about
The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteinsStructure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complexWeak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular RecognitionCorrelated inter-domain motions in adenylate kinaseLow-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Protein structure determination from NMR chemical shiftsFast and accurate predictions of protein NMR chemical shifts from interatomic distances.Toward an atomistic description of the urea-denatured state of proteins.Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.Structural analysis of substance P using molecular dynamics and NMR spectroscopy.Synthetic ligands able to interact with the p53 tetramerization domain. Towards understanding a protein surface recognition event.Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.RARRES3 suppresses breast cancer lung metastasis by regulating adhesion and differentiationLocal cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.FoxA and LIPG endothelial lipase control the uptake of extracellular lipids for breast cancer growthUnderstanding biomolecular motion, recognition, and allostery by use of conformational ensembles.Structural aspects of amyloid formation.Understanding protein dynamics using conformational ensembles.Human serum albumin, systemic inflammation, and cirrhosis.Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.Toward the discovery of effective polycyclic inhibitors of alpha-synuclein amyloid assembly.Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.Electrostatic effects in filamentous protein aggregation.The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.Validated Conformational Ensembles Are Key for the Successful Prediction of Protein Complexes.EPI-001, A Compound Active against Castration-Resistant Prostate Cancer, Targets Transactivation Unit 5 of the Androgen Receptor.CPEB4 is regulated during cell cycle by ERK2/Cdk1-mediated phosphorylation and its assembly into liquid-like droplets.Development of Bag-1L as a therapeutic target in androgen receptor-dependent prostate cancer.Population of nonnative states of lysozyme variants drives amyloid fibril formation.Sequence Context Influences the Structure and Aggregation Behavior of a PolyQ Tract.Identification of fibril-like tertiary contacts in soluble monomeric α-synucleinTime averaging of NMR chemical shifts in the MLF peptide in the solid state.Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.Solution structure of the antitumor candidate trunkamide A by 2D NMR and restrained simulated annealing methods.Correlated motions are a fundamental property of β-sheets.A tetraguanidinium ligand binds to the surface of the tetramerization domain of protein P53.A new class of foldamers based on cis-gamma-amino-L-proline.Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation.Peptide nanofibrils boost retroviral gene transfer and provide a rapid means for concentrating viruses.
P50
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P50
description
hulumtues
@sq
researcher
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ricercatore
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wetenschapper
@nl
հետազոտող
@hy
name
Xavier Salvatella
@ast
Xavier Salvatella
@en
Xavier Salvatella
@es
Xavier Salvatella
@nl
Xavier Salvatella
@sl
type
label
Xavier Salvatella
@ast
Xavier Salvatella
@en
Xavier Salvatella
@es
Xavier Salvatella
@nl
Xavier Salvatella
@sl
prefLabel
Xavier Salvatella
@ast
Xavier Salvatella
@en
Xavier Salvatella
@es
Xavier Salvatella
@nl
Xavier Salvatella
@sl
P214
P244
P1053
C-7337-2008
P106
P1153
6602617527
P1580
P21
P214
P244
n2010182020
P31
P3829
P496
0000-0002-8371-4185
P735
P7859
lccn-n2010182020