The N-terminal dimerization is required for TDP-43 splicing activity
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Title
The N-terminal dimerization is required for TDP-43 splicing activity
Authors
Keywords
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Journal
Scientific Reports
Volume 7, Issue 1, Pages -
Publisher
Springer Nature
Online
2017-07-17
DOI
10.1038/s41598-017-06263-3
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Note: Only part of the references are listed.- The TDP-43 N-terminal domain structure at high resolution
- (2016) Miguel Mompeán et al. FEBS Journal
- Untangling the structure of the TDP-43 N-terminal domain
- (2016) Chung-ke Chang et al. FEBS Journal
- 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
- Structural insights into the multi-determinant aggregation of TDP-43 in motor neuron-like cells
- (2016) F. Bozzo et al. NEUROBIOLOGY OF DISEASE
- Which TDP-43 aggregates are toxic in ALS?
- (2016) Cristiana Valle et al. Oncotarget
- Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation
- (2016) Lei-Lei Jiang et al. Scientific Reports
- Interaction of RNA with a C-terminal fragment of the amyotrophic lateral sclerosis-associated TDP43 reduces cytotoxicity
- (2016) Akira Kitamura et al. Scientific Reports
- Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43
- (2015) Miguel Mompeán et al. Journal of Physical Chemistry Letters
- Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy
- (2015) Huayan Yang et al. Nature Protocols
- 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
- 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
- Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations
- (2014) Nael H. Alami et al. NEURON
- A new cellular model of pathological TDP-43: The neurotoxicity of stably expressed CTF25 of TDP-43 depends on the proteasome
- (2014) Y. Liu et al. NEUROSCIENCE
- 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
- 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
- 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
- (2013) David X. Medina et al. NEUROBIOLOGY OF AGING
- Characterizing TDP-43 interaction with its RNA targets
- (2013) Amit Bhardwaj et al. NUCLEIC ACIDS RESEARCH
- ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43
- (2013) E. S. Arnold et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 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
- 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
- Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)
- (2012) Eva Bentmann 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
- Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
- (2011) Mei-Xia Che et al. FASEB JOURNAL
- TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1
- (2011) Karli K. McDonald et al. HUMAN MOLECULAR GENETICS
- A “Two-hit” Hypothesis for Inclusion Formation by Carboxyl-terminal Fragments of TDP-43 Protein Linked to RNA Depletion and Impaired Microtubule-dependent Transport
- (2011) G. Scott Pesiridis et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
- (2011) James R Tollervey et al. NATURE NEUROSCIENCE
- Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
- (2011) Edward B. Lee et al. NATURE REVIEWS NEUROSCIENCE
- An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
- (2011) Weirui Guo et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism
- (2011) Chunxing Yang 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
- 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
- The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
- (2010) Emanuele Buratti et al. RNA Biology
- Rethinking ALS: The FUS about TDP-43
- (2009) Clotilde Lagier-Tourenne et al. CELL
- Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
- (2009) G. S. Pesiridis et al. HUMAN MOLECULAR GENETICS
- 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
- Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
- (2009) Y.-J. Zhang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 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
- TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
- (2008) J. Sreedharan et al. SCIENCE
- Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
- (2007) Emanuele Buratti Frontiers in Bioscience-Landmark
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