Structural properties of an amyloid precursor of beta(2)-microglobulin.
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Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic propertiesA regulatable switch mediates self-association in an immunoglobulin foldβ2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesStructural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsThe rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosisCutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicityNMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Systemic amyloidosis: lessons from β2-microglobulin.Sequence determinants of amyloid fibril formationSimulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Proinsulin is refractory to protein fibrillation: topological protection of a precursor protein from cross-beta assembly.Rapid generation of amyloid from native proteins in vitro.Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.FlgM gains structure in living cells.Structures and relative free energies of partially folded states of proteinsFolding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid diseaseMyoglobin forms amyloid fibrils by association of unfolded polypeptide segments.Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis.Structural defects and the diagnosis of amyloidogenic propensityA simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation.The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies.Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.Nucleation of protein fibrillation by nanoparticlesStructure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations.The structural biology of protein aggregation diseases: Fundamental questions and some answersPhysiological temperature has a crucial role in amyloid β in the absence and presence of hydrophobic and hydrophilic nanoparticles.Folding versus aggregation: polypeptide conformations on competing pathwaysMonitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilProtein folding and aggregation into amyloid: the interference by natural phenolic compoundsHacking the code of amyloid formation: the amyloid stretch hypothesis.Conformational properties of beta-PrP.SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease.beta(2)-microglobulin: from physiology to amyloidosis.Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils.The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.
P2860
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P2860
Structural properties of an amyloid precursor of beta(2)-microglobulin.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Structural properties of an amyloid precursor of beta
@nl
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en-gb
type
label
Structural properties of an amyloid precursor of beta
@nl
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en-gb
prefLabel
Structural properties of an amyloid precursor of beta
@nl
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en-gb
P2093
P356
P1476
Structural properties of an amyloid precursor of beta(2)-microglobulin.
@en
P2093
Arnout P Kalverda
Steve W Homans
Victoria J McParland
P304
P356
10.1038/NSB791
P577
2002-05-01T00:00:00Z