Biophysical characterization of full‐length TAR DNA‐binding protein ( TDP ‐43) phase separation

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

(2022) Lara A Gruijs da Silva et al.   EMBO JOURNAL

Effect of In Vitro Solvation Conditions on Inter- and Intramolecular Assembly of Full-Length TDP-43

(2022) Abhilasha A. Doke et al.   JOURNAL OF PHYSICAL CHEMISTRY B

An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature

(2022) Roberta Cascella et al.   ANNALS OF MEDICINE

A generic approach to study the kinetics of liquid–liquid phase separation under near-native conditions

(2021) Joris Van Lindt et al.   Communications Biology

Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands

(2021) Praveen P.N. Rao et al.   EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY

Structure of pathological TDP-43 filaments from ALS with FTLD

(2021) Diana Arseni et al.   NATURE

Stress Induces Dynamic, Cytotoxicity-Antagonizing TDP-43 Nuclear Bodies via Paraspeckle LncRNA NEAT1-Mediated Liquid-Liquid Phase Separation

(2020) Chen Wang et al.   MOLECULAR CELL

Aggregation of the nucleic acid–binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation

(2019) Youjun Chen et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

(2019) Fatima Gasset-Rosa et al.   NEURON

The role of liquid-liquid phase separation in aggregation of the TDP-43 low complexity domain

(2019) W. Michael Babinchak et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration

(2019) Mirella Vivoli Vega et al.   FASEB JOURNAL

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

Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior

(2018) Titus Franzmann et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Advances in Understanding Stimulus-Responsive Phase Behavior of Intrinsically Disordered Protein Polymers

(2018) Kiersten M. Ruff et al.   JOURNAL OF MOLECULAR BIOLOGY

Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization

(2018) Leeanne McGurk et al.   MOLECULAR CELL

Physiologically Important Electrolytes as Regulators of TDP-43 Aggregation and Droplet-Phase Behavior

(2018) Yulong Sun et al.   BIOCHEMISTRY

A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation

(2018) Kyoung-Jae Choi et al.   BIOCHEMISTRY

Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons

(2017) Pallavi P. Gopal et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2017) Tariq Afroz et al.   Nature Communications

Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation

(2017) Christine Xue et al.   Royal Society Open Science

Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies

(2016) Roberta Cascella et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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

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

(2015) Amandine Molliex et al.   CELL

Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles

(2015) Timothy J. Nott et al.   MOLECULAR CELL

Poly-A Binding Protein-1 Localization to a Subset of TDP-43 Inclusions in Amyotrophic Lateral Sclerosis Occurs More Frequently in Patients Harboring an Expansion inC9orf72

(2014) Leeanne McGurk et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY

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

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

Stages of pTDP-43 pathology in amyotrophic lateral sclerosis

(2013) Johannes Brettschneider et al.   ANNALS OF NEUROLOGY

Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones

(2013) Maria Udan-Johns et al.   HUMAN MOLECULAR GENETICS

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

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

The changing scene of amyotrophic lateral sclerosis

(2013) Wim Robberecht et al.   NATURE REVIEWS NEUROSCIENCE

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

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

The long non-coding RNA nuclear-enriched abundant transcript 1_2 induces paraspeckle formation in the motor neuron during the early phase of amyotrophic lateral sclerosis

(2013) Yoshinori Nishimoto et al.   Molecular Brain

Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects

(2012) Glenda Halliday et al.   ACTA NEUROPATHOLOGICA

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 Seeds of Neurodegeneration: Prion-like Spreading in ALS

(2011) Magdalini Polymenidou et al.   CELL

TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

(2011) Robert H. Baloh   FEBS Journal

TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies

(2011) Todd J. Cohen et al.   TRENDS IN MOLECULAR MEDICINE

Amyotrophic lateral sclerosis: dash-like accumulation of phosphorylated TDP-43 in somatodendritic and axonal compartments of somatomotor neurons of the lower brainstem and spinal cord

(2010) Heiko Braak et al.   ACTA NEUROPATHOLOGICA

Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form

(2010) Aaron Kerman et al.   ACTA NEUROPATHOLOGICA

Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution

(2010) Harry Levine   PROTEIN SCIENCE

TDP-43 Redistribution is an Early Event in Sporadic Amyotrophic Lateral Sclerosis

(2009) Maria Teresa Giordana et al.   BRAIN PATHOLOGY

TDP-43 Dimerizes in Human Cells in Culture

(2009) Yuki Shiina et al.   CELLULAR AND MOLECULAR NEUROBIOLOGY

TDP-43 is recruited to stress granules in conditions of oxidative insult

(2009) Claudia Colombrita et al.   JOURNAL OF NEUROCHEMISTRY

ALS motor phenotype heterogeneity, focality, and spread: Deconstructing motor neuron degeneration

(2009) J. M. Ravits et al.   NEUROLOGY

Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations

(2008) Ian R. A. Mackenzie et al.   ACTA NEUROPATHOLOGICA

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

Structural determinants of the cellular localization and shuttling of TDP-43

(2008) Y. M. Ayala et al.   JOURNAL OF CELL SCIENCE

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

Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease

(2008) Claudia Schwab et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY