Cited by Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules DOI

Benjamin Falcon, Jasenko Zivanov, Wenjuan Zhang

et al.

Nature, Journal Year: 2019, Volume and Issue: 568(7752), P. 420 - 423

Published: March 20, 2019

Language: Английский

Citations

629

Structures of α-synuclein filaments from multiple system atrophy DOI

Manuel Schweighauser, Yang Shi, Airi Tarutani

et al.

Nature, Journal Year: 2020, Volume and Issue: 585(7825), P. 464 - 469

Published: May 27, 2020

Language: Английский

Citations

606

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis DOI

Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo

et al.

Chemical Reviews, Journal Year: 2021, Volume and Issue: 121(4), P. 2545 - 2647

Published: Feb. 5, 2021

Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural dynamic characterization all species along pathways from monomers to fibrils challenging by experimental computational means because they involve intrinsically disordered proteins most diseases. Yet understanding how amyloid become toxic challenge developing treatment for these Here we review what computer, vitro, vivo, pharmacological experiments tell us about accumulation deposition oligomers (Aβ, tau), α-synuclein, IAPP, superoxide dismutase 1 proteins, which have been mainstream concept underlying Alzheimer's disease (AD), Parkinson's (PD), type II diabetes (T2D), amyotrophic lateral sclerosis (ALS) research, respectively, years.

Language: Английский

Citations

552

Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue DOI

Marius Kollmer, William Close,

Leonie Funk

et al.

Nature Communications, Journal Year: 2019, Volume and Issue: 10(1)

Published: Oct. 29, 2019

Abstract The formation of Aβ amyloid fibrils is a neuropathological hallmark Alzheimer’s disease and cerebral angiopathy. However, the structure from brain tissue poorly understood. Here we report purification meningeal their structural analysis with cryo-electron microscopy. We show that these are polymorphic but consist similarly structured protofilaments. Brain derived right-hand twisted peptide fold differs sharply previously analyzed were formed in vitro. These data underscore importance to use patient-derived when investigating basis disease.

Language: Английский

Citations

497

Novel tau filament fold in corticobasal degeneration DOI

Wenjuan Zhang, Airi Tarutani,

Kathy L. Newell

et al.

Nature, Journal Year: 2020, Volume and Issue: 580(7802), P. 283 - 287

Published: Feb. 12, 2020

Language: Английский

Citations

482

Protein transmission in neurodegenerative disease DOI

Chao Peng, John Q. Trojanowski, Virginia M.‐Y. Lee

et al.

Nature Reviews Neurology, Journal Year: 2020, Volume and Issue: 16(4), P. 199 - 212

Published: March 23, 2020

Language: Английский

Citations

481

Cryo-EM structures of amyloid-β 42 filaments from human brains DOI

Yang Yang, Diana Arseni, Wenjuan Zhang

et al.

Science, Journal Year: 2022, Volume and Issue: 375(6577), P. 167 - 172

Published: Jan. 14, 2022

Hi-res view of human Aβ42 filaments Alzheimer’s disease is characterized by a loss memory and other cognitive functions the filamentous assembly Aβ tau in brain. The peptides into that end at residue 42 central event. Yang et al . used electron cryo–electron microscopy to determine structures from brain (see Perspective Willem Fändrich). They identified two types related S-shaped filaments, each consisting identical protofilaments. These will inform development better vitro animal models, inhibitors assembly, imaging agents with increased specificity sensitivity. —SMH

Language: Английский

Citations

360

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains DOI

Tamta Arakhamia,

Christina E. Lee,

Yari Carlomagno

et al.

Cell, Journal Year: 2020, Volume and Issue: 180(4), P. 633 - 644.e12

Published: Feb. 1, 2020

Language: Английский

Citations

348

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy DOI

Ricardo Guerrero-Ferreira, Nicholas M. I. Taylor, Ana‐Andreea Arteni

et al.

eLife, Journal Year: 2019, Volume and Issue: 8

Published: Dec. 9, 2019

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure fibrils (residues 1–121), composed two protofibrils that connected via densely-packed interface formed by residues 50–57 (Guerrero-Ferreira, eLife 218;7:e36402). We here report new polymorphic atomic structures termed polymorphs 2a and 2b, at 3.0 Å 3.4 resolution, respectively. These show radically different compared to previously polymorphs. The have 10 nm fibril diameter protofilaments which interact intermolecular salt-bridges between amino acids K45, E57 (polymorph 2a) or E46 2b). non-amyloid component (NAC) region is fully buried non-described interactions with N-terminus. A hydrophobic cleft, location familial PD mutation sites, nature protofilament now invite formulate hypotheses about formation, growth stability.

Language: Английский

Citations

292

The expanding amyloid family: Structure, stability, function, and pathogenesis DOI

M.R. Sawaya, Michael P. Hughes,

José A. Rodríguez

et al.

Cell, Journal Year: 2021, Volume and Issue: 184(19), P. 4857 - 4873

Published: Sept. 1, 2021

Language: Английский

Citations

279