Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease

(2021) Dan Li et al.   Nature Chemical Biology

Inclusion of the C-Terminal Domain in the β-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy

(2021) Aurelio J. Dregni et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components

(2021) Evan Lester et al.   NEURON

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

(2021) Michael R. Sawaya et al.   CELL

Structure-based classification of tauopathies

(2021) Yang Shi et al.   NATURE

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

(2020) Tamta Arakhamia et al.   CELL

Novel tau filament fold in corticobasal degeneration

(2020) Wenjuan Zhang et al.   NATURE

Structures of α-synuclein filaments from multiple system atrophy

(2020) Manuel Schweighauser et al.   NATURE

Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease

(2020) Romany Abskharon et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cryo-EM structures of tau filaments

(2020) Sjors HW Scheres et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

The three-dimensional structure of human β-endorphin amyloid fibrils

(2020) Carolin Seuring et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

(2020) Jiahui Lu et al.   Nature Communications

RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction

(2020) Mauro Montalbano et al.   Nature Communications

Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids

(2019) Falk Liberta et al.   Nature Communications

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

(2019) Benjamin Falcon et al.   NATURE

The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations

(2019) Martin D. Gelenter et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

(2019) Xinrui Gui et al.   Nature Communications

Structure-based inhibitors halt prion-like seeding by Alzheimer's disease–and tauopathy–derived brain tissue samples

(2019) Paul Matthew Seidler et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Tau-Cofactor Complexes as Building Blocks of Tau Fibrils

(2019) Yann Fichou et al.   Frontiers in Neuroscience

A brave new world of RNA-binding proteins

(2018) Matthias W. Hentze et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Automated map sharpening by maximization of detail and connectivity

(2018) Thomas C. Terwilliger et al.   Acta Crystallographica Section D-Structural Biology

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

(2018) Benjamin Falcon et al.   NATURE

Cofactors are essential constituents of stable and seeding-active tau fibrils

(2018) Yann Fichou et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Helical reconstruction in RELION

(2017) Shaoda He et al.   JOURNAL OF STRUCTURAL BIOLOGY

Cryo-EM structures of tau filaments from Alzheimer’s disease

(2017) Anthony W. P. Fitzpatrick et al.   NATURE

Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo

(2017) Daniel J. Apicco et al.   NATURE NEUROSCIENCE

Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

(2017) Susmitha Ambadipudi et al.   Nature Communications

RNA stores tau reversibly in complex coacervates

(2017) Xuemei Zhang et al.   PLOS BIOLOGY

The Presence of Select Tau Species in Human Peripheral Tissues and Their Relation to Alzheimer’s Disease

(2016) Brittany N. Dugger et al.   JOURNAL OF ALZHEIMERS DISEASE

Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo

(2016) Sarah K. Kaufman et al.   NEURON

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

(2016) Alexander E. Conicella et al.   STRUCTURE

RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth

(2015) Paul D. Dinkel et al.   BIOCHEMISTRY

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

(2015) Amandine Molliex et al.   CELL

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

(2015) Avinash Patel et al.   CELL

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

(2015) Alexis Rohou et al.   JOURNAL OF STRUCTURAL BIOLOGY

Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins

(2015) Yuan Lin et al.   MOLECULAR CELL

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

(2014) David W. Sanders et al.   NEURON

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

(2012) Masato Kato et al.   CELL

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

(2012) Sjors H.W. Scheres   JOURNAL OF STRUCTURAL BIOLOGY

NIH Image to ImageJ: 25 years of image analysis

(2012) Caroline A Schneider et al.   NATURE METHODS

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

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

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Generating a Prion with Bacterially Expressed Recombinant Prion Protein

(2010) F. Wang et al.   SCIENCE

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY