Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies DOI Creative Commons
Galina Limorenko, Hilal A. Lashuel

Chemical Society Reviews, Journal Year: 2021, Volume and Issue: 51(2), P. 513 - 565

Published: Dec. 10, 2021

We discuss novel approaches for embracing and reproducing complexity of Tau pathology required developing disease-relevant diagnostics effective therapies.

Language: Английский

Structure-based classification of tauopathies DOI
Yang Shi, Wenjuan Zhang, Yang Yang

et al.

Nature, Journal Year: 2021, Volume and Issue: 598(7880), P. 359 - 363

Published: Sept. 29, 2021

Language: Английский

Citations

624
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
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

485
Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains DOI Creative Commons

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
Tau molecular diversity contributes to clinical heterogeneity in Alzheimer’s disease DOI
Simon Dujardin,

Caitlin Commins,

Aurélien Lathuilière

et al.

Nature Medicine, Journal Year: 2020, Volume and Issue: 26(8), P. 1256 - 1263

Published: June 22, 2020

Language: Английский

Citations

342
The expanding amyloid family: Structure, stability, function, and pathogenesis DOI Creative Commons
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
Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation DOI Creative Commons
Carolina Alquézar, Shruti Arya, Aimee W. Kao

et al.

Frontiers in Neurology, Journal Year: 2021, Volume and Issue: 11

Published: Jan. 7, 2021

Post-translational modifications (PTMs) on tau have long been recognized as affecting protein function and contributing to neurodegeneration. The explosion of information potential observed PTMs provides an opportunity better understand these in the context homeostasis, which becomes perturbed with aging disease. Prevailing views regard a that undergoes abnormal phosphorylation prior its accumulation into toxic aggregates implicated Alzheimer's disease (AD) other tauopathies. However, may, fact, represent part normal but interrupted catabolism protein. In addition phosphorylation, another forms post-translational modification including (but not limited to), acetylation, ubiquitination, glycation, glycosylation, SUMOylation, methylation, oxidation, nitration. A holistic appreciation how regulate during health are potentially hijacked remains elusive. Recent studies reinforced idea play critical role localization, protein-protein interactions, maintenance levels, modifying aggregate structure. These also provide tantalizing clues possibility neurons actively choose is post-translationally modified, competitive combinatorial ways, achieve broad, cellular programs commensurate distinctive environmental conditions found development, aging, stress, Here, we review describe what currently known about their functional impacts. addition, classify from perspectives electrostatics, stability, all contribute homeostasis. Finally, assess impact solubility aggregation. Tau occupies undoubtedly important position biology neurodegenerative diseases. This aims integrated perspective actively, purposefully, dynamically remodel function, clearance, doing so, hope enable more comprehensive understanding will positively future studies.

Language: Английский

Citations

252
Cryo-EM structures of tau filaments DOI
Sjors H. W. Scheres, Wenjuan Zhang, Benjamin Falcon

et al.

Current Opinion in Structural Biology, Journal Year: 2020, Volume and Issue: 64, P. 17 - 25

Published: June 27, 2020

Language: Английский

Citations

226
High-Contrast In Vivo Imaging of Tau Pathologies in Alzheimer’s and Non-Alzheimer’s Disease Tauopathies DOI Creative Commons
Kenji Tagai, Maiko Ono, Manabu Kubota

et al.

Neuron, Journal Year: 2020, Volume and Issue: 109(1), P. 42 - 58.e8

Published: Oct. 30, 2020

Language: Английский

Citations

210