced by 6-hydroxydopamine in the rat striatum.Factors that control the reactivity of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi.Catalysis and stability of triosephosphate isomerase from Trypanosoma brucei with different residues at position 14 of the dimer interface. Characterization of a catalytically competent monomeric enzyme.Susceptibility to proteolysis of triosephosphate isomerase from two pathogenic parasites: characterization of an enzyme with an intact and a nicked monomer.Highly specific inactivation of triosephosphate isomerase from Trypanosoma cruzi.Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers.Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.An unusual triosephosphate isomerase from the early divergent eukaryote Giardia lamblia.1,2,4-thiadiazol-5(4H)-ones: a new class of selective inhibitors of Trypanosoma cruzi triosephosphate isomerase. Study of the mechanism of inhibition.Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface.New chemotypes as Trypanosoma cruzi triosephosphate isomerase inhibitors: a deeper insight into the mechanism of inhibition.Pyruvate kinase revisited: the activating effect of K+.Key residues of loop 3 in the interaction with the interface residue at position 14 in triosephosphate isomerase from Trypanosoma brucei.Loosely packed papain prosegment displays inhibitory activity.Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes.Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi.Polymorphism analysis of the internal transcribed spacer and small subunit of ribosomal RNA genes of Leishmania mexicana.Interplay between Protein Thermal Flexibility and Kinetic Stability.Derivatization of the Interface Cysteine of Triosephosphate Isomerase fromTrypanosoma bruceiandTrypanosoma cruzias Probe of the Interrelationship between the Catalytic Sites and the Dimer Interface†A strategy based on thermal flexibility to design triosephosphate isomerase proteins with increased or decreased kinetic stability
P50
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P50
description
onderzoeker
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researcher ORCID ID = 0000-0003-0810-1159
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name
Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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type
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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prefLabel
Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
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Ruy Pérez-Montfort
@nl
P106
P1153
7004155242
P21
P31
P496
0000-0003-0810-1159