about
Intertwined dimeric structure for the SH3 domain of the c-Src tyrosine kinase induced by polyethylene glycol bindingThe structural and energetic basis for high selectivity in a high-affinity protein-protein interactionParalogous chemoreceptors mediate chemotaxis towards protein amino acids and the non-protein amino acid gamma-aminobutyrate (GABA)Molecular Binding Mechanism of TtgR Repressor to Antibiotics and AntimicrobialsParalogous Regulators ArsR1 and ArsR2 of Pseudomonas putida KT2440 as a Basis for Arsenic Biosensor DevelopmentMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry.A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.
P50
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P50
description
hulumtues
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onderzoeker
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researcher
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հետազոտող
@hy
name
Bertrand Morel
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Bertrand Morel
@en
Bertrand Morel
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Bertrand Morel
@nl
Bertrand Morel
@sl
type
label
Bertrand Morel
@ast
Bertrand Morel
@en
Bertrand Morel
@es
Bertrand Morel
@nl
Bertrand Morel
@sl
prefLabel
Bertrand Morel
@ast
Bertrand Morel
@en
Bertrand Morel
@es
Bertrand Morel
@nl
Bertrand Morel
@sl