Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer's and Pick's diseases (Q61799266)

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21 April 2020

title

Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer's and Pick's diseases (English)

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21 April 2020

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21 April 2020

Benjamin Falcon

2

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21 April 2020

Sjors Scheres

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21 April 2020

author name string

Juan Fan

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21 April 2020

R Anthony Crowther

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21 April 2020

Michel Goedert

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21 April 2020

Alexey G Murzin

3

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21 April 2020

language of work or name

English

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publication date

5 February 2019

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21 April 2020

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21 April 2020

volume

8

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The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease

21 April 2020

cites work

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12 December 2020

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Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro

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Straight and paired helical filaments in Alzheimer disease have a common structural unit

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Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

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RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

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Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau.

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Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation.

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Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution

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Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly

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Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments

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Accelerated filament formation from tau protein with specific FTDP-17 missense mutations.

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Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments

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Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau.

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Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure

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Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias

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In vitro assembly of tau protein: mapping the regions involved in filament formation

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Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure

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MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

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12 December 2020

Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis

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12 December 2020

Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments

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12 December 2020

Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

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12 December 2020

Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure

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12 December 2020

Refinement of macromolecular structures by the maximum-likelihood method

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12 December 2020

Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells

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12 December 2020

Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins

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12 December 2020

Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions

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The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis.

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In vitro tau fibrillization: mapping protein regions.

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Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy

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Characterization of two VQIXXK motifs for tau fibrillization in vitro

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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12 December 2020

A novel MAPT mutation (P301T) associated with familial frontotemporal dementia.

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12 December 2020

Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy

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12 December 2020

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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12 December 2020

Features and development of Coot

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12 December 2020

Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease

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12 December 2020

Variations in filament conformation dictate seeding barrier between three- and four-repeat tau

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12 December 2020

Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein

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12 December 2020

The dynamic structure of filamentous tau

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12 December 2020

Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau.

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12 December 2020

β-Sheet core of tau paired helical filaments revealed by solid-state NMR.

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12 December 2020

RELION: implementation of a Bayesian approach to cryo-EM structure determination

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12 December 2020

High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy

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12 December 2020

Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein

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12 December 2020

Conformation determines the seeding potencies of native and recombinant Tau aggregates

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12 December 2020

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A Two-Component Adhesive: Tau Fibrils Arise from a Combination of a Well-Defined Motif and Conformationally Flexible Interactions.

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Helical reconstruction in RELION.

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12 December 2020

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Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.

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12 December 2020

Cryo-EM structures of tau filaments from Alzheimer's disease.

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12 December 2020

Propagation of Tau Aggregates and Neurodegeneration

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12 December 2020

A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells

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12 December 2020

Fibril structure of amyloid-β(1-42) by cryo-electron microscopy

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12 December 2020

Structure-based inhibitors of tau aggregation

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12 December 2020

Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments

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12 December 2020

Near-atomic model of microtubule-tau interactions

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12 December 2020

Cryo-EM structure of alpha-synuclein fibrils

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12 December 2020

Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy

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12 December 2020

Structures of filaments from Pick's disease reveal a novel tau protein fold

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12 December 2020

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

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12 December 2020

Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms

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12 December 2020

Tau filaments from multiple cases of sporadic and inherited Alzheimer's disease adopt a common fold

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12 December 2020

New tools for automated high-resolution cryo-EM structure determination in RELION-3

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12 December 2020

Identifiers

DOI

10.7554/ELIFE.43584

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30720432%20AND%20SRC:MED&resulttype=core&format=json

21 April 2020

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21 April 2020

PubMed publication ID

30720432

1 reference