about
XYLab: an interactive plotting tool for mixed multivariate data observation and interpretation.Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes.Quantitative measurement of protein stability from unfolding equilibria monitored with the fluorescence maximum wavelength.Prevention of amyloid-like aggregation as a driving force of protein evolution.Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregationα-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios.The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathwayAmyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism.Improving the stability of an antibody variable fragment by a combination of knowledge-based approaches: validation and mechanisms.
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P50
description
Forscher
@de
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
研究者
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name
Elodie Monsellier
@ast
Elodie Monsellier
@en
Elodie Monsellier
@es
Elodie Monsellier
@nl
type
label
Elodie Monsellier
@ast
Elodie Monsellier
@en
Elodie Monsellier
@es
Elodie Monsellier
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prefLabel
Elodie Monsellier
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Elodie Monsellier
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Elodie Monsellier
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Elodie Monsellier
@nl
P106
P1153
23094790400
P31
P496
0000-0001-7944-7531