Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid.
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Assessing the causes and consequences of co-polymerization in amyloid formationStability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-merComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationCharacterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequenceInvestigation of the molecular similarity in closely related protein systems: The PrP case study.Identification of fibrillogenic regions in human triosephosphate isomerase.Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanolTwo amyloid States of the prion protein display significantly different folding patternsThe polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivityFluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutionsInsights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometryAmyloid structure and assembly: insights from scanning transmission electron microscopy.Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrilsStacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.Orthogonal cross-seeding: an approach to explore protein aggregates in living cells.Mysterious oligomerization of the amyloidogenic proteinsCharacterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.The interconversion between a flexible β-sheet and a fibril β-arrangement constitutes the main conformational event during misfolding of PSD95-PDZ3 domainDirect three-dimensional visualization of membrane disruption by amyloid fibrilsKinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Structural complexity of a composite amyloid fibril.Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau proteinLocalization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.A three-stage kinetic model of amyloid fibrillation.Nucleation of protein fibrillation by nanoparticlesInsights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation.A Protocol for the Design of Protein and Peptide Nanostructure Self-Assemblies Exploiting Synthetic Amino Acids.Solvent-induced tuning of internal structure in a protein amyloid protofibril.Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrilsSystematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assemblyInstantaneous amyloid fibril formation of alpha-synuclein from the oligomeric granular structures in the presence of hexaneFolding versus aggregation: polypeptide conformations on competing pathways
P2860
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P2860
Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
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2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
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@yue
2005年學術文章
@zh-hant
name
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en-gb
Competing pathways determine f ...... a2-microglobulin into amyloid.
@nl
type
label
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en-gb
Competing pathways determine f ...... a2-microglobulin into amyloid.
@nl
prefLabel
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en-gb
Competing pathways determine f ...... a2-microglobulin into amyloid.
@nl
P2093
P1476
Competing pathways determine f ...... a2-microglobulin into amyloid.
@en
P2093
D Alastair Smith
Isobel J Morten
Neil H Thomson
Walraj S Gosal
P304
P356
10.1016/J.JMB.2005.06.040
P407
P577
2005-08-01T00:00:00Z