A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
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Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation.Identification of fibrillogenic regions in human triosephosphate isomerase.Apoferritin fibers: a new template for 1D fluorescent hybrid nanostructures.Protein self-association in solution: the bovine beta -lactoglobulin dimer and octamer.Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils.Role of small oligomers on the amyloidogenic aggregation free-energy landscapeElucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionThe regulatory subunit of PKA-I remains partially structured and undergoes β-aggregation upon thermal denaturation.polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reactionThermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.What drives amyloid molecules to assemble into oligomers and fibrils?A monomer-trimer model supports intermittent glucagon fibril growth.Coarse-grained strategy for modeling protein stability in concentrated solutions. III: directional protein interactionsFibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Simple moment-closure model for the self-assembly of breakable amyloid filaments.Temperature-induced dissociation of Abeta monomers from amyloid fibril.Analytical Description of Degradation-Relaxation Transformations in Nanoinhomogeneous Spinel Ceramics.Aqueous urea solution destabilizes Abeta(16-22) oligomers.Label-free imaging of amyloids using their intrinsic linear and nonlinear optical properties.Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI.Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study.Glycerol inhibits the primary pathways and transforms the secondary pathway of insulin aggregation.Conformational transitions in beta-lactoglobulin induced by cationic amphiphiles: equilibrium studies.The effect of concentration, temperature and stirring on hen egg white lysozyme amyloid formation.Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.Protein fibrillation lag times during kinetic inhibition.Analysis of the kinetics of folding of proteins and peptides using circular dichroism.Flow-assisted assembly of nanostructured protein microfibers.A statistical-mechanical theory of fibril formation in dilute protein solutions.Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II).Cysteine inhibits the fibrillisation and cytotoxicity of amyloid-β 40 and 42: implications for the contribution of the thiophilic interaction.Stimulation of insulin fibrillation by urea-induced intermediates.Non-native states of bovine beta-lactoglobulin induced by acetonitrile: pH-dependent unfolding of the two genetic variants A and B.Analysing Cytochrome c Aggregation and Fibrillation upon Interaction with Acetonitrile: an in Vitro Study.Controlled Supramolecular Self-Assembly of Super-charged β-Lactoglobulin A-PEG Conjugates into Nanocapsules.Asymptotic solutions of the Oosawa model for the length distribution of biofilaments.Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin.Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level InteractionsInhibiting, promoting, and preserving stability of functional proteinfibrils
P2860
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P2860
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@ast
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@en
type
label
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@ast
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@en
prefLabel
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@ast
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@en
P2860
P356
P1433
P1476
A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.
@en
P2093
Daizo Hamada
P2860
P304
P356
10.1110/PS.0217702
P50
P577
2002-10-01T00:00:00Z