Shapeshifter TDP-43: Molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators

Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43

(2022) Yi Xiao Jiang et al.   NATURE

Cell environment shapes TDP-43 function with implications in neuronal and muscle disease

(2022) Urša Šušnjar et al.   Communications Biology

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

Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes

(2022) Harmeen K. Deol et al.   BIOPHYSICAL CHEMISTRY

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

(2022) Tommaso Staderini et al.   PROTEIN SCIENCE

Multistep molecular mechanism of amyloid‐like aggregation of nucleic acid‐binding domain of TDP ‐43

(2022) Meenakshi Pillai et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

NMR assignments for the C-terminal domain of human TDP-43

(2021) David Pantoja-Uceda et al.   Biomolecular NMR Assignments

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

(2021) Phuong H. Nguyen et al.   CHEMICAL REVIEWS

DCTN1 Binds to TDP-43 and Regulates TDP-43 Aggregation

(2021) Manami Deshimaru et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

N-terminal Domain of TDP43 Enhances Liquid-Liquid Phase Separation of Globular Proteins

(2021) G. Campbell Carter et al.   JOURNAL OF MOLECULAR BIOLOGY

Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates

(2021) David Pantoja-Uceda et al.   PLOS BIOLOGY

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

Aggregation is a Context-Dependent Constraint on Protein Evolution

(2021) Michele Monti et al.   Frontiers in Molecular Biosciences

Clustering of Aromatic Residues in Prion-like Domains Can Tune the Formation, State, and Organization of Biomolecular Condensates

(2021) Alex S. Holehouse et al.   BIOCHEMISTRY

Transient disorder along pathways to amyloid

(2021) Gareth J. Morgan   BIOPHYSICAL CHEMISTRY

Metals in ALS TDP-43 Pathology

(2021) Lassi Koski et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

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

Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43

(2020) Anukool A. Bhopatkar et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Solid-State NMR Reveals the Structural Transformation of the TDP-43 Amyloidogenic Region upon Fibrillation

(2020) Xiao-Feng Zhuo et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

TDP-43 α-helical structure tunes liquid–liquid phase separation and function

(2020) Alexander E. Conicella et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains

(2020) Erik W. Martin et al.   SCIENCE

Mice Carrying ALS Mutant TDP-43, but Not Mutant FUS, Display In Vivo Defects in Axonal Transport of Signaling Endosomes

(2020) James N. Sleigh et al.   Cell Reports

TDP-43 Is Efficiently Transferred Between Neuron-Like Cells in a Manner Enhanced by Preservation of Its N-Terminus but Independent of Extracellular Vesicles

(2020) Christopher Sackmann et al.   Frontiers in Neuroscience

Nucleo–cytoplasmic transport defects and protein aggregates in neurodegeneration

(2020) Giacomo Bitetto et al.   Translational Neurodegeneration

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

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

The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies

(2020) Myungjin Jo et al.   EXPERIMENTAL AND MOLECULAR MEDICINE

The role of water in the primary nucleation of protein amyloid aggregation

(2020) José D. Camino et al.   BIOPHYSICAL CHEMISTRY

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

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

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 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

Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates

(2019) Simon Alberti et al.   CELL

Delineating the effect of mutations on the conformational dynamics of N-terminal domain of TDP-43

(2019) Vijay Kumar et al.   BIOPHYSICAL CHEMISTRY

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

(2019) Mirella Vivoli Vega et al.   FASEB JOURNAL

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy

(2019) Han-Jou Chen et al.   BRAIN

Suppression of Progranulin Expression Leads to Formation of Intranuclear TDP-43 Inclusions In Vitro: A Cell Model of Frontotemporal Lobar Degeneration

(2019) Jiuling Zhu et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY

Cdc48/VCP and endocytosis regulate TDP-43 and FUS toxicity and turnover

(2019) Guangbo Liu et al.   MOLECULAR AND CELLULAR BIOLOGY

Phase separation-deficient TDP43 remains functional in splicing

(2019) Hermann Broder Schmidt et al.   Nature Communications

TDP-43 Regulates Coupled Dendritic mRNA Transport-Translation Processes in Co-operation with FMRP and Staufen1

(2019) Jen-Fei Chu et al.   Cell Reports

TDP-43 NTD can be induced while CTD is significantly enhanced by ssDNA to undergo liquid-liquid phase separation

(2018) Lu Wang et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

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

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

(2018) Ailin Wang et al.   EMBO JOURNAL

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

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

(2018) Shovamayee Maharana et al.   SCIENCE

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

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

(2018) Helena Ederle et al.   Scientific Reports

Keys to Amyloid City: Computational sampling, refined by solution NMR, captures potential TDP-43 intermediates in ALS neurodegeneration

(2018) Matthias Buck   BIOPHYSICAL JOURNAL

TARDBP Mutation Analysis in TDP-43 Proteinopathies and Deciphering the Toxicity of Mutant TDP-43

(2018) Tania F. Gendron et al.   JOURNAL OF ALZHEIMERS DISEASE

Selective vulnerability in neurodegenerative diseases

(2018) Hongjun Fu et al.   NATURE NEUROSCIENCE

Protein-protein interactions reveal key canonical pathways, upstream regulators, interactome domains, and novel targets in ALS

(2018) Ina Dervishi et al.   Scientific Reports

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

Poly(ADP-ribose) Engages the TDP-43 Nuclear-Localization Sequence to Regulate Granulo-Filamentous Aggregation

(2018) Leeanne McGurk et al.   BIOCHEMISTRY

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

(2018) Thomas O. Vogler et al.   NATURE

TDP-43 shapeshifts to encipher FTD severity

(2018) Edward M. Barbieri et al.   NATURE NEUROSCIENCE

TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates

(2018) Florent Laferrière et al.   NATURE NEUROSCIENCE

Heavy Metal Neurotoxicants Induce ALS-Linked TDP-43 Pathology

(2018) Peter E A Ash et al.   TOXICOLOGICAL SCIENCES

A physics-based model explains the prion-like features of neurodegeneration in Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis

(2018) Johannes Weickenmeier et al.   JOURNAL OF THE MECHANICS AND PHYSICS OF SOLIDS

Exploring the aggregation-prone regions from structural domains of human TDP-43

(2018) Vijay Kumar et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

TDP-43 and FUS en route from the nucleus to the cytoplasm

(2017) Helena Ederle et al.   FEBS LETTERS

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

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

An Alternatively Packed Dry Molten Globule-like Intermediate in the Native State Ensemble of a Multidomain Protein

(2017) Prajna Mishra et al.   JOURNAL OF PHYSICAL CHEMISTRY B

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

ATP as a biological hydrotrope

(2017) Avinash Patel et al.   SCIENCE

Liquid phase condensation in cell physiology and disease

(2017) Yongdae Shin et al.   SCIENCE

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

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 TDP-43 N-terminal domain structure at high resolution

(2016) Miguel Mompeán et al.   FEBS Journal

TDP-43 binds and transports G-quadruplex-containing mRNAs into neurites for local translation

(2016) Akira Ishiguro et al.   GENES TO CELLS

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

(2016) Antonia Ratti et al.   JOURNAL OF NEUROCHEMISTRY

Decoding ALS: from genes to mechanism

(2016) J. Paul Taylor et al.   NATURE

In vitro prion-like behaviour of TDP-43 in ALS

(2016) Phillip Smethurst et al.   NEUROBIOLOGY OF DISEASE

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

In Vivo Formation of Vacuolated Multi-phase Compartments Lacking Membranes

(2016) Hermann Broder Schmidt et al.   Cell Reports

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

(2016) Miguel Mompeán et al.   PLOS BIOLOGY

Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation

(2016) Chien-Hao Chiang et al.   Scientific Reports

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

(2016) Fuyuki Kametani et al.   Scientific Reports

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

(2015) Amandine Molliex et al.   CELL

Activation of ER Stress and Autophagy Induced by TDP-43 A315T as Pathogenic Mechanism and the Corresponding Histological Changes in Skin as Potential Biomarker for ALS with the Mutation

(2015) Xuejing Wang et al.   International Journal of Biological Sciences

TDP-43 is intercellularly transmitted across axon terminals

(2015) Marisa S. Feiler et al.   JOURNAL OF CELL BIOLOGY

An acetylation switch controls TDP-43 function and aggregation propensity

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

Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure

(2015) Xuebing Ding et al.   Oncotarget

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

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

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

(2014) Yulong Sun et al.   BIOCHEMISTRY

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

Evolutionarily Conserved Heterogeneous Nuclear Ribonucleoprotein (hnRNP) A/B Proteins Functionally Interact with Human andDrosophilaTAR DNA-binding Protein 43 (TDP-43)

(2014) Maurizio Romano et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

 -Synuclein Is Localized to Mitochondria-Associated ER Membranes

(2014) C. Guardia-Laguarta et al.   JOURNAL OF NEUROSCIENCE

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

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

Delineating the membrane-disrupting and seeding properties of the TDP-43 amyloidogenic core

(2013) Gerard Chun-Hao Liu et al.   CHEMICAL COMMUNICATIONS

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

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

Aberrant Assembly of RNA Recognition Motif 1 Links to Pathogenic Conversion of TAR DNA-binding Protein of 43 kDa (TDP-43)

(2013) Akemi Shodai 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

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 ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth

(2012) Claudia Fallini et al.   HUMAN MOLECULAR GENETICS

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

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

The Transthyretin Amyloidoses: From Delineating the Molecular Mechanism of Aggregation Linked to Pathology to a Regulatory-Agency-Approved Drug

(2012) Steven M. Johnson et al.   JOURNAL OF MOLECULAR BIOLOGY

Inhibition of TDP-43 Accumulation by Bis(thiosemicarbazonato)-Copper Complexes

(2012) Sarah J. Parker et al.   PLoS One

Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation

(2012) Y. Yoshimura et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

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

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

The Seeds of Neurodegeneration: Prion-like Spreading in ALS

(2011) Magdalini Polymenidou et al.   CELL

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

(2011) Akash Saini et al.   CHEMBIOCHEM

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

(2011) Todd J Cohen et al.   EMBO JOURNAL

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

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

(2011) Smita Saxena et al.   NEURON

TDP-43 and FUS: a nuclear affair

(2011) Dorothee Dormann et al.   TRENDS IN NEUROSCIENCES

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

Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration

(2010) Agnes L. Nishimura et al.   BRAIN

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

(2010) Youhna M Ayala et al.   EMBO JOURNAL

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

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

Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes

(2010) Chantelle F. Sephton et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA

(2010) Sang Hwa Kim et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1

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

Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis

(2010) S. J. Barmada et al.   JOURNAL OF NEUROSCIENCE

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

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

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

(2010) Ian RA Mackenzie et al.   LANCET NEUROLOGY

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

TAR DNA-binding protein 43 in neurodegenerative disease

(2010) Alice S. Chen-Plotkin et al.   Nature Reviews Neurology

TDP-43-Mediated Neuron Loss In Vivo Requires RNA-Binding Activity

(2010) Aaron Voigt et al.   PLoS One

Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue

(2010) Liqun Liu-Yesucevitz et al.   PLoS One

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

The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation

(2010) Emanuele Buratti et al.   RNA Biology

TDP-43 Dimerizes in Human Cells in Culture

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

Molecular Neuropathology of TDP-43 Proteinopathies

(2009) Manuela Neumann   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

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

Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery

(2009) Brian D. Freibaum et al.   JOURNAL OF PROTEOME RESEARCH

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo

(2009) A. D'Ambrogio et al.   NUCLEIC ACIDS RESEARCH

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

Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

(2008) Lionel M. Igaz et al.   AMERICAN JOURNAL OF PATHOLOGY

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

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS

(2008) Yuki Inukai et al.   FEBS LETTERS

A90V TDP-43 variant results in the aberrant localization of TDP-43 in vitro

(2008) Matthew J. Winton et al.   FEBS LETTERS

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

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

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

TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis

(2008) Vivianna M Van Deerlin et al.   LANCET NEUROLOGY

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

(2008) J. Sreedharan et al.   SCIENCE