Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins
暂无分享,去创建一个
[1] G. Dreyfuss,et al. Messenger-RNA-binding proteins and the messages they carry , 2002, Nature Reviews Molecular Cell Biology.
[2] C. Geula,et al. 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, Acta Neuropathologica.
[3] J. Trojanowski,et al. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration , 2011, Nature Reviews Neuroscience.
[4] E. Buratti,et al. TDP-43 high throughput screening analyses in neurodegeneration: Advantages and pitfalls , 2013, Molecular and Cellular Neuroscience.
[5] O. King,et al. Prion-like disorders: blurring the divide between transmissibility and infectivity , 2010, Journal of Cell Science.
[6] D. Laurents,et al. Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43. , 2015, The journal of physical chemistry letters.
[7] M. Strong,et al. TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein , 2007, Molecular and Cellular Neuroscience.
[8] Stephanie C Huelga,et al. Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs , 2012, Nature Neuroscience.
[9] A. Yamaguchi,et al. The Effect of PRMT1-Mediated Arginine Methylation on the Subcellular Localization, Stress Granules, and Detergent-Insoluble Aggregates of FUS/TLS , 2012, PloS one.
[10] C. Sephton,et al. TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development* , 2009, The Journal of Biological Chemistry.
[11] Chi‐Huey Wong,et al. Heat-shock protein dysregulation is associated with functional and pathological TDP-43 aggregation , 2013, Nature Communications.
[12] Thomas Tuschl,et al. Evolutionary conservation and expression of human RNA-binding proteins and their role in human genetic disease. , 2014, Advances in experimental medicine and biology.
[13] T. Takumi,et al. TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines , 2005, Journal of Cell Science.
[14] P. Drapeau,et al. Loss and gain of FUS function impair neuromuscular synaptic transmission in a genetic model of ALS. , 2013, Human molecular genetics.
[15] I. Bozzoni,et al. An ALS-associated mutation in the FUS 3′-UTR disrupts a microRNA–FUS regulatory circuitry , 2014, Nature Communications.
[16] I. Bozzoni,et al. FUS stimulates microRNA biogenesis by facilitating co‐transcriptional Drosha recruitment , 2012, The EMBO journal.
[17] G. Halliday,et al. Long noncoding RNAs in TDP-43 and FUS/TLS-related frontotemporal lobar degeneration (FTLD) , 2015, Neurobiology of Disease.
[18] H. Kretzschmar,et al. A new subtype of frontotemporal lobar degeneration with FUS pathology. , 2009, Brain : a journal of neurology.
[19] E. Goodall,et al. Neuronal dark matter: the emerging role of microRNAs in neurodegeneration , 2013, Front. Cell. Neurosci..
[20] I-Fan Wang,et al. TDP‐43, the signature protein of FTLD‐U, is a neuronal activity‐responsive factor , 2008, Journal of neurochemistry.
[21] Gene W. Yeo,et al. ALS-causative mutations in FUS/TLS confer gain- and loss-of-function by altered association with SMN and U1-snRNP , 2015, Nature Communications.
[22] M. Heller,et al. FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors , 2015, Nucleic acids research.
[23] Chris Sander,et al. RNA targets of wild-type and mutant FET family proteins , 2011, Nature Structural &Molecular Biology.
[24] D. Mann,et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. , 2013, Cell reports.
[25] E. Wang,et al. Characterization of FUS Mutations in Amyotrophic Lateral Sclerosis Using RNA-Seq , 2013, PloS one.
[26] E. Rogaeva,et al. MTHFSD and DDX58 are novel RNA-binding proteins abnormally regulated in amyotrophic lateral sclerosis. , 2016, Brain : a journal of neurology.
[27] R. Tibbetts,et al. Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA* , 2010, The Journal of Biological Chemistry.
[28] S. Richard,et al. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. , 2012, Human molecular genetics.
[29] A. Iaconcig,et al. TDP-43 regulates β-adducin (Add2) transcript stability , 2014, RNA biology.
[30] Virander S. Chauhan,et al. Delineation of the Core Aggregation Sequences of TDP‐43 C‐Terminal Fragment , 2011, Chembiochem : a European journal of chemical biology.
[31] J L Haines,et al. Supporting Online Material Materials and Methods Figs. S1 to S7 Tables S1 to S4 References Mutations in the Fus/tls Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis , 2022 .
[32] C. Desnuelle,et al. Deciphering spreading mechanisms in amyotrophic lateral sclerosis: clinical evidence and potential molecular processes. , 2015, Current opinion in neurology.
[33] F. Moreau-Gachelin,et al. Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads , 2005, Neuroscience Letters.
[34] Tomaž Curk,et al. Analysis of alternative splicing associated with aging and neurodegeneration in the human brain. , 2011, Genome research.
[35] Olaf Ansorge,et al. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. , 2011, Brain : a journal of neurology.
[36] Christian Haass,et al. Stress granules in neurodegeneration – lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma , 2013, The FEBS journal.
[37] Elise M. Stewart,et al. SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation , 2015, Molecular Neurodegeneration.
[38] C. Troakes,et al. Compromised paraspeckle formation as a pathogenic factor in FUSopathies , 2013, Human molecular genetics.
[39] A. Gitler,et al. TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity* , 2009, The Journal of Biological Chemistry.
[40] T. Shelkovnikova. Modelling FUSopathies: focus on protein aggregation. , 2013, Biochemical Society transactions.
[41] A. Kakita,et al. Alteration of POLDIP3 Splicing Associated with Loss of Function of TDP-43 in Tissues Affected with ALS , 2012, PloS one.
[42] M. Neumann. Frontotemporal lobar degeneration and amyotrophic lateral sclerosis: molecular similarities and differences. , 2013, Revue neurologique.
[43] Xun Hu,et al. TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis , 2008, Science.
[44] J. Ule,et al. Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43 , 2013, Nature Structural &Molecular Biology.
[45] I. Bozzoni,et al. TDP-43 Regulates the Microprocessor Complex Activity During In Vitro Neuronal Differentiation , 2013, Molecular Neurobiology.
[46] C. Glass,et al. Induced ncRNAs Allosterically Modify RNA Binding Proteins in cis to Inhibit Transcription , 2008, Nature.
[47] Li-Huei Tsai,et al. Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons , 2013, Nature Neuroscience.
[48] Michael Benatar,et al. Prion-like domain mutations in hnRNPs cause multisystem proteinopathy and ALS , 2013, Nature.
[49] M. Mangelsdorf,et al. Identification of RNA bound to the TDP-43 ribonucleoprotein complex in the adult mouse brain , 2013, Amyotrophic lateral sclerosis & frontotemporal degeneration.
[50] Hyung-Jun Kim,et al. Prion-like Mechanism in Amyotrophic Lateral Sclerosis: are Protein Aggregates the Key? , 2014, Experimental neurobiology.
[51] Thomas C Roberts,et al. The role of long non-coding RNAs in neurodevelopment, brain function and neurological disease , 2014, Philosophical Transactions of the Royal Society B: Biological Sciences.
[52] R. Baloh. How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other? , 2012, Current opinion in neurology.
[53] Virander S. Chauhan,et al. Self-assembling properties of peptides derived from TDP-43 C-terminal fragment. , 2014, Langmuir : the ACS journal of surfaces and colloids.
[54] Gene W. Yeo,et al. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43 , 2011, Nature Neuroscience.
[55] G. Mills,et al. Tat‐activating regulatory DNA‐binding protein regulates glycolysis in hepatocellular carcinoma by regulating the platelet isoform of phosphofructokinase through microRNA 520 , 2013, Hepatology.
[56] M. Mann,et al. Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA , 2016, Science.
[57] L. Petrucelli,et al. TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor. , 2016, Human molecular genetics.
[58] Peter K. Todd,et al. Neurodegeneration the RNA way , 2012, Progress in Neurobiology.
[59] N. Nukina,et al. A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions*♦ , 2011, The Journal of Biological Chemistry.
[60] R. Shiekhattar,et al. The Microprocessor complex mediates the genesis of microRNAs , 2004, Nature.
[61] Kinji Ohno,et al. Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions , 2012, Scientific Reports.
[62] I-Fan Wang,et al. TDP-43 Overexpression Enhances Exon 7 Inclusion during the Survival of Motor Neuron Pre-mRNA Splicing* , 2008, Journal of Biological Chemistry.
[63] S. Gygi,et al. FUS-SMN protein interactions link the motor neuron diseases ALS and SMA. , 2012, Cell reports.
[64] Frederick P. Roth,et al. Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes , 2010, The Journal of Biological Chemistry.
[65] R. Chitta,et al. Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. , 2010, Journal of proteome research.
[66] M. Mayr,et al. Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport , 2015, Neuroscience.
[67] V. Buchman,et al. Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm , 2013, Cell cycle.
[68] N. Shneider,et al. The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span. , 2011, The Journal of clinical investigation.
[69] P. Callaerts,et al. TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis? , 2014, Trends in molecular medicine.
[70] T. Takumi,et al. Myosin-Va Facilitates the Accumulation of mRNA/Protein Complex in Dendritic Spines , 2006, Current Biology.
[71] Lorne Zinman,et al. Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis , 2014, Nature Neuroscience.
[72] Y. Hayashi,et al. An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation. , 1994, Cancer research.
[73] J. Dubnau,et al. Transposable Elements in TDP-43-Mediated Neurodegenerative Disorders , 2012, PloS one.
[74] M. Cozzolino,et al. Mislocalised FUS mutants stall spliceosomal snRNPs in the cytoplasm , 2013, Neurobiology of Disease.
[75] K. Wada,et al. TDP‐43 associates with stalled ribosomes and contributes to cell survival during cellular stress , 2013, Journal of neurochemistry.
[76] Yun-Ru Chen,et al. Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients , 2014, Nature Communications.
[77] C. DeCarli,et al. Detection of TDP‐43 oligomers in frontotemporal lobar degeneration–TDP , 2015, Annals of neurology.
[78] T. Hashikawa,et al. FUS/TLS deficiency causes behavioral and pathological abnormalities distinct from amyotrophic lateral sclerosis , 2015, Acta Neuropathologica Communications.
[79] P. Alexiou,et al. FUS regulates genes coding for RNA-binding proteins in neurons by binding to their highly conserved introns. , 2013, RNA.
[80] K. Eggan,et al. Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations , 2014, Neuron.
[81] V. Buchman,et al. Fused in Sarcoma (FUS) Protein Lacking Nuclear Localization Signal (NLS) and Major RNA Binding Motifs Triggers Proteinopathy and Severe Motor Phenotype in Transgenic Mice , 2013, The Journal of Biological Chemistry.
[82] Yong Yu,et al. U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish , 2015, Nucleic acids research.
[83] J. Ule,et al. Hexanucleotide Repeats in ALS/FTD Form Length-Dependent RNA Foci, Sequester RNA Binding Proteins, and Are Neurotoxic , 2013, Cell reports.
[84] M. Berciano,et al. TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons. , 2009, Journal of structural biology.
[85] John L. Robinson,et al. TDP-43 skeins show properties of amyloid in a subset of ALS cases , 2012, Acta Neuropathologica.
[86] M. Ohki,et al. Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes. , 1998, Gene.
[87] S. Apolloni,et al. MicroRNAs: newcomers into the ALS picture. , 2015, CNS & neurological disorders drug targets.
[88] J. Hardy,et al. Review: Prion‐like mechanisms of transactive response DNA binding protein of 43 kDa (TDP‐43) in amyotrophic lateral sclerosis (ALS) , 2015, Neuropathology and applied neurobiology.
[89] J. Morris,et al. TDP‐43 A315T mutation in familial motor neuron disease , 2008, Annals of neurology.
[90] G. Lederkremer,et al. Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress , 2013, Nature Communications.
[91] R. Baloh,et al. TDP-43-Based Animal Models of Neurodegeneration: New Insights into ALS Pathology and Pathophysiology , 2010, Neurodegenerative Diseases.
[92] E. Kremmer,et al. Arginine methylation next to the PY‐NLS modulates Transportin binding and nuclear import of FUS , 2012, The EMBO journal.
[93] B. Traynor,et al. The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients , 2012, Acta Neuropathologica.
[94] B. McConkey,et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis , 2008, Nature Genetics.
[95] A. Kakita,et al. TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation , 2007, Acta Neuropathologica.
[96] 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.
[97] G. Rouleau,et al. TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. , 2011, Human molecular genetics.
[98] R. Bowser,et al. RBM45 homo-oligomerization mediates association with ALS-linked proteins and stress granules , 2015, Scientific Reports.
[99] E. Buratti,et al. Nuclear factor TDP‐43 can affect selected microRNA levels , 2010, The FEBS journal.
[100] Vincenzo Silani,et al. TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like Cells* , 2012, The Journal of Biological Chemistry.
[101] M. Pennuto,et al. Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo , 2013, PloS one.
[102] S. Weber,et al. TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6 , 2011, Molecular Neurodegeneration.
[103] Runsheng Chen,et al. Transcriptome-wide analysis of TDP-43 binding small RNAs identifies miR-NID1 (miR-8485), a novel miRNA that represses NRXN1 expression. , 2014, Genomics.
[104] Yi Zhao,et al. A liver-enriched long non-coding RNA, lncLSTR, regulates systemic lipid metabolism in mice. , 2015, Cell metabolism.
[105] G. Sobue,et al. Position-specific binding of FUS to nascent RNA regulates mRNA length , 2015, Genes & development.
[106] A. Levey,et al. Multiplex SILAC Analysis of a Cellular TDP-43 Proteinopathy Model Reveals Protein Inclusions Associated with SUMOylation and Diverse Polyubiquitin Chains* , 2010, Molecular & Cellular Proteomics.
[107] H. Okano,et al. The long non-coding RNA nuclear-enriched abundant transcript 1_2 induces paraspeckle formation in the motor neuron during the early phase of amyotrophic lateral sclerosis , 2013, Molecular Brain.
[108] G. Sobue,et al. FUS regulates AMPA receptor function and FTLD/ALS-associated behaviour via GluA1 mRNA stabilization , 2015, Nature Communications.
[109] Y. Kawahara,et al. TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes , 2012, Proceedings of the National Academy of Sciences.
[110] D. Laurents,et al. "Structural characterization of the minimal segment of TDP-43 competent for aggregation". , 2014, Archives of biochemistry and biophysics.
[111] Xun Hu,et al. Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6 , 2009, Science.
[112] I. Mackenzie,et al. ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import , 2010, The EMBO journal.
[113] K. Eggan,et al. FUS is sequestered in nuclear aggregates in ALS patient fibroblasts , 2014, Molecular biology of the cell.
[114] Deyu Li,et al. TDP-43 is intercellularly transmitted across axon terminals , 2015, The Journal of cell biology.
[115] F. Baralle,et al. Aggregate formation prevents dTDP-43 neurotoxicity in the Drosophila melanogaster eye , 2014, Neurobiology of Disease.
[116] D. Cleveland,et al. Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis , 2013, Neuron.
[117] J. Hardy,et al. Motor neuron disease and frontotemporal dementia: sometimes related, sometimes not , 2014, Experimental Neurology.
[118] T. Haystead,et al. The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules , 2013, The Journal of cell biology.
[119] G. Hicks,et al. The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology , 2005, Current Biology.
[120] E. Buratti. Functional Significance of TDP-43 Mutations in Disease. , 2015, Advances in genetics.
[121] T. Cech,et al. FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2. , 2012, Genes & development.
[122] 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.
[123] L. Petrucelli,et al. Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor , 2012, Proceedings of the National Academy of Sciences.
[124] G. Bassell,et al. Making and breaking synapses through local mRNA regulation. , 2011, Current opinion in genetics & development.
[125] F. Chiti,et al. TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells , 2014, PloS one.
[126] J. Rouse,et al. Identification and characterization of FUS/TLS as a new target of ATM. , 2008, The Biochemical journal.
[127] Yong Yu,et al. FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP , 2015, Proceedings of the National Academy of Sciences.
[128] Robert V Farese,et al. Downregulation of MicroRNA-9 in iPSC-Derived Neurons of FTD/ALS Patients with TDP-43 Mutations , 2013, PloS one.
[129] N. Proudfoot,et al. Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection. , 2012, Genes & development.
[130] Ewout J. N. Groen,et al. Protein aggregation in amyotrophic lateral sclerosis , 2013, Acta Neuropathologica.
[131] Jing Chen,et al. Self-assembled FUS binds active chromatin and regulates gene transcription , 2014, Proceedings of the National Academy of Sciences.
[132] Gene W. Yeo,et al. RNA-binding proteins in neurodegeneration: Seq and you shall receive , 2015, Trends in Neurosciences.
[133] Petr Klus,et al. Neurodegenerative diseases: quantitative predictions of protein-RNA interactions. , 2013, RNA.
[134] E. Buratti,et al. TDP-43: gumming up neurons through protein-protein and protein-RNA interactions. , 2012, Trends in biochemical sciences.
[135] Ju-Seog Lee,et al. Identification of a subnuclear body involved in sequence-specific cytokine RNA processing , 2015, Nature Communications.
[136] J. Trojanowski,et al. An acetylation switch controls TDP-43 function and aggregation propensity , 2015, Nature Communications.
[137] Wenlung Chen,et al. Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis. , 2010, Journal of the American Chemical Society.
[138] Virgil Muresan,et al. Shared Molecular Mechanisms in Alzheimer's Disease and Amyotrophic Lateral Sclerosis: Neurofilament-Dependent Transport of sAPP, FUS, TDP-43 and SOD1, with Endoplasmic Reticulum-Like Tubules , 2015, Neurodegenerative Diseases.
[139] G. Rouleau,et al. TARDBP and FUS Mutations Associated with Amyotrophic Lateral Sclerosis: Summary and Update , 2013, Human mutation.
[140] C. Lien,et al. TDP-43 regulates the mammalian spinogenesis through translational repression of Rac1 , 2012, Acta Neuropathologica.
[141] Chen Wang,et al. An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity , 2011, Nature Structural &Molecular Biology.
[142] E. Buratti,et al. From transcriptomic to protein level changes in TDP-43 and FUS loss-of-function cell models. , 2015, Biochimica et biophysica acta.
[143] Adam S. Mastrocola,et al. The RNA-binding Protein Fused in Sarcoma (FUS) Functions Downstream of Poly(ADP-ribose) Polymerase (PARP) in Response to DNA Damage* , 2013, The Journal of Biological Chemistry.
[144] Ji Han Kim,et al. A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43. , 2011, Human molecular genetics.
[145] Bruce L. Miller,et al. Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis , 2006, Science.
[146] C. Broeckhoven,et al. hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations , 2013, Acta Neuropathologica.
[147] R. Wickner,et al. FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis , 2011, Protein & Cell.
[148] N. Mandahl,et al. Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma , 1993, Nature.
[149] Zuoshang Xu. Does a loss of TDP-43 function cause neurodegeneration? , 2012, Molecular Neurodegeneration.
[150] Qinghua Zhou,et al. Regulation of MALAT1 expression by TDP43 controls the migration and invasion of non-small cell lung cancer cells in vitro. , 2015, Biochemical and biophysical research communications.
[151] B. Wolozin,et al. Role of Stress Granules and RNA-Binding Proteins in Neurodegeneration: A Mini-Review , 2013, Gerontology.
[152] E. Rogaeva,et al. RNA targets of TDP-43 identified by UV-CLIP are deregulated in ALS , 2011, Molecular and Cellular Neuroscience.
[153] W. Rossoll,et al. The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth. , 2012, Human molecular genetics.
[154] C. Haass,et al. TDP-43 and FUS: a nuclear affair , 2011, Trends in Neurosciences.
[155] E. Buratti,et al. The molecular links between TDP-43 dysfunction and neurodegeneration. , 2009, Advances in genetics.
[156] Huilin Zhou,et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS , 2010, Proceedings of the National Academy of Sciences.
[157] D. Edbauer,et al. FUS-mediated alternative splicing in the nervous system: consequences for ALS and FTLD , 2013, Journal of Molecular Medicine.
[158] M. Strong,et al. RNA-binding proteins as molecular links between cancer and neurodegeneration , 2014, Biogerontology.
[159] E. Buratti,et al. TBPH/TDP-43 modulates translation of Drosophila futsch mRNA through an UG-rich sequence within its 5′UTR , 2016, Brain Research.
[160] C. Haass,et al. Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration , 2013, Molecular and Cellular Neuroscience.
[161] A. Gitler,et al. Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS , 2011, PLoS biology.
[162] G. Hicks,et al. ALS-Associated FUS Mutations Result in Compromised FUS Alternative Splicing and Autoregulation , 2013, PLoS genetics.
[163] J. Ule,et al. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. , 2011, Nature neuroscience.
[164] H. Ruley,et al. Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death , 2000, Nature Genetics.
[165] T. Golde. The therapeutic importance of understanding mechanisms of neuronal cell death in neurodegenerative disease , 2009, Molecular Neurodegeneration.
[166] D. Burns,et al. TDP-43, an ALS Linked Protein, Regulates Fat Deposition and Glucose Homeostasis , 2013, PloS one.
[167] Daniela C. Zarnescu,et al. Futsch/MAP1B mRNA Is a Translational Target of TDP-43 and Is Neuroprotective in a Drosophila Model of Amyotrophic Lateral Sclerosis , 2014, The Journal of Neuroscience.
[168] J. Trojanowski,et al. Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations , 2007, Annals of neurology.
[169] D. Srivastava,et al. The RNA-binding Protein TDP-43 Selectively Disrupts MicroRNA-1/206 Incorporation into the RNA-induced Silencing Complex*♦ , 2014, The Journal of Biological Chemistry.
[170] Jernej Ule,et al. TDP‐43 regulates its mRNA levels through a negative feedback loop , 2011, The EMBO journal.
[171] 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.
[172] I. Mackenzie,et al. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia , 2010, The Lancet Neurology.
[173] G. Sobue,et al. The ALS/FTLD-related RNA-binding proteins TDP-43 and FUS have common downstream RNA targets in cortical neurons☆ , 2013, FEBS open bio.
[174] T. Hortobágyi,et al. Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration. , 2010, Brain : a journal of neurology.
[175] M. Gorospe,et al. Long noncoding RNAs (lncRNAs) and the molecular hallmarks of aging , 2014, Aging.
[176] E. Brustein,et al. FUS and TARDBP but Not SOD1 Interact in Genetic Models of Amyotrophic Lateral Sclerosis , 2011, PLoS genetics.
[177] Robert H. Brown,et al. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. , 2010, Human molecular genetics.
[178] Stuart A. Wilson,et al. Sequestration of multiple RNA recognition motif-containing proteins by C9orf72 repeat expansions , 2014, Brain : a journal of neurology.
[179] I. Mackenzie,et al. FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis , 2012, Brain Research.
[180] Y. Chern,et al. The Influence of Pathological Mutations and Proline Substitutions in TDP-43 Glycine-Rich Peptides on Its Amyloid Properties and Cellular Toxicity , 2014, PloS one.
[181] E. Buratti,et al. TDP‐43 is recruited to stress granules in conditions of oxidative insult , 2009, Journal of neurochemistry.
[182] Anke Busch,et al. Evolution of SR protein and hnRNP splicing regulatory factors , 2012, Wiley interdisciplinary reviews. RNA.
[183] A. Levey,et al. Coaggregation of RNA-Binding Proteins in a Model of TDP-43 Proteinopathy with Selective RGG Motif Methylation and a Role for RRM1 Ubiquitination , 2012, PloS one.
[184] D. Ron,et al. Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation* , 1999, The Journal of Biological Chemistry.
[185] Fumiaki Tanaka,et al. Spliceosome integrity is defective in the motor neuron diseases ALS and SMA , 2013, EMBO molecular medicine.
[186] T. Cech,et al. Nucleic acid-binding specificity of human FUS protein , 2015, Nucleic acids research.
[187] A. Aulas,et al. Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS? , 2015, Front. Cell. Neurosci..
[188] Majid Hafezparast,et al. PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage , 2013, Nucleic acids research.
[189] Nejc Haberman,et al. Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain , 2012, Scientific Reports.
[190] A. Zell,et al. TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR , 2011, Nucleic acids research.
[191] Oliver D. King,et al. Stress granules as crucibles of ALS pathogenesis , 2013, The Journal of cell biology.
[192] T. Dörk,et al. Nuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping , 2001, The EMBO journal.
[193] M. Mann,et al. Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry. , 1995, RNA.
[194] D. Cleveland,et al. Prion-like spread of protein aggregates in neurodegeneration , 2012, The Journal of experimental medicine.
[195] N. Cairns,et al. Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects , 2012, Acta Neuropathologica.
[196] Q. Zhan,et al. Long non‐coding RNA gadd7 interacts with TDP‐43 and regulates Cdk6 mRNA decay , 2012, The EMBO journal.
[197] J. Jankovic,et al. The role of FUS gene variants in neurodegenerative diseases , 2014, Nature Reviews Neurology.
[198] E. Buratti,et al. TDP-43 Regulates Drosophila Neuromuscular Junctions Growth by Modulating Futsch/MAP1B Levels and Synaptic Microtubules Organization , 2011, PloS one.
[199] Gang Yu,et al. The function of RNA-binding proteins at the synapse: implications for neurodegeneration , 2015, Cellular and Molecular Life Sciences.
[200] T. Kigawa,et al. Aberrant Assembly of RNA Recognition Motif 1 Links to Pathogenic Conversion of TAR DNA-binding Protein of 43 kDa (TDP-43)* , 2013, The Journal of Biological Chemistry.