Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease
Structure of tau protein and assembly into paired helical filaments
Spin—spin coupling and the conformational states of peptide systems
Designing conditions for
<i>in vitro</i>
formation of amyloid protofilaments and fibrils
Frontotemporal Dementia and Parkinsonism Linked to Chromosome 17: A New Group of Tauopathies
Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2
Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin‐binding repeats of the τ protein reveal structural features of paired helical filament assembly
MOLMOL: A program for display and analysis of macromolecular structures
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Structural and Functional Differences between 3-Repeat and 4-Repeat Tau Isoforms
Tau proteins with FTDP‐17 mutations have a reduced ability to promote microtubule assembly
Altered conformation of recombinant frontotemporal dementia-17 mutant tau proteins
Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17
Amphipathic helical behavior of the third repeat fragment in the tau microtubule-binding domain, studied by 1H NMR spectroscopy
Prion Protein Peptides Induce .alpha.-Helix to .beta.-Sheet Conformational Transitions
Peptides as Conformational Switch: Medium‐Induced Conformational Transitions of Designed Peptides
Tau Mutations Cause Frontotemporal Dementias
Optimization of Hydrophobic Domains in Peptides that Undergo Transformation from α-Helix to β-Fibril
Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations
Engineering peptides and proteins that undergo α-to-β transitions
Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif (
<sup>306</sup>
VQIVYK
<sup>311</sup>
) forming β structure
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.
A nucleated assembly mechanism of Alzheimer paired helical filaments