ArticleBiophysical journal2006
Structure of core domain of fibril-forming PHF/Tau fragments.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 112 citations in OpenAlex.
- Tau Oligomers Resist Phase Separation.Biomolecules · 2025Article
- "Cyclophilin A" Enzymatic Effect on the Aggregation Behavior of 1N4R Tau Protein: An Overlooked Crucial Determinant that should be Re-considered in Alzheimer's Disease Pathogenesis.Current Alzheimer research · 2024Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- A theoretical study of polymorphism in VQIVYK fibrils.Biophysical journal · 2021Article
- Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6.RSC advances · 2020Article
- Membrane-mediated fibrillation and toxicity of the tau hexapeptide PHF6.The Journal of biological chemistry · 2019Article
- Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation.Alzheimer's research & therapy · 2019Article
- Naphthoquinone Tryptophan Hybrids: A Promising Small Molecule Scaffold for Mitigating Aggregation of Amyloidogenic Proteins and Peptides.Frontiers in cell and developmental biology · 2019Review
- The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulations.Protein science : a publication of the Protein Society · 2012Article
- Heterodivalent linked macrocyclic β-sheets with enhanced activity against Aβ aggregation: two sites are better than one.Journal of the American Chemical Society · 2012Article
- Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.Nature chemical biology · 2012Article
- Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.The journal of physical chemistry. B · 2012Article
- Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein.The Journal of biological chemistry · 2011Article
- Comparison of β-sheets of capped polyalanine with those of the tau-amyloid structures VQIVYK and VQIINK. A density functional theory study.The journal of physical chemistry. B · 2011Article
- X-ray diffraction from intact tau aggregates in human brain tissue.Nuclear instruments & methods in physics research. Section A, Accelerators, spectrometers, detectors and associated equipment · 2011Article
- The Effects of Regularly Spaced Glutamine Substitutions on Alpha-Helical Peptide Structures. A DFT/ONIOM Study.Chemical physics letters · 2011Article
- Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Journal of the American Chemical Society · 2011Article
- Complete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitor.PloS one · 2010Article
- New age of neuroproteomics in Alzheimer's disease research.Cellular and molecular neurobiology · 2009Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Short peptide sequences within the microtubule binding domain of the protein Tau are proposed to be core nucleation sites for formation of amyloid fibrils displaying the paired helical filament (PHF) morphology characteristic of neurofibrillary tangles. To study the structure of these proposed nucleation sites, we analyzed the x-ray diffraction patterns from the assemblies formed by a variety of PHF/tau-related peptide constructs containing the motifs VQIINK (PHF6*) in the second repeat and VQIVYK (PHF6) in the third repeat of tau. Peptides included: tripeptide acetyl-VYK-amide (AcVYK), tetrapeptide acetyl-IVYK-amide (AcPHF4), hexapeptide acetyl-VQIVYK-amide (AcPHF6), and acetyl-GKVQIINKLDLSNVQKDNIKHGSVQIVYKPVDLSKVT-amide (AcTR4). All diffraction patterns showed reflections at spacings of 4.7 A, 3.8 A, and approximately 8-10 A, which are characteristic of an orthogonal unit cell of beta-sheets having dimensions a=9.4 A, b=6.6 A, and c=approximately 8-10 A (where a, b, and c are the lattice constants in the H-bonding, chain, and intersheet directions). The sharp 4.7 A reflections indicate that the beta-crystallites are likely to be elongated along the H-bonding direction and in a cross-beta conformation. The assembly of the AcTR4 peptide, which contains both the PHF6 and PHF6* motifs, consisted of twisted sheets, as indicated by a unique fanning of the diffuse equatorial scattering and meridional accentuation of the (210) reflection at 3.8 A spacing. The diffraction data for AcVYK, AcPHF4, and AcPHF6 all were consistent with approximately 50 A-wide tubular assemblies having double-walls, where beta-strands constitute the walls. In this structure, the peptides are H-bonded together in the fiber direction, and the intersheet direction is radial. The positive-charged lysine residues face the aqueous medium, and tyrosine-tyrosine aromatic interactions stabilize the intersheet (double-wall) layers. This particular contact, which may be involved in PHF fibril formation, is proposed here as a possible aromatic target for anti-tauopathy drugs.
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