Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB
about
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroIonic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone proteinDesigned protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assemblyUsing simple artificial intelligence methods for predicting amyloidogenesis in antibodiesSequence determinants of amyloid fibril formationBiophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B.Construction and characterization of protein libraries composed of secondary structure modules.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Evidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion aggregates.Charge transport and intrinsic fluorescence in amyloid-like fibrils.Expression and characterization of Cryptococcus neoformans recombinant App1.Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation.Freezing of a fish antifreeze protein results in amyloid fibril formation.Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein.Amyloidogenic sequences in native protein structures.Mutational analysis of the propensity for amyloid formation by a globular protein.Competing intrachain interactions regulate the formation of beta-sheet fibrils in bovine PrP peptides.Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.Understanding the sequence determinants of conformational switching using protein design.Sonication of proteins causes formation of aggregates that resemble amyloid.Molecular tweezers for lysine and arginine - powerful inhibitors of pathologic protein aggregationAmyloid fibrils from the mammalian protein prothymosin alpha.The role of hydrophobic interactions in amyloidogenesis: example of prion-related polypeptides.Folding of prion protein to its native alpha-helical conformation is under kinetic control.Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptideDifferent morphology of amyloid fibrils originating from agitated and non-agitated conditions
P2860
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P2860
Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@ast
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@en
type
label
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@ast
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@en
prefLabel
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@ast
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@en
P2093
P2860
P356
P1433
P1476
Formation of amyloid fibrils b ...... terial cold shock protein CspB
@en
P2093
C M Dobson
D K Wilkins
M C Pitkeathly
P2860
P304
P356
10.1110/PS.8.6.1350
P577
1999-06-01T00:00:00Z