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Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein bindingThe RalB-RLIP76 Complex Reveals a Novel Mode of Ral-Effector InteractionIntegrated description of protein dynamics from room-temperature X-ray crystallography and NMRCorrelated inter-domain motions in adenylate kinaseAverage conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.RARRES3 suppresses breast cancer lung metastasis by regulating adhesion and differentiationAccurate scoring of non-uniform sampling schemes for quantitative NMRCofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.Classic Analysis of Biopolymer Dynamics Is Model FreeNMR reveals a dynamic allosteric pathway in thrombin.Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles.Direct Investigation of Slow Correlated Dynamics in Proteins via Dipolar Interactions.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.Correlated motions are a fundamental property of β-sheets.Resonance assignments for the RLIP76 Ral binding domain in its free form and in complex with the small G protein RalB.Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion.Slow Dynamics of Tryptophan-Water Networks in Proteins.Detection of Correlated Protein Backbone and Side-Chain Angle Fluctuations.Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G.1H, 13C and 15N resonance assignments for the active conformation of the small G protein RalB in complex with its effector RLIP76.1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation.Refinement of ensembles describing unstructured proteins using NMR residual dipolar couplings.Utilizing dipole-dipole cross-correlated relaxation for the measurement of angles between pairs of opposing CαHα-CαHα bonds in anti-parallel β-sheets.Kinetics of Conformational Sampling in UbiquitinREVEL and BayesDel outperform other in silico meta-predictors for clinical variant classification
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P50
description
Amerikaans onderzoeker
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forsker
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researcher ORCID ID = 0000-0002-0925-7422
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name
R. Bryn Fenwick
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R. Bryn Fenwick
@nl
Robert Fenwick
@en
Robert Fenwick
@es
Robert Fenwick
@nb
type
label
R. Bryn Fenwick
@ast
R. Bryn Fenwick
@nl
Robert Fenwick
@en
Robert Fenwick
@es
Robert Fenwick
@nb
altLabel
R. Bryn Fenwick
@en
prefLabel
R. Bryn Fenwick
@ast
R. Bryn Fenwick
@nl
Robert Fenwick
@en
Robert Fenwick
@es
Robert Fenwick
@nb
P106
P31
P496
0000-0002-0925-7422