Assembly of recombinant tau into filaments identical to those of Alzheimer’s disease and chronic traumatic encephalopathy

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

(2022) Yang Yang et al.   SCIENCE

Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis

(2022) Liisa Lutter et al.   JOURNAL OF MOLECULAR BIOLOGY

Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis

(2021) Lynn Radamaker et al.   Nature Communications

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

(2021) Qiuye Li et al.   Nature Communications

Seeded assembly in vitro does not replicate the structures of α‐synuclein filaments from multiple system atrophy

(2021) Sofia Lövestam et al.   FEBS Open Bio

Cryo-EM structures of tau filaments from Alzheimer’s disease with PET ligand APN-1607

(2021) Yang Shi et al.   ACTA NEUROPATHOLOGICA

The AD tau core spontaneously self-assembles and recruits full-length tau to filaments

(2021) Yari Carlomagno et al.   Cell Reports

Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils

(2021) Pijush Chakraborty et al.   Nature Communications

New tools for automated cryo-EM single-particle analysis in RELION-4.0

(2021) Dari Kimanius et al.   BIOCHEMICAL JOURNAL

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

(2021) Tamta Arakhamia et al.   CELL

Structure-based classification of tauopathies

(2021) Yang Shi et al.   NATURE

Structure of pathological TDP-43 filaments from ALS with FTLD

(2021) Diana Arseni et al.   NATURE

Novel tau filament fold in corticobasal degeneration

(2020) Wenjuan Zhang et al.   NATURE

Amyloid structure determination in RELION-3.1

(2020) Sjors H. W. Scheres   Acta Crystallographica Section D-Structural Biology

Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1

(2020) Jasenko Zivanov et al.   IUCrJ

Structures of α-synuclein filaments from multiple system atrophy

(2020) Manuel Schweighauser et al.   NATURE

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease

(2020) Hendrik Wesseling et al.   CELL

Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis

(2019) Lynn Radamaker et al.   Nature Communications

Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient

(2019) Paolo Swuec et al.   Nature Communications

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

(2019) Benjamin Falcon et al.   NATURE

Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

(2019) Wenjuan Zhang et al.   eLife

4-Repeat tau seeds and templating subtypes as brain and CSF biomarkers of frontotemporal lobar degeneration

(2019) Eri Saijo et al.   ACTA NEUROPATHOLOGICA

Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs

(2019) Tristan Bepler et al.   NATURE METHODS

Current Developments in Coot for Macromolecular Model Building of Electron Cryo‐microscopy and Crystallographic Data

(2019) Ana Casañal et al.   PROTEIN SCIENCE

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

(2019) Marius Kollmer et al.   Nature Communications

Tau (297‐391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain

(2019) Youssra K. Al‐Hilaly et al.   FEBS LETTERS

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

(2019) Ricardo Guerrero-Ferreira et al.   eLife

ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

(2018) Tristan Ian Croll   Acta Crystallographica Section D-Structural Biology

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

(2018) Yaowang Li et al.   CELL RESEARCH

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

(2018) Benjamin Falcon et al.   NATURE

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

(2018) Binsen Li et al.   Nature Communications

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

(2018) Benjamin Falcon et al.   ACTA NEUROPATHOLOGICA

A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis

(2018) Jasenko Zivanov et al.   IUCrJ

Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking

(2017) Youssra K. Al-Hilaly et al.   JOURNAL OF MOLECULAR BIOLOGY

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

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

(2016) Marielle Aulikki Wälti et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

IVA cloning: A single-tube universal cloning system exploiting bacterial In Vivo Assembly

(2016) Javier García-Nafría et al.   Scientific Reports

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

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

Tau and neurodegenerative disease: the story so far

(2015) Khalid Iqbal et al.   Nature Reviews Neurology

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers

(2015) Sarah L. Shammas et al.   Nature Communications

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

(2013) Jun-Xia Lu et al.   CELL

Tau binds ATP and induces its aggregation

(2013) Mina Farid et al.   MICROSCOPY RESEARCH AND TECHNIQUE

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

(2013) Shaoxia Chen et al.   ULTRAMICROSCOPY

Cross-seeding and Conformational Selection between Three- and Four-repeat Human Tau Proteins

(2012) Xiang Yu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A New Structural Model of Aβ40Fibrils

(2011) Ivano Bertini et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Inhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau

(2009) Wenkai Li et al.   JOURNAL OF NEUROCHEMISTRY