Structure of core domain of fibril-forming PHF/Tau fragments.
about
X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's diseaseComplete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitorFormation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentX-ray diffraction from intact tau aggregates in human brain tissuePhenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Butyrylcholinesterase attenuates amyloid fibril formation in vitro.Comparison of β-sheets of capped polyalanine with those of the tau-amyloid structures VQIVYK and VQIINK. A density functional theory study.The Effects of Regularly Spaced Glutamine Substitutions on Alpha-Helical Peptide Structures. A DFT/ONIOM StudyUnderstanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau proteinHeterodivalent linked macrocyclic β-sheets with enhanced activity against Aβ aggregation: two sites are better than one.Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.Molecular origin of the self-assembly of lanreotide into nanotubes: a mutational approach.Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulationsThe fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush.Use of biomolecular templates for the fabrication of metal nanowires.Structural principles of tau and the paired helical filaments of Alzheimer's disease.Self assembly of short aromatic peptides into amyloid fibrils and related nanostructures.Cytoplasmic domain of zebrafish myelin protein zero: adhesive role depends on beta-conformation.Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy.The "jaws" of the tau-microtubule interaction.The generic amyloid formation inhibition effect of a designed small aromatic β-breaking peptide
P2860
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P2860
Structure of core domain of fibril-forming PHF/Tau fragments.
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Structure of core domain of fibril-forming PHF/Tau fragments.
@ast
Structure of core domain of fibril-forming PHF/Tau fragments.
@en
Structure of core domain of fibril-forming PHF/Tau fragments.
@nl
type
label
Structure of core domain of fibril-forming PHF/Tau fragments.
@ast
Structure of core domain of fibril-forming PHF/Tau fragments.
@en
Structure of core domain of fibril-forming PHF/Tau fragments.
@nl
prefLabel
Structure of core domain of fibril-forming PHF/Tau fragments.
@ast
Structure of core domain of fibril-forming PHF/Tau fragments.
@en
Structure of core domain of fibril-forming PHF/Tau fragments.
@nl
P2093
P2860
P1433
P1476
Structure of core domain of fibril-forming PHF/Tau fragments
@en
P2093
Deepak Sharma
Hideyo Inouye
Warren J Goux
P2860
P304
P356
10.1529/BIOPHYSJ.105.070136
P407
P577
2005-12-09T00:00:00Z