A panel of TDP-43-regulated splicing events verifies loss of TDP-43 function in amyotrophic lateral sclerosis brain tissue
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[1] P. Wong,et al. A fluid biomarker reveals loss of TDP-43 splicing repression in pre-symptomatic ALS , 2023, bioRxiv.
[2] M. Nalls,et al. Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS/FTD , 2023, bioRxiv.
[3] C. Link,et al. TDP-43 knockdown in mouse model of ALS leads to dsRNA deposition, gliosis, and neurodegeneration in the spinal cord. , 2022, Cerebral cortex.
[4] Emma L. Scotter,et al. Transcriptional targets of amyotrophic lateral sclerosis/frontotemporal dementia protein TDP-43 – meta-analysis and interactive graphical database , 2022, Disease Models & Mechanisms.
[5] Jane Y. Wu,et al. The amyotrophic lateral sclerosis-linked protein TDP-43 regulates interleukin-6 cytokine production by human brain pericytes , 2022, Molecular and Cellular Neuroscience.
[6] J. Winkelmann,et al. Fast versus slow disease progression in amyotrophic lateral sclerosis–clinical and genetic factors at the edges of the survival spectrum , 2022, Neurobiology of Aging.
[7] J. Douwes,et al. Serum biomarkers of neuroinflammation and blood-brain barrier leakage in amyotrophic lateral sclerosis , 2022, BMC Neurology.
[8] Anna L. Brown,et al. TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A , 2022, Nature.
[9] H. Kang,et al. Microscopic examination of spatial transcriptome using Seq-Scope , 2021, Cell.
[10] Caitlin M. Rodriguez,et al. TDP-43 represses cryptic exon inclusion in the FTD–ALS gene UNC13A , 2021, Nature.
[11] G. Tucker-Kellogg,et al. TDP-43 maximizes nerve conduction velocity by repressing a cryptic exon for paranodal junction assembly in Schwann cells , 2021, eLife.
[12] N. Luscombe,et al. Reactive astrocytes in ALS display diminished intron retention , 2021, Nucleic acids research.
[13] F. Hirth,et al. Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation , 2021, Nature Reviews Neuroscience.
[14] Anna L. Brown,et al. Truncated stathmin-2 is a marker of TDP-43 pathology in frontotemporal dementia. , 2020, The Journal of clinical investigation.
[15] Steven L Salzberg,et al. Graph-based genome alignment and genotyping with HISAT2 and HISAT-genotype , 2019, Nature Biotechnology.
[16] Eddie B. Lee,et al. Loss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons , 2019, Cell reports.
[17] R. Rahbarghazi,et al. Targeting pericytes for neurovascular regeneration , 2019, Cell Communication and Signaling.
[18] M. Gos,et al. Correction to: Splicing mutations in human genetic disorders: examples, detection, and confirmation , 2019, Journal of Applied Genetics.
[19] Timothy A. Miller,et al. Postmortem Cortex Samples Identify Distinct Molecular Subtypes of ALS: Retrotransposon Activation, Oxidative Stress, and Activated Glia , 2019, bioRxiv.
[20] Michael J. Steinbaugh,et al. ALS IMPLICATED PROTEIN TDP-43 SUSTAINS LEVELS OF STMN2 A MEDIATOR OF MOTOR NEURON GROWTH AND REPAIR , 2019, Nature Neuroscience.
[21] F. Rigo,et al. Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration , 2018, Nature Neuroscience.
[22] R. Faull,et al. Markers for human brain pericytes and smooth muscle cells , 2018, Journal of Chemical Neuroanatomy.
[23] I. Ferrer,et al. Cryptic exon splicing function of TARDBP interacts with autophagy in nervous tissue , 2018, Autophagy.
[24] M. Dragunow,et al. Unique and shared inflammatory profiles of human brain endothelia and pericytes , 2018, Journal of Neuroinflammation.
[25] D. Rowe,et al. The genotype–phenotype landscape of familial amyotrophic lateral sclerosis in Australia , 2017, Clinical genetics.
[26] P. Wong,et al. Cryptic exon incorporation occurs in Alzheimer’s brain lacking TDP-43 inclusion but exhibiting nuclear clearance of TDP-43 , 2017, Acta Neuropathologica.
[27] J. Dittman,et al. Synaptic UNC13A protein variant causes increased neurotransmission and dyskinetic movement disorder , 2017, The Journal of clinical investigation.
[28] M. Dragunow,et al. Brain Pericytes As Mediators of Neuroinflammation. , 2017, Trends in pharmacological sciences.
[29] P. Wong,et al. Tdp-43 cryptic exons are highly variable between cell types , 2017, Molecular Neurodegeneration.
[30] A. Emili,et al. DLG5 connects cell polarity and Hippo signaling protein networks by linking PAR-1 with MST1/2 , 2016, Genes & development.
[31] H. Braak,et al. Pathological TDP-43 changes in Betz cells differ from those in bulbar and spinal α-motoneurons in sporadic amyotrophic lateral sclerosis , 2016, Acta Neuropathologica.
[32] V. Plagnol,et al. Quantitative analysis of cryptic splicing associated with TDP-43 depletion , 2016, bioRxiv.
[33] Jeffrey T Leek,et al. Transcript-level expression analysis of RNA-seq experiments with HISAT, StringTie and Ballgown , 2016, Nature Protocols.
[34] E. S. Graham,et al. TGF-beta1 regulates human brain pericyte inflammatory processes involved in neurovasculature function , 2016, Journal of Neuroinflammation.
[35] J. Trojanowski,et al. Transcriptomic Changes Due to Cytoplasmic TDP-43 Expression Reveal Dysregulation of Histone Transcripts and Nuclear Chromatin , 2015, PloS one.
[36] E. Buratti,et al. TDP-43 affects splicing profiles and isoform production of genes involved in the apoptotic and mitotic cellular pathways , 2015, Nucleic acids research.
[37] P. Wong,et al. TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD , 2015, Science.
[38] J. Trojanowski,et al. Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43 , 2015, Acta Neuropathologica.
[39] R. Faull,et al. An anti-inflammatory role for C/EBPδ in human brain pericytes , 2015, Scientific Reports.
[40] Christine Mayr,et al. Alternative 3'UTRs act as scaffolds to regulate membrane protein localization , 2015, Nature.
[41] Robert H. Brown,et al. Novel mutations support a role for Profilin 1 in the pathogenesis of ALS , 2015, Neurobiology of Aging.
[42] K. Talbot,et al. TARDBP pathogenic mutations increase cytoplasmic translocation of TDP-43 and cause reduction of endoplasmic reticulum Ca2+ signaling in motor neurons , 2015, Neurobiology of Disease.
[43] W. Huber,et al. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2 , 2014, Genome Biology.
[44] R. Huganir,et al. Dlg5 Regulates Dendritic Spine Formation and Synaptogenesis by Controlling Subcellular N-Cadherin Localization , 2014, The Journal of Neuroscience.
[45] M. Dragunow,et al. A role for human brain pericytes in neuroinflammation , 2014, Journal of Neuroinflammation.
[46] W. Koh,et al. Noninvasive in vivo monitoring of tissue-specific global gene expression in humans , 2014, Proceedings of the National Academy of Sciences.
[47] Juan Li,et al. DLG5 in Cell Polarity Maintenance and Cancer Development , 2014, International journal of biological sciences.
[48] P. Rustin,et al. Supernumerary subunits NDUFA3, NDUFA5 and NDUFA12 are required for the formation of the extramembrane arm of human mitochondrial complex I , 2014, FEBS letters.
[49] P. Callaerts,et al. TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis? , 2014, Trends in molecular medicine.
[50] Timothy Sterne-Weiler,et al. Exon identity crisis: disease-causing mutations that disrupt the splicing code , 2014, Genome Biology.
[51] Timothy Sterne-Weiler,et al. Exon identity crisis: disease-causing mutations that disrupt the splicing code , 2014, Genome Biology.
[52] D. Cleveland,et al. Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis , 2013, Neuron.
[53] Murray Grossman,et al. Stages of pTDP‐43 pathology in amyotrophic lateral sclerosis , 2013, Annals of neurology.
[54] G. Sobue,et al. Loss of TDP-43 causes age-dependent progressive motor neuron degeneration. , 2013, Brain : a journal of neurology.
[55] Gene W. Yeo,et al. ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43 , 2013, Proceedings of the National Academy of Sciences.
[56] A. Kakita,et al. Alteration of POLDIP3 Splicing Associated with Loss of Function of TDP-43 in Tissues Affected with ALS , 2012, PloS one.
[57] Jesse D. Sengillo,et al. Blood–spinal cord barrier pericyte reductions contribute to increased capillary permeability , 2012, Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism.
[58] S. C. Chafe,et al. Mutations in the Profilin 1 Gene Cause Familial Amyotrophic Lateral Sclerosis , 2012, Nature.
[59] Shane S. Sturrock,et al. Geneious Basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data , 2012, Bioinform..
[60] Helga Thorvaldsdóttir,et al. Integrative Genomics Viewer (IGV): high-performance genomics data visualization and exploration , 2012, Briefings Bioinform..
[61] W. Huber,et al. Detecting differential usage of exons from RNA-seq data , 2012, Genome research.
[62] J. Trojanowski,et al. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration , 2011, Nature Reviews Neuroscience.
[63] M. Esteller. Non-coding RNAs in human disease , 2011, Nature Reviews Genetics.
[64] S. Weber,et al. TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6 , 2011, Molecular Neurodegeneration.
[65] J. Ule,et al. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. , 2011, Nature neuroscience.
[66] Gene W. Yeo,et al. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43 , 2011, Nature Neuroscience.
[67] J. Ule,et al. Characterising the RNA targets and position-dependent splicing regulation by TDP-43; implications for neurodegenerative diseases , 2011, Nature Neuroscience.
[68] Thomas C. Südhof,et al. RIM Proteins Activate Vesicle Priming by Reversing Autoinhibitory Homodimerization of Munc13 , 2011, Neuron.
[69] Jernej Ule,et al. TDP‐43 regulates its mRNA levels through a negative feedback loop , 2011, The EMBO journal.
[70] Helga Thorvaldsdóttir,et al. Integrative Genomics Viewer , 2011, Nature Biotechnology.
[71] S. Akbarian,et al. The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism , 2010, PloS one.
[72] Bengt R. Johansson,et al. Pericytes regulate the blood–brain barrier , 2010, Nature.
[73] B. Barres,et al. Pericytes are required for blood–brain barrier integrity during embryogenesis , 2010, Nature.
[74] Frederick P. Roth,et al. Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes , 2010, The Journal of Biological Chemistry.
[75] J. Trojanowski,et al. Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP‐43 proteinopathies , 2010, Neuropathology : official journal of the Japanese Society of Neuropathology.
[76] S. Pereson,et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration , 2010, Proceedings of the National Academy of Sciences.
[77] E. Buratti,et al. Alternative splicing: role of pseudoexons in human disease and potential therapeutic strategies , 2010, The FEBS journal.
[78] N. Cairns,et al. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration , 2009, Proceedings of the National Academy of Sciences.
[79] M. Neumann,et al. Molecular Neuropathology of TDP-43 Proteinopathies , 2009, International journal of molecular sciences.
[80] D. Geschwind,et al. Novel Mutations in TARDBP (TDP-43) in Patients with Familial Amyotrophic Lateral Sclerosis , 2008, PLoS genetics.
[81] M. Morita,et al. Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis , 2008, Annals of neurology.
[82] J. Trojanowski,et al. Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation* , 2008, Journal of Biological Chemistry.
[83] Xun Hu,et al. TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis , 2008, Science.
[84] M. Curtis,et al. The collection and processing of human brain tissue for research , 2008, Cell and Tissue Banking.
[85] R. Faull,et al. Cellular composition of human glial cultures from adult biopsy brain tissue , 2007, Journal of Neuroscience Methods.
[86] H. Akiyama,et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. , 2006, Biochemical and biophysical research communications.
[87] Bruce L. Miller,et al. Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis , 2006, Science.
[88] S. Reske,et al. Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS and FTD , 2005, Annals of neurology.
[89] P. Lockhart,et al. Identification of the Human Ubiquitin Specific Protease 31 (USP31) Gene: Structure, Sequence and Expression Analysis , 2004, DNA sequence : the journal of DNA sequencing and mapping.
[90] Francisco E. Baralle,et al. Characterization and Functional Implications of the RNA Binding Properties of Nuclear Factor TDP-43, a Novel Splicing Regulator ofCFTR Exon 9* , 2001, The Journal of Biological Chemistry.
[91] Thomas C. Südhof,et al. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles , 1999, Nature.
[92] J. Smeitink,et al. cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. , 1998, Biochemical and biophysical research communications.
[93] G. Struhl,et al. Cis- acting sequences responsible for anterior localization of bicoid mRNA in Drosophila embryos , 1988, Nature.
[94] T. Curran,et al. Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[95] H. Braak,et al. Anterior Cingulate Cortex TDP-43 Pathology in Sporadic Amyotrophic Lateral Sclerosis , 2018, Journal of neuropathology and experimental neurology.
[96] E. Buratti. Functional Significance of TDP-43 Mutations in Disease. , 2015, Advances in genetics.
[97] Juan Li,et al. DLG5 in Cell Polarity Maintenance and Cancer , 2014 .
[98] E. Kieff,et al. Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB. , 2006, Cellular signalling.
[99] B. Madras,et al. Polymorphisms in the 3′-untranslated region of human and monkey dopamine transporter genes affect reporter gene expression , 2002, Molecular Psychiatry.