about
Structural and dynamical insights into the membrane-bound α-synuclein.A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures.Single-molecule biophysics: at the interface of biology, physics and chemistryDirect and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogsChain collapse of an amyloidogenic intrinsically disordered protein.Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.Nanoscopic Amyloid Pores Formed via Stepwise Protein Assembly.Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins.Structure and dynamics of a molecular hydrogel derived from a tripodal cholamide.Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH.Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface.Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin.Site-Specific Fluorescence Depolarization Kinetics Distinguishes the Amyloid Folds Responsible for Distinct Yeast Prion Strains.pH-Responsive Mechanistic Switch Regulates the Formation of Dendritic and Fibrillar Nanostructures of a Functional Amyloid.Confined Water in Amyloid-Competent Oligomers of the Prion Protein.Water Rearrangements upon Disorder-to-Order Amyloid Transition.Conformational Switching and Nanoscale Assembly of Human Prion Protein into Polymorphic Amyloids via Structurally Labile Oligomers.Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin.Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgAFemtosecond Hydration Map of Intrinsically Disordered α-SynucleinSynergistic Amyloid Switch Triggered by Early Heterotypic Oligomerization of Intrinsically Disordered α-Synuclein and TauHydrophobic Pockets in a Nonpolymeric Aqueous Gel: Observation of such a Gelation Process by Color Change We thank the Jawaharlal Nehru Center for Advanced Scientific Research (Bangalore), and Mitokor, Inc. (San Diego) for supporting this work throuFacile synthesis, aggregation behavior, and cholesterol solubilization ability of avicholic acidpH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescenceCharacterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamicsInsights into the mechanism of aggregation and fibril formation from bovine serum albuminKinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopyNanoscale Fluorescence Imaging of Single Amyloid FibrilsOrdered water within the collapsed globules of an amyloidogenic intrinsically disordered proteinStudying backbone torsional dynamics of intrinsically disordered proteins using fluorescence depolarization kineticsFormation of Heterotypic Amyloids: α-Synuclein in Co-AggregationLiquid-Liquid Phase Separation Is Driven by Large-Scale Conformational Unwinding and Fluctuations of Intrinsically Disordered Protein MoleculesIntermolecular Charge-Transfer Modulates Liquid-Liquid Phase Separation and Liquid-to-Solid Maturation of an Intrinsically Disordered pH-Responsive DomainPreferential Recruitment of Conformationally Distinct Amyloid-β Oligomers by the Intrinsically Disordered Region of the Human Prion ProteinFluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered Proteins
P50
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P50
description
researcher
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wetenschapper
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հետազոտող
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name
Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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সম্রাট মুখোপাধ্যায়
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type
label
Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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সম্রাট মুখোপাধ্যায়
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prefLabel
Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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Samrat Mukhopadhyay
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সম্রাট মুখোপাধ্যায়
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P106
P1153
56269154000
P31
P496
0000-0003-1242-9958