Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
about
Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic propertiesβ2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationFolding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation.Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.Inhibition of tau aggregation by a rosamine derivative that blocks tau intermolecular disulfide cross-linking.Structure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations.Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granulesbeta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.Investigation into the role of macrophages in the formation and degradation of beta2-microglobulin amyloid fibrils.Formation of DNA-copolymer fibrils through an amyloid-like nucleation polymerization mechanism.Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrilsThe mechanism of fibril formation of a non-inhibitory serpin ovalbumin revealed by the identification of amyloidogenic core regions.Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond.The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphismDynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation
P2860
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P2860
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@ast
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@en
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@nl
type
label
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@ast
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@en
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@nl
prefLabel
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@ast
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@en
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@nl
P2860
P3181
P356
P1433
P1476
Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro
@en
P2093
S E Radford
P2860
P304
P3181
P356
10.1110/PS.4901
P407
P577
2001-09-01T00:00:00Z