A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils
about
A regulatable switch mediates self-association in an immunoglobulin foldConformational Conversion during Amyloid Formation at Atomic Resolutionβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHThe impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Characterization 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 fibrilspH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersStructural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growthGlobular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscapebeta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomesAn anti-Aβ (amyloid β) single-chain variable fragment prevents amyloid fibril formation and cytotoxicity by withdrawing Aβ oligomers from the amyloid pathway.Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain.Intermolecular alignment in β2-microglobulin amyloid fibrils.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril FormationDelineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.Fibril fragmentation enhances amyloid cytotoxicity.Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
P2860
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P2860
A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
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2008年论文
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name
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@ast
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en-gb
type
label
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@ast
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en-gb
prefLabel
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@ast
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en-gb
P2860
P356
P1476
A common beta-sheet architectu ...... -microglobulin amyloid fibrils
@en
P2093
Glenys A Tennent
P2860
P304
17279-17286
P356
10.1074/JBC.M710351200
P407
P577
2008-04-18T00:00:00Z