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

Protonation–Deprotonation Switch Controls the Amyloid-like Misfolding of Nucleic-Acid-Binding Domains of TDP-43

(2021) Divya Patni et al.   JOURNAL OF PHYSICAL CHEMISTRY B

The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation

(2021) Juan Carlos Rengifo-Gonzalez et al.   eLife

Early Metastable Assembly during the Stress-Induced Formation of Worm-like Amyloid Fibrils of Nucleic Acid Binding Domains of TDP-43

(2020) Meenakshi Pillai et al.   BIOCHEMISTRY

Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases

(2020) Gareth S.A. Wright et al.   iScience

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis

(2019) Archana Prasad et al.   Frontiers in Molecular Neuroscience

RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43

(2019) Jacob R. Mann et al.   NEURON

Global, regional, and national burden of neurological disorders, 1990–2016: a systematic analysis for the Global Burden of Disease Study 2016

(2019) Valery L Feigin et al.   LANCET NEUROLOGY

RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43

(2019) Elsa Zacco et al.   JOURNAL OF MOLECULAR BIOLOGY

Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation

(2019) Rachel L. French et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43

(2018) Hao-Ru Li et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

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

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

RNA buffers the phase separation behavior of prion-like RNA binding proteins

(2018) Shovamayee Maharana et al.   SCIENCE

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

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

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

Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine

(2017) Samantha S. Stadmiller et al.   JOURNAL OF MOLECULAR BIOLOGY

Clinical Neurology and Epidemiology of the Major Neurodegenerative Diseases

(2017) Michael G. Erkkinen et al.   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

Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates

(2017) Cyrille Garnier et al.   Scientific Reports

Distinct TDP-43 inclusion morphologies in frontotemporal lobar degeneration with and without amyotrophic lateral sclerosis

(2017) Rachel H. Tan et al.   Acta Neuropathologica Communications

Decoding ALS: from genes to mechanism

(2016) J. Paul Taylor et al.   NATURE

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

(2016) Miguel Mompeán et al.   PLOS BIOLOGY

Distinct stages in stress granule assembly and disassembly

(2016) Joshua R Wheeler et al.   eLife

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

(2015) Amandine Molliex et al.   CELL

An acetylation switch controls TDP-43 function and aggregation propensity

(2015) Todd J. Cohen et al.   Nature Communications

Binding of TDP-43 to the 3′UTR of Its Cognate mRNA Enhances Its Solubility

(2014) Yulong Sun et al.   BIOCHEMISTRY

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

Inhibition of TDP-43 Aggregation by Nucleic Acid Binding

(2013) Yi-Chen Huang et al.   PLoS One

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

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

Targeted Depletion of TDP-43 Expression in the Spinal Cord Motor Neurons Leads to the Development of Amyotrophic Lateral Sclerosis-like Phenotypes in Mice

(2012) Lien-Szu Wu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Intracellular pH is a tightly controlled signal in yeast

(2011) Rick Orij et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site

(2011) Yoshiaki Furukawa et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking

(2011) Todd J Cohen et al.   EMBO JOURNAL

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

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

Selective Neuronal Vulnerability in Neurodegenerative Diseases: from Stressor Thresholds to Degeneration

(2011) Smita Saxena et al.   NEURON

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

(2010) Matthew Biancalana et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

TDP-43 regulates its mRNA levels through a negative feedback loop

(2010) Youhna M Ayala et al.   EMBO JOURNAL

Phosphorylation Promotes Neurotoxicity in a Caenorhabditis elegans Model of TDP-43 Proteinopathy

(2010) N. F. Liachko et al.   JOURNAL OF NEUROSCIENCE

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

TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor

(2010) C. M. Dewey et al.   MOLECULAR AND CELLULAR BIOLOGY

ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS

(2010) S.-C. Ling et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Clinical and Pathological Continuum of Multisystem TDP-43 Proteinopathies

(2009) Felix Geser et al.   ARCHIVES OF NEUROLOGY

TDP-43 Dimerizes in Human Cells in Culture

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

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

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

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

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

Evidence for Stepwise Formation of Amyloid Fibrils by the Mouse Prion Protein

(2008) Shweta Jain et al.   JOURNAL OF MOLECULAR BIOLOGY

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE