Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16

Cryo-EM structures of four polymorphic TDP-43 amyloid cores

(2019) Qin Cao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

(2018) Ailin Wang et al.   EMBO JOURNAL

TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues

(2018) Hao-Ru Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR

(2018) Irina Matlahov et al.   METHODS

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

(2018) Antoine Loquet et al.   METHODS

Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation

(2018) Veronica H. Ryan et al.   MOLECULAR CELL

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation

(2018) Elizabeth L. Guenther et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2

(2018) Elizabeth L. Guenther et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Protein Phase Separation: A New Phase in Cell Biology

(2018) Steven Boeynaems et al.   TRENDS IN CELL BIOLOGY

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation

(2018) Elizabeth L. Guenther et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2

(2018) Elizabeth L. Guenther et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Characterization of the Partially Folded States of TDP-43 RRM2 and Their Significance to ALS Pathogenesis

(2018) Davide Tavella et al.   BIOPHYSICAL JOURNAL

The Folding and Aggregation Energy Landscapes of Tethered RRM Domains of Human TDP-43 Are Coupled via a Metastable Molten Globule-like Oligomer

(2018) Meenakshi Pillai et al.   BIOCHEMISTRY

TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle

(2018) Thomas O. Vogler et al.   NATURE

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions

(2017) Miguel Mompeán et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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

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

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

(2017) Lothar Gremer et al.   SCIENCE

Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy

(2017) Patrick C.A. van der Wel   SOLID STATE NUCLEAR MAGNETIC RESONANCE

Solid-state NMR spectroscopic trends for supramolecular assemblies and protein aggregates

(2017) Rasmus Linser   SOLID STATE NUCLEAR MAGNETIC RESONANCE

Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR

(2017) Beat H. Meier et al.   TRENDS IN BIOCHEMICAL SCIENCES

The Amyloid Phenomenon and Its Links with Human Disease

(2017) Christopher M. Dobson   Cold Spring Harbor Perspectives in Biology

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

(2017) Tariq Afroz et al.   Nature Communications

The N-terminal dimerization is required for TDP-43 splicing activity

(2017) Lei-Lei Jiang et al.   Scientific Reports

The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivo

(2016) Hiroki Sasaguri et al.   BRAIN RESEARCH

The amyloid hypothesis of Alzheimer's disease at 25 years

(2016) Dennis J Selkoe et al.   EMBO Molecular Medicine

The TDP-43 N-terminal domain structure at high resolution

(2016) Miguel Mompeán et al.   FEBS Journal

Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins

(2016) Antonia Ratti et al.   JOURNAL OF NEUROCHEMISTRY

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

(2016) Michael T. Colvin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity

(2016) Wenzhang Wang et al.   NATURE MEDICINE

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

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

The Three-Dimensional Structures of Amyloids

(2016) Roland Riek   Cold Spring Harbor Perspectives in Biology

Yeast and Fungal Prions

(2016) Reed B. Wickner   Cold Spring Harbor Perspectives in Biology

Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation

(2016) Lei-Lei Jiang et al.   Scientific Reports

Structural Biology of PrP Prions

(2016) Gerald Stubbs et al.   Cold Spring Harbor Perspectives in Medicine

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43

(2016) Liangzhong Lim et al.   PLOS BIOLOGY

An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds

(2016) Miguel Mompeán et al.   Frontiers in Molecular Neuroscience

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

(2015) Amandine Molliex et al.   CELL

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

(2015) Miguel Mompeán et al.   Journal of Physical Chemistry Letters

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

The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity

(2015) Quan Li et al.   Nature Communications

An acetylation switch controls TDP-43 function and aggregation propensity

(2015) Todd J. Cohen 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

Liquid-Liquid Phase Separation in Biology

(2014) Anthony A. Hyman et al.   Annual Review of Cell and Developmental Biology

TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain

(2014) Mauricio Budini et al.   HUMAN MOLECULAR GENETICS

Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State

(2014) Brian C. Mackness et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA

(2014) Haina Qin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Physical and structural basis for polymorphism in amyloid fibrils

(2014) Robert Tycko   PROTEIN SCIENCE

Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients

(2014) Yu-Sheng Fang et al.   Nature Communications

Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils

(2013) Ming Tang et al.   ACCOUNTS OF CHEMICAL RESEARCH

Molecular Structures of Amyloid and Prion Fibrils: Consensus versus Controversy

(2013) Robert Tycko et al.   ACCOUNTS OF CHEMICAL RESEARCH

The Conformation of the Prion Domain of Sup35 p in Isolation and in the Full-Length Protein

(2013) Nina Luckgei et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation

(2013) Yong-Jie Zhang et al.   HUMAN MOLECULAR GENETICS

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS

(2013) Hong Joo Kim et al.   NATURE

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

(2013) Peter J Lukavsky et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains

(2013) Takashi Nonaka et al.   Cell Reports

Cognitive and functional resilience despite molecular evidence of Alzheimer’s disease pathology

(2012) Selam Negash et al.   Alzheimers & Dementia

A Native-Like Conformation for the C-Terminal Domain of the Prion Ure2p within its Fibrillar Form

(2012) Birgit Habenstein et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity

(2012) Chung-ke Chang et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease

(2012) Oliver D. King et al.   BRAIN RESEARCH

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

(2012) Masato Kato et al.   CELL

Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies

(2012) Tina W. Han et al.   CELL

Screening of the SOD1, FUS, TARDBP, ANG, and OPTN mutations in Korean patients with familial and sporadic ALS

(2012) Min-Jung Kwon et al.   NEUROBIOLOGY OF AGING

Understanding the role of TDP-43 and FUS/TLS in ALS and beyond

(2011) Sandrine Da Cruz et al.   CURRENT OPINION IN NEUROBIOLOGY

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

(2011) Weirui Guo et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Rethinking ALS: The FUS about TDP-43

(2009) Clotilde Lagier-Tourenne et al.   CELL

Stress granules

(2009) Paul Anderson et al.   CURRENT BIOLOGY

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

(2009) Brian S. Johnson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Molecular Organization of the Fungal Prion HET-s in Its Amyloid Form

(2009) Christian Wasmer et al.   JOURNAL OF MOLECULAR BIOLOGY

Prion Fibrils of Ure2p Assembled under Physiological Conditions Contain Highly Ordered, Natively Folded Modules

(2009) Antoine Loquet et al.   JOURNAL OF MOLECULAR BIOLOGY

Eukaryotic Stress Granules: The Ins and Outs of Translation

(2009) J. Ross Buchan et al.   MOLECULAR CELL

Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

(2009) T. J. Kwiatkowski et al.   SCIENCE

Sporadic amyotrophic lateral sclerosis: two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions

(2008) Yasushi Nishihira et al.   ACTA NEUROPATHOLOGICA

Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia

(2008) Fumiaki Mori et al.   ACTA NEUROPATHOLOGICA

Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation

(2008) Matthew J. Winton et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core

(2008) C. Wasmer et al.   SCIENCE

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

(2008) J. Sreedharan et al.   SCIENCE

Novel Mutations in TARDBP (TDP-43) in Patients with Familial Amyotrophic Lateral Sclerosis

(2008) Nicola J. Rutherford et al.   PLoS Genetics