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

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 TDP-43 N-terminal domain structure at high resolution

(2016) Miguel Mompeán et al.   FEBS Journal

Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons

(2016) Miguel Mompeán et al.   Journal of Physical Chemistry Letters

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

(2016) Miguel Mompeán et al.   PLOS BIOLOGY

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

Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion

(2016) Alba Espargaró et al.   Frontiers in Molecular Neuroscience

Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains

(2016) Fuyuki Kametani et al.   Scientific Reports

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

(2015) Avinash Patel 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

Review: Prion-like mechanisms of transactive response DNA binding protein of 43 kDa (TDP-43) in amyotrophic lateral sclerosis (ALS)

(2015) Phillip Smethurst et al.   NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY

The structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function

(2015) Valentina Romano et al.   Prion

“Structural characterization of the minimal segment of TDP-43 competent for aggregation”

(2014) Miguel Mompeán et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution

(2014) Li Zhu et al.   HUMAN MOLECULAR GENETICS

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

Self-Assembling Properties of Peptides Derived from TDP-43 C-Terminal Fragment

(2014) Akash Saini et al.   LANGMUIR

TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells

(2014) Claudia Capitini et al.   PLoS One

The Influence of Pathological Mutations and Proline Substitutions in TDP-43 Glycine-Rich Peptides on Its Amyloid Properties and Cellular Toxicity

(2014) Chia-Sui Sun et al.   PLoS One

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

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

Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid

(2013) Eileen H. Bigio et al.   ACTA NEUROPATHOLOGICA

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

Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion

(2013) Lei-Lei Jiang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Truncated C-terminal RNA Recognition Motif of TDP-43 Protein Plays a Key Role in Forming Proteinaceous Aggregates

(2013) Yi-Ting Wang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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

TDP-43 skeins show properties of amyloid in a subset of ALS cases

(2012) John L. Robinson et al.   ACTA NEUROPATHOLOGICA

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

(2012) Masato Kato et al.   CELL

Cellular Model of TAR DNA-binding Protein 43 (TDP-43) Aggregation Based on Its C-terminal Gln/Asn-rich Region

(2012) Mauricio Budini et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43: gumming up neurons through protein–protein and protein–RNA interactions

(2012) Emanuele Buratti et al.   TRENDS IN BIOCHEMICAL SCIENCES

A harmonized classification system for FTLD-TDP pathology

(2011) Ian R. A. Mackenzie et al.   ACTA NEUROPATHOLOGICA

Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment

(2011) Akash Saini et al.   CHEMBIOCHEM

TDP-43: new aspects of autoregulation mechanisms in RNA binding proteins and their connection with human disease

(2011) Emanuele Buratti et al.   FEBS Journal

Amyotrophic lateral sclerosis

(2011) Matthew C Kiernan et al.   LANCET

Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

(2011) Magdalini Polymenidou et al.   NATURE NEUROSCIENCE

Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

(2011) James R Tollervey et al.   NATURE NEUROSCIENCE

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

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

Hyperphosphorylation as a Defense Mechanism to Reduce TDP-43 Aggregation

(2011) Huei-Ying Li et al.   PLoS One

Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43

(2010) Rodrigo A. Fuentealba et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1

(2010) Owen A. Brady et al.   JOURNAL OF NEUROCHEMISTRY

Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis

(2010) Allan K.-H. Chen et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

(2009) Manuela Neumann et al.   ACTA NEUROPATHOLOGICA

Identification of casein kinase-1 phosphorylation sites on TDP-43

(2009) Fuyuki Kametani et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis

(2009) G. S. Pesiridis et al.   HUMAN MOLECULAR GENETICS

Structural insights into TDP-43 in nucleic-acid binding and domain interactions

(2009) P.-H. Kuo et al.   NUCLEIC ACIDS RESEARCH

Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases

(2008) Wen-Lang Lin et al.   ACTA NEUROPATHOLOGICA

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

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy

(2008) Julian R. Thorpe et al.   JOURNAL OF NEURAL TRANSMISSION

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity

(2008) B. S. Johnson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA