Related references
Note: Only part of the references are listed.Cytoplasmic TDP-43 is involved in cell fate during stress recovery
Youn-Bok Lee et al.
HUMAN MOLECULAR GENETICS (2022)
The roles ofhnRNP A2/B1inRNAbiology and disease
Yu Liu et al.
WILEY INTERDISCIPLINARY REVIEWS-RNA (2021)
RNA-Binding Proteins and the Complex Pathophysiology of ALS
Wanil Kim et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)
RNA Quality in Post-mortem Human Brain Tissue Is Affected by Alzheimer's Disease
Blake Highet et al.
FRONTIERS IN MOLECULAR NEUROSCIENCE (2021)
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Alistair Wood et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)
A Comprehensive Analysis of the Role of hnRNP A1 Function and Dysfunction in the Pathogenesis of Neurodegenerative Disease
Joseph P. Clarke et al.
FRONTIERS IN MOLECULAR BIOSCIENCES (2021)
Molecular, functional, and pathological aspects of TDP-43 fragmentation
Deepak Chhangani et al.
ISCIENCE (2021)
Mechanisms of TDP-43 Proteinopathy Onset and Propagation
Han-Jou Chen et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)
RNA Droplets
Kevin Rhine et al.
ANNUAL REVIEW OF BIOPHYSICS, VOL 49, 2020 (2020)
Cytoplasmic localization of amyotrophic lateral sclerosis-related TDP-43 proteins modulates stress granule formation
Corinne Besnard-Guerin
EUROPEAN JOURNAL OF NEUROSCIENCE (2020)
Dysregulation of RNA-Binding Proteins in Amyotrophic Lateral Sclerosis
Yuan Chao Xue et al.
FRONTIERS IN MOLECULAR NEUROSCIENCE (2020)
Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43
Mirella Vivoli-Vega et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2020)
The role of TDP-43 mislocalization in amyotrophic lateral sclerosis
Terry R. Suk et al.
MOLECULAR NEURODEGENERATION (2020)
Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseases
Gina Picchiarelli et al.
CELL STRESS (2020)
Improved detection of RNA foci in C9orf72 amyotrophic lateral sclerosis post-mortem tissue using BaseScope™ shows a lack of association with cognitive dysfunction
Arpan R. Mehta et al.
BRAIN COMMUNICATIONS (2020)
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43
Jacob R. Mann et al.
NEURON (2019)
Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions
Julia K. Nussbacher et al.
NEURON (2019)
Stress granules and neurodegeneration
Benjamin Wolozin et al.
NATURE REVIEWS NEUROSCIENCE (2019)
RNA Binding Proteins and the Pathogenesis of Frontotemporal Lobar Degeneration
Jeffrey W. Hofmann et al.
ANNUAL REVIEW OF PATHOLOGY: MECHANISMS OF DISEASE, VOL 14 (2019)
Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation
Youjun Chen et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
TDP-43 aggregation inside micronuclei reveals a potential mechanism for protein inclusion formation in ALS
Cristian A. Droppelmann et al.
SCIENTIFIC REPORTS (2019)
The TIA1 RNA-Binding Protein Family Regulates EIF2AK2-Mediated Stress Response and Cell Cycle Progression
Cindy Meyer et al.
MOLECULAR CELL (2018)
Abnormal RNA stability in amyotrophic lateral sclerosis
E. M. Tank et al.
NATURE COMMUNICATIONS (2018)
Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions
Miguel Mompean et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics
Ian R. Mackenzie et al.
NEURON (2017)
TIA-1 RRM23 binding and recognition of target oligonucleotides
Saboora Waris et al.
NUCLEIC ACIDS RESEARCH (2017)
Pathology of Neurodegenerative Diseases
Brittany N. Dugger et al.
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2017)
The N-terminal dimerization is required for TDP-43 splicing activity
Lei-Lei Jiang et al.
SCIENTIFIC REPORTS (2017)
RNA-binding proteins with prion-like domains in health and disease
Alice Ford Harrison et al.
BIOCHEMICAL JOURNAL (2017)
Determinants of affinity and specificity in RNA-binding proteins
Stephanie Helder et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2016)
Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology
Hui Yang et al.
FEBS JOURNAL (2016)
Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies
Roberta Cascella et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2016)
Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death
Shangxi Xiao et al.
ACTA NEUROPATHOLOGICA (2015)
T-cell intracellular antigens in health and disease
Carmen Sanchez-Jimenez et al.
CELL CYCLE (2015)
TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA
Mei-Xia Che et al.
FEBS LETTERS (2015)
G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA
Anais Aulas et al.
JOURNAL OF CELL BIOLOGY (2015)
Review: Prion-like mechanisms of transactive response DNA binding protein of 43kDa (TDP-43) in amyotrophic lateral sclerosis (ALS)
P. Smethurst et al.
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY (2015)
Emerging Roles of Disordered Sequences in RNA-Binding Proteins
Sara Calabretta et al.
TRENDS IN BIOCHEMICAL SCIENCES (2015)
RNA Recognition and Stress Granule Formation by TIA Proteins
Saboora Waris et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2014)
Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis
Janel O. Johnson et al.
NATURE NEUROSCIENCE (2014)
Accumulation of C-terminal fragments of transactive response DNA-binding protein 43 leads to synaptic loss and cognitive deficits in human TDP-43 transgenic mice
David X. Medina et al.
NEUROBIOLOGY OF AGING (2014)
Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: Implication in a loss-of-function pathology
Hui Yang et al.
SCIENTIFIC REPORTS (2014)
PABPN1: molecular function and muscle disease
Ayan Banerjee et al.
FEBS JOURNAL (2013)
RNA binding mediates neurotoxicity in the transgenic Drosophila model of TDP-43 proteinopathy
Ryoko Ihara et al.
HUMAN MOLECULAR GENETICS (2013)
Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion
Lei-Lei Jiang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Hong Joo Kim et al.
NATURE (2013)
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
Peter J. Lukavsky et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2013)
Characterizing TDP-43 interaction with its RNA targets
Amit Bhardwaj et al.
NUCLEIC ACIDS RESEARCH (2013)
Inhibition of TDP-43 Aggregation by Nucleic Acid Binding
Yi-Chen Huang et al.
PLOS ONE (2013)
Cellular Model of TAR DNA-binding Protein 43 (TDP-43) Aggregation Based on Its C-terminal Gln/Asn-rich Region
Mauricio Budini et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
UG Repeats/TDP-43 Interactions near 5′ Splice Sites Exert Unpredictable Effects on Splicing Modulation
Monica Passoni et al.
JOURNAL OF MOLECULAR BIOLOGY (2012)
The Aggregation and Neurotoxicity of TDP-43 and Its ALS-Associated 25 kDa Fragment Are Differentially Affected by Molecular Chaperones in Drosophila
Jenna M. Gregory et al.
PLOS ONE (2012)
Spinocerebellar ataxia type 2 (SCA2) is associated with TDP-43 pathology
Yasuko Toyoshima et al.
ACTA NEUROPATHOLOGICA (2011)
Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
Mei-Xia Che et al.
FASEB JOURNAL (2011)
A Two-hit Hypothesis for Inclusion Formation by Carboxyl-terminal Fragments of TDP-43 Protein Linked to RNA Depletion and Impaired Microtubule-dependent Transport
G. Scott Pesiridis et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2011)
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
James R. Tollervey et al.
NATURE NEUROSCIENCE (2011)
Characterization of Alternative Isoforms and Inclusion Body of the TAR DNA-binding Protein-43
Yoshinori Nishimoto et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery
Brian D. Freibaum et al.
JOURNAL OF PROTEOME RESEARCH (2010)
Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
Andrew C. Elden et al.
NATURE (2010)
The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
Emanuele Buratti et al.
RNA BIOLOGY (2010)
Rethinking ALS: The FUS about TDP-43
Clotilde Lagier-Tourenne et al.
CELL (2009)
RNA recognition motifs:: boring?: Not quite
Antoine Clery et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2008)
Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
Matthew J. Winton et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Tetsuaki Arai et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2006)
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Manuela Neumann et al.
SCIENCE (2006)
TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail - An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
E Buratti et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Human, Drosophila, and C-elegans TDP43:: Nucleic acid binding properties and splicing regulatory function
YM Ayala et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
E Buratti et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)