%D9%83%D8%B1%D9%8A%D8%B3_%D8%AF%D9%88%D8%A8%D8%B3%D9%88%D9%86%DA%A9%D8%B1%DB%8C%D8%B3_%D8%AF%D8%A7%D8%A8%D8%B3%D9%88%D9%86Category:Christopher_DobsonChristopher_M._DobsonChris_Dobson%DA%A9%D8%B1%DB%8C%D8%B3_%D8%AF%D8%A7%D8%A8%D8%B3%D9%88%D9%86Christopher_DobsonChris_DobsonChris_Dobson%D0%94%D0%BE%D0%B1%D1%81%D0%BE%D0%BD,_%D0%9A%D1%80%D0%B8%D1%81Chris_Dobson%D0%9A%D1%80%D1%96%D1%81%D1%82%D0%BE%D1%84%D0%B5%D1%80_%D0%94%D0%BE%D0%B1%D1%81%D0%BE%D0%BDQ1982431
about
P26
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicityThe extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structuresProtease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanismsChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipThe structural basis of protein folding and its links with human diseaseA camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozymeHigh-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopyA Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal TransductionStructure and properties of a complex of α-synuclein and a single-domain camelid antibodyAtomic structure and hierarchical assembly of a cross- amyloid fibrilA Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril FormationInstability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesisProtein misfolding, functional amyloid, and human diseaseProtein folding and misfoldingInteraction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationProtein misfolding and disease: from the test tube to the organismHigh-sensitivity fluorescence anisotropy detection of protein-folding events: application to alpha-lactalbuminUltrastructural organization of amyloid fibrils by atomic force microscopy.Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivoIn-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cellsTargeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's diseaseAltered aggregation properties of mutant gamma-crystallins cause inherited cataractIdentification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for TauopathiesAmyloid-β oligomers are sequestered by both intracellular and extracellular chaperonesTowards a structural biology of the hydrophobic effect in protein foldingChemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synucleinHeat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar speciesIntermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions.Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.Cytochrome display on amyloid fibrils.Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.Molecular recycling within amyloid fibrils.Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Transition states for protein folding have native topologies despite high structural variability.Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.Calculation of mutational free energy changes in transition states for protein folding.Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.
P50
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P50
description
British chemist
@en
British chemist
@en-ca
British chemist
@en-gb
Brits moleculair bioloog
@nl
Suurbritannia keemik
@et
brit kémikus
@hu
britischer Chemiker, Molekularbiologe und Biophysiker
@de
chimico inglese
@it
chimist britanic
@ro
chimiste britannique
@fr
name
Chris Dobson
@en
Chris Dobson
@es
Chris Dobson
@fi
Chris Dobson
@hu
Chris Dobson
@nb
Chris Dobson
@nl
Chris Dobson
@nn
Chris Dobson
@pt
Chris Dobson
@sl
Christopher Dobson
@it
type
label
Chris Dobson
@en
Chris Dobson
@es
Chris Dobson
@fi
Chris Dobson
@hu
Chris Dobson
@nb
Chris Dobson
@nl
Chris Dobson
@nn
Chris Dobson
@pt
Chris Dobson
@sl
Christopher Dobson
@it
altLabel
Christopher M. Dobson
@en
Christopher Martin Dobson
@en
Christopher Martin Dobson
@it
Sir Christopher Martin Dobson
@en
prefLabel
Chris Dobson
@en
Chris Dobson
@es
Chris Dobson
@fi
Chris Dobson
@hu
Chris Dobson
@nb
Chris Dobson
@nl
Chris Dobson
@nn
Chris Dobson
@pt
Chris Dobson
@sl
Christopher Dobson
@it