Stress granules in the spinal muscular atrophy and amyotrophic lateral sclerosis: The correlation and promising therapy

[1]  Stephen A. Goutman,et al.  Amyotrophic lateral sclerosis , 2022, Nature Reviews Disease Primers.

[2]  T. Iwatsubo,et al.  ALS-linked cytoplasmic FUS assemblies are compositionally different from physiological stress granules and sequester hnRNPA3, a novel modifier of FUS toxicity , 2021, Neurobiology of Disease.

[3]  Sinem Usluer,et al.  Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation , 2021, Frontiers in Molecular Biosciences.

[4]  Reilly L. Allison,et al.  Viral mediated knockdown of GATA6 in SMA iPSC‐derived astrocytes prevents motor neuron loss and microglial activation , 2021, bioRxiv.

[5]  Jing Dong,et al.  Syringic acid demonstrates promising protective effect against tau fibrillization and cytotoxicity through regulation of endoplasmic reticulum stress-mediated pathway as a prelude to Alzheimer's disease. , 2021, International journal of biological macromolecules.

[6]  S. Choi,et al.  Drug Discovery of Spinal Muscular Atrophy (SMA) from the Computational Perspective: A Comprehensive Review , 2021, International journal of molecular sciences.

[7]  Y. Chern,et al.  Contribution of Energy Dysfunction to Impaired Protein Translation in Neurodegenerative Diseases , 2021, Frontiers in Cellular Neuroscience.

[8]  M. Butchbach,et al.  Genomic Variability in the Survival Motor Neuron Genes (SMN1 and SMN2): Implications for Spinal Muscular Atrophy Phenotype and Therapeutics Development , 2021, International journal of molecular sciences.

[9]  Nicole F. Liachko,et al.  Regulation of TDP-43 phosphorylation in aging and disease , 2021, GeroScience.

[10]  A. Agar,et al.  Protective mechanism of Syringic acid in an experimental model of Parkinson’s disease , 2021, Metabolic Brain Disease.

[11]  G. Mentis,et al.  Gain of toxic function by long-term AAV9-mediated SMN overexpression in the sensory-motor circuit , 2021, Nature Neuroscience.

[12]  M. Taheri,et al.  Comprehensive Mutation Analysis and Report of 12 Novel Mutations in a Cohort of Patients with Spinal Muscular Atrophy in Iran , 2021, Journal of Molecular Neuroscience.

[13]  Q. Ding,et al.  SARS-CoV-2 nucleocapsid protein phase separates with G3BPs to disassemble stress granules and facilitate viral production , 2021, Science Bulletin.

[14]  B. Portz,et al.  FUS and TDP-43 Phases in Health and Disease. , 2021, Trends in biochemical sciences.

[15]  J. Veldink,et al.  Genetic analysis of ALS cases in the isolated island population of Malta , 2021, European journal of human genetics : EJHG.

[16]  T. Ha,et al.  ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. , 2020, Molecular cell.

[17]  A. Aguilera,et al.  TDP-43 mutations link Amyotrophic Lateral Sclerosis with R-loop homeostasis and R loop-mediated DNA damage , 2020, PLoS genetics.

[18]  D. Rasà,et al.  Drug Screening and Drug Repositioning as Promising Therapeutic Approaches for Spinal Muscular Atrophy Treatment , 2020, Frontiers in Pharmacology.

[19]  Hanna S. Yuan,et al.  Frontotemporal dementia‐linked P112H mutation of TDP‐43 induces protein structural change and impairs its RNA binding function , 2020, Protein science : a publication of the Protein Society.

[20]  S. Mousa,et al.  Current and emerging therapies for Duchenne muscular dystrophy and spinal muscular atrophy. , 2020, Pharmacology & therapeutics.

[21]  J. Sung,et al.  ALS-Linked Mutant SOD1 Associates with TIA-1 and Alters Stress Granule Dynamics , 2020, Neurochemical Research.

[22]  E. Bertini,et al.  Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases , 2020, International journal of molecular sciences.

[23]  P. Ivanov,et al.  Molecular mechanisms of stress granule assembly and disassembly. , 2020, Biochimica et biophysica acta. Molecular cell research.

[24]  J. Mendell,et al.  Gene Therapy for Spinal Muscular Atrophy: Safety and Early Outcomes , 2020, Pediatrics.

[25]  Ana Martínez,et al.  Therapeutic potential of novel Cell Division Cycle Kinase 7 inhibitors on TDP‐43‐related pathogenesis such as Frontotemporal Lobar Degeneration (FTLD) and amyotrophic lateral sclerosis (ALS) , 2020, Journal of neurochemistry.

[26]  P. Ivanov,et al.  Stress granule subtypes: an emerging link to neurodegeneration , 2020, Cellular and Molecular Life Sciences.

[27]  C. Besnard‐Guérin Cytoplasmic localization of amyotrophic lateral sclerosis‐related TDP‐43 proteins modulates stress granule formation , 2020, The European journal of neuroscience.

[28]  X. Kong,et al.  Mutation analysis of 419 family and prenatal diagnosis of 339 cases of spinal muscular atrophy in China , 2020, BMC Medical Genetics.

[29]  Cheri K Walker,et al.  Onasemnogene Abeparvovec-xioi: Gene Therapy for Spinal Muscular Atrophy , 2020, The Annals of pharmacotherapy.

[30]  K. Fischbeck,et al.  Combinatorial treatment for spinal muscular atrophy , 2020, Journal of neurochemistry.

[31]  P. Claus,et al.  The Need for SMN-Independent Treatments of Spinal Muscular Atrophy (SMA) to Complement SMN-Enhancing Drugs , 2020, Frontiers in Neurology.

[32]  C. van Broeckhoven,et al.  Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrum , 2020, Neurobiology of Disease.

[33]  L. Servais,et al.  New treatments in spinal muscular atrophy: an overview of currently available data , 2020, Expert opinion on pharmacotherapy.

[34]  S. Myong,et al.  Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations. , 2020, Molecular cell.

[35]  Li Jiang,et al.  Stress granule: A promising target for cancer treatment , 2019, British journal of pharmacology.

[36]  J. Wilce,et al.  TDP-43 and FUS-structural insights into RNA recognition and self-association. , 2019, Current opinion in structural biology.

[37]  P. Ivanov,et al.  Stress granules and neurodegeneration , 2019, Nature Reviews Neuroscience.

[38]  N. Hoot Nusinersen for Type 1 Spinal Muscular Atrophy: A Father’s Perspective , 2019, Pediatrics.

[39]  Gene W. Yeo,et al.  Small-Molecule Modulation of TDP-43 Recruitment to Stress Granules Prevents Persistent TDP-43 Accumulation in ALS/FTD , 2019, Neuron.

[40]  T. Boeckers,et al.  FUS-mediated regulation of acetylcholine receptor transcription at neuromuscular junctions is compromised in amyotrophic lateral sclerosis , 2019, Nature Neuroscience.

[41]  Chun-quan Cai,et al.  High-throughput screening reveals novel mutations in spinal muscular atrophy patients , 2019, Italian Journal of Pediatrics.

[42]  M. Bowerman,et al.  Teaching an old drug new tricks: repositioning strategies for spinal muscular atrophy , 2019, Future Neurology.

[43]  I. Bozzoni,et al.  Mutant FUS and ELAVL4 (HuD) Aberrant Crosstalk in Amyotrophic Lateral Sclerosis , 2019, Cell reports.

[44]  Carrie Arnold Tailored treatment for ALS poised to move ahead. , 2019, Nature medicine.

[45]  Nicolas L. Fawzi,et al.  TDP-43 α-helical structure tunes liquid–liquid phase separation and function , 2019, Proceedings of the National Academy of Sciences.

[46]  M. Hegde,et al.  Amyotrophic lateral sclerosis-associated TDP-43 mutation Q331K prevents nuclear translocation of XRCC4-DNA ligase 4 complex and is linked to genome damage-mediated neuronal apoptosis. , 2019, Human molecular genetics.

[47]  T. Prior,et al.  Complete sequencing of the SMN2 gene in SMA patients detects SMN gene deletion junctions and variants in SMN2 that modify the SMA phenotype , 2019, Human Genetics.

[48]  N. Shneider,et al.  Mutant TDP-43 Causes Early-Stage Dose-Dependent Motor Neuron Degeneration in a TARDBP Knockin Mouse Model of ALS. , 2019, Cell reports.

[49]  P. Oliver,et al.  Single-copy expression of an amyotrophic lateral sclerosis-linked TDP-43 mutation (M337V) in BAC transgenic mice leads to altered stress granule dynamics and progressive motor dysfunction , 2019, Neurobiology of Disease.

[50]  M. Lapeyre-Mestre,et al.  Microtubule-Driven Stress Granule Dynamics Regulate Inhibitory Immune Checkpoint Expression in T Cells. , 2019, Cell reports.

[51]  P. Cyr,et al.  Cost-effectiveness analysis of using onasemnogene abeparvocec (AVXS-101) in spinal muscular atrophy type 1 patients , 2019, Journal of market access & health policy.

[52]  F. Rigo,et al.  Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration , 2018, Nature Neuroscience.

[53]  D. Pastré,et al.  Relation Between Stress Granules and Cytoplasmic Protein Aggregates Linked to Neurodegenerative Diseases , 2018, Current Neurology and Neuroscience Reports.

[54]  Nathan P. Staff,et al.  Amyotrophic Lateral Sclerosis: An Update for 2018 , 2018, Mayo Clinic proceedings.

[55]  C. Soares-Cunha,et al.  Dysregulation of autophagy and stress granule-related proteins in stress-driven Tau pathology , 2018, Cell Death & Differentiation.

[56]  L. Servais,et al.  Nusinersen treatment of spinal muscular atrophy: current knowledge and existing gaps , 2018, Developmental medicine and child neurology.

[57]  R. Kalb,et al.  Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization. , 2018, Molecular cell.

[58]  M. Jaiswal,et al.  Riluzole and edaravone: A tale of two amyotrophic lateral sclerosis drugs , 2018, Medicinal research reviews.

[59]  P. Ivanov,et al.  Stress Granules and Processing Bodies in Translational Control. , 2018, Cold Spring Harbor perspectives in biology.

[60]  Seung-Jae Lee,et al.  Mechanism of neuroprotection by trehalose: controversy surrounding autophagy induction , 2018, Cell Death & Disease.

[61]  P. Tomançak,et al.  RNA buffers the phase separation behavior of prion-like RNA binding proteins , 2018, Science.

[62]  Ahmad Al Khleifat,et al.  Stage at which riluzole treatment prolongs survival in patients with amyotrophic lateral sclerosis: a retrospective analysis of data from a dose-ranging study , 2018, The Lancet Neurology.

[63]  Julie C. Sung,et al.  Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains , 2018, Cell.

[64]  M. Repici,et al.  The Parkinson’s Disease-Linked Protein DJ-1 Associates with Cytoplasmic mRNP Granules During Stress and Neurodegeneration , 2018, Molecular Neurobiology.

[65]  John K. Kim,et al.  FUS Regulates Activity of MicroRNA-Mediated Gene Silencing. , 2018, Molecular cell.

[66]  Ewout J. N. Groen,et al.  Advances in therapy for spinal muscular atrophy: promises and challenges , 2018, Nature Reviews Neurology.

[67]  Ewout J. N. Groen,et al.  Overview of Current Drugs and Molecules in Development for Spinal Muscular Atrophy Therapy , 2018, Drugs.

[68]  Gene W. Yeo,et al.  Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules , 2018, Cell.

[69]  L. Piedrafita,et al.  Cellular bases of the RNA metabolism dysfunction in motor neurons of a murine model of spinal muscular atrophy: Role of Cajal bodies and the nucleolus , 2017, Neurobiology of Disease.

[70]  R. Tycko,et al.  Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains , 2017, Cell.

[71]  Hu Li,et al.  Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo , 2017, Nature Neuroscience.

[72]  A. Camargo,et al.  Morus nigra and its major phenolic, syringic acid, have antidepressant-like and neuroprotective effects in mice , 2017, Metabolic Brain Disease.

[73]  Nicolas L. Fawzi,et al.  Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity , 2017, The EMBO journal.

[74]  E. Whitley,et al.  TIA1 is a gender-specific disease modifier of a mild mouse model of spinal muscular atrophy , 2017, Scientific Reports.

[75]  S. Henry,et al.  Population Pharmacokinetics of Nusinersen in the Cerebral Spinal Fluid and Plasma of Pediatric Patients With Spinal Muscular Atrophy Following Intrathecal Administrations , 2017, Journal of clinical pharmacology.

[76]  Xiang-jun Chen,et al.  Screening novel stress granule regulators from a natural compound library , 2017, Protein & Cell.

[77]  Hanns Lochmüller,et al.  Prevalence, incidence and carrier frequency of 5q–linked spinal muscular atrophy – a literature review , 2017, Orphanet Journal of Rare Diseases.

[78]  Y. Itoyama,et al.  Safety and efficacy of edaravone in well defined patients with amyotrophic lateral sclerosis: a randomised, double-blind, placebo-controlled trial , 2017, The Lancet Neurology.

[79]  Ashley R. Jones,et al.  A comprehensive analysis of rare genetic variation in amyotrophic lateral sclerosis in the UK , 2017, Brain : a journal of neurology.

[80]  U. Stochaj,et al.  Cytoplasmic stress granules: Dynamic modulators of cell signaling and disease. , 2017, Biochimica et biophysica acta. Molecular basis of disease.

[81]  David A. Knowles,et al.  Therapeutic reduction of ataxin 2 extends lifespan and reduces pathology in TDP-43 mice , 2017, Nature.

[82]  V. Buchman,et al.  Modulation of p-eIF2α cellular levels and stress granule assembly/disassembly by trehalose , 2017, Scientific Reports.

[83]  E. Ottesen,et al.  Diverse role of survival motor neuron protein. , 2017, Biochimica et biophysica acta. Gene regulatory mechanisms.

[84]  E. Huang,et al.  Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis , 2016, Brain Research.

[85]  R. Parker,et al.  Distinct stages in stress granule assembly and disassembly , 2016, eLife.

[86]  R. Parker,et al.  Principles and Properties of Stress Granules. , 2016, Trends in cell biology.

[87]  L. Hayward,et al.  ALS mutant SOD1 interacts with G3BP1 and affects stress granule dynamics , 2016, Acta Neuropathologica.

[88]  M. Paronetto,et al.  Role of FET proteins in neurodegenerative disorders , 2016, RNA biology.

[89]  E. Buratti,et al.  Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins , 2016, Journal of neurochemistry.

[90]  M. Sousa,et al.  The cytoskeleton as a novel therapeutic target for old neurodegenerative disorders , 2016, Progress in Neurobiology.

[91]  J. Lieberman,et al.  G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits , 2016, The Journal of cell biology.

[92]  N. Atsuta,et al.  Next-generation sequencing of 28 ALS-related genes in a Japanese ALS cohort , 2016, Neurobiology of Aging.

[93]  Anthony Barsic,et al.  ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure , 2016, Cell.

[94]  Yimei Lu,et al.  ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43 , 2016, PLoS biology.

[95]  Claire H. Michel,et al.  ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function , 2015, Neuron.

[96]  K. Boylan Familial Amyotrophic Lateral Sclerosis. , 2015, Neurologic clinics.

[97]  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..

[98]  Lin Guo,et al.  It's Raining Liquids: RNA Tunes Viscoelasticity and Dynamics of Membraneless Organelles. , 2015, Molecular cell.

[99]  K. Nakayama,et al.  Isolated inclusion body myopathy caused by a multisystem proteinopathy–linked hnRNPA1 mutation , 2015, Neurology: Genetics.

[100]  E. Dadali,et al.  SMN1 gene point mutations in type I–IV proximal spinal muscular atrophy patients with a single copy of SMN1 , 2015, Russian Journal of Genetics.

[101]  Marco Y. Hein,et al.  A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation , 2015, Cell.

[102]  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.

[103]  I. Bozzoni,et al.  ALS mutant FUS proteins are recruited into stress granules in induced pluripotent stem cell-derived motoneurons , 2015, Disease Models & Mechanisms.

[104]  R. Finkel,et al.  209th ENMC International Workshop: Outcome Measures and Clinical Trial Readiness in Spinal Muscular Atrophy 7–9 November 2014, Heemskerk, The Netherlands , 2015, Neuromuscular Disorders.

[105]  I. Poser,et al.  Author response: Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules , 2015 .

[106]  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.

[107]  C. Ki,et al.  De novo FUS mutations in 2 Korean patients with sporadic amyotrophic lateral sclerosis , 2015, Neurobiology of Aging.

[108]  Y. Tohyama,et al.  Intragenic mutations in SMN1 may contribute more significantly to clinical severity than SMN2 copy numbers in some spinal muscular atrophy (SMA) patients , 2014, Brain and Development.

[109]  D. Rubinsztein,et al.  Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly , 2014, Cell Death and Differentiation.

[110]  Gregor Bieri,et al.  Profilin 1 Associates with Stress Granules and ALS-Linked Mutations Alter Stress Granule Dynamics , 2014, The Journal of Neuroscience.

[111]  J. Jankovic,et al.  The role of FUS gene variants in neurodegenerative diseases , 2014, Nature Reviews Neurology.

[112]  L. Schöls,et al.  Targeted high-throughput sequencing identifies a TARDBP mutation as a cause of early-onset FTD without motor neuron disease , 2014, Neurobiology of Aging.

[113]  J. Ule,et al.  Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43 , 2013, Nature Structural &Molecular Biology.

[114]  D. A. Bosco,et al.  Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics , 2013, Molecular Neurodegeneration.

[115]  P. Lomonte,et al.  The Tudor protein survival motor neuron (SMN) is a chromatin-binding protein that interacts with methylated lysine 79 of histone H3 , 2013, Journal of Cell Science.

[116]  D. Cleveland,et al.  Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis , 2013, Neuron.

[117]  E. Klann,et al.  Suppression of eIF2α kinases alleviates AD-related synaptic plasticity and spatial memory deficits , 2013, Nature Neuroscience.

[118]  D. Mann,et al.  Prion-like properties of pathological TDP-43 aggregates from diseased brains. , 2013, Cell reports.

[119]  R. Parker,et al.  Eukaryotic Stress Granules Are Cleared by Autophagy and Cdc48/VCP Function , 2013, Cell.

[120]  C. Hetz,et al.  Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons , 2013, Autophagy.

[121]  Ewout J. N. Groen,et al.  Protein aggregation in amyotrophic lateral sclerosis , 2013, Acta Neuropathologica.

[122]  Oliver D. King,et al.  Stress granules as crucibles of ALS pathogenesis , 2013, The Journal of cell biology.

[123]  Liuqing Yang,et al.  HDAC6 Regulates Mutant SOD1 Aggregation through Two SMIR Motifs and Tubulin Acetylation* , 2013, The Journal of Biological Chemistry.

[124]  L. Pallanck,et al.  VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations , 2013, Neuron.

[125]  Rebecca B. Smith,et al.  RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations. , 2013, Human molecular genetics.

[126]  T. Hortobágyi,et al.  ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules , 2013, Human molecular genetics.

[127]  I. Blair,et al.  Ataxin-2 interacts with FUS and intermediate-length polyglutamine expansions enhance FUS-related pathology in amyotrophic lateral sclerosis. , 2013, Human molecular genetics.

[128]  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.

[129]  S. Gygi,et al.  FUS-SMN protein interactions link the motor neuron diseases ALS and SMA. , 2012, Cell reports.

[130]  A. Aulas,et al.  Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP , 2012, Molecular Neurodegeneration.

[131]  M. Strong,et al.  Co-aggregation of RNA binding proteins in ALS spinal motor neurons: evidence of a common pathogenic mechanism , 2012, Acta Neuropathologica.

[132]  K. Tsai,et al.  Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43 , 2012, Proceedings of the National Academy of Sciences.

[133]  I. Mackenzie,et al.  FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis , 2012, Brain Research.

[134]  K. Duff,et al.  Contrasting Pathology of the Stress Granule Proteins TIA-1 and G3BP in Tauopathies , 2012, The Journal of Neuroscience.

[135]  S. C. Chafe,et al.  Mutations in the Profilin 1 Gene Cause Familial Amyotrophic Lateral Sclerosis , 2012, Nature.

[136]  D. Dinsdale,et al.  Sustained translational repression by eIF2α-P mediates prion neurodegeneration , 2012, Nature.

[137]  C. Haass,et al.  Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)* , 2012, The Journal of Biological Chemistry.

[138]  E. Bertini,et al.  Childhood spinal muscular atrophy: controversies and challenges , 2012, The Lancet Neurology.

[139]  V. Meininger,et al.  Phenotype difference between ALS patients with expanded repeats in C9ORF72 and patients with mutations in other ALS-related genes , 2012, Journal of Medical Genetics.

[140]  Y. Qu,et al.  [Mutation analysis of SMN1 gene in patients with spinal muscular atrophy]. , 2011, Zhonghua er ke za zhi = Chinese journal of pediatrics.

[141]  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.

[142]  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.

[143]  R. Singer,et al.  The Survival of Motor Neuron (SMN) Protein Interacts with the mRNA-Binding Protein HuD and Regulates Localization of Poly(A) mRNA in Primary Motor Neuron Axons , 2011, The Journal of Neuroscience.

[144]  Yong-jian Liu,et al.  FUS Transgenic Rats Develop the Phenotypes of Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration , 2011, PLoS genetics.

[145]  W. Xie,et al.  Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander? , 2011, Molecular biology international.

[146]  V. Meininger,et al.  Identification of novel FUS mutations in sporadic cases of amyotrophic lateral sclerosis , 2011, Amyotrophic lateral sclerosis : official publication of the World Federation of Neurology Research Group on Motor Neuron Diseases.

[147]  J. Côté,et al.  HuD interacts with survival motor neuron protein and can rescue spinal muscular atrophy-like neuronal defects. , 2011, Human molecular genetics.

[148]  M. Sahin,et al.  SMN Deficiency Reduces Cellular Ability to Form Stress Granules, Sensitizing Cells to Stress , 2011, Cellular and Molecular Neurobiology.

[149]  Daniel R. Dries,et al.  TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor , 2010, Molecular and Cellular Biology.

[150]  D. A. Bosco,et al.  Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. , 2010, Human molecular genetics.

[151]  L. Petrucelli,et al.  Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue , 2010, PloS one.

[152]  I. Mackenzie,et al.  ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import , 2010, The EMBO journal.

[153]  A. Chiò,et al.  Amyotrophic lateral sclerosis-frontotemporal lobar dementia in 3 families with p.Ala382Thr TARDBP mutations. , 2010, Archives of neurology.

[154]  D. Cleveland,et al.  TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. , 2010, Human molecular genetics.

[155]  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.

[156]  R. Jackson,et al.  The mechanism of eukaryotic translation initiation and principles of its regulation , 2010, Nature Reviews Molecular Cell Biology.

[157]  E. Buratti,et al.  TDP‐43 is recruited to stress granules in conditions of oxidative insult , 2009, Journal of neurochemistry.

[158]  G. Comi,et al.  Mutations of FUS gene in sporadic amyotrophic lateral sclerosis , 2009, Journal of Medical Genetics.

[159]  Loic Hamon,et al.  Role of Microtubules in Stress Granule Assembly , 2009, The Journal of Biological Chemistry.

[160]  L. Fenart,et al.  Involvement of LRP1 and RAGE in the transport of β-amyloid (Aβ) peptide across the blood-brain barrier: Use of an in vitro model , 2009, Alzheimer's & Dementia.

[161]  B. Castellotti,et al.  High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis , 2009, Human mutation.

[162]  M. Pericak-Vance,et al.  Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis , 2009, Science.

[163]  Xun Hu,et al.  Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6 , 2009, Science.

[164]  P. Leigh,et al.  Amyotrophic lateral sclerosis , 2009, Orphanet journal of rare diseases.

[165]  Claire L. Simpson,et al.  Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration , 2008, Human molecular genetics.

[166]  Sarah Tisdale,et al.  A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly , 2008, Nature Cell Biology.

[167]  A. Ståhlberg,et al.  The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response , 2008, BMC Cell Biology.

[168]  B. McConkey,et al.  TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis , 2008, Nature Genetics.

[169]  Murray Grossman,et al.  TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis , 2008, The Lancet Neurology.

[170]  Xun Hu,et al.  TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis , 2008, Science.

[171]  H. Moine,et al.  In Vitro and in Cellulo Evidences for Association of the Survival of Motor Neuron Complex with the Fragile X Mental Retardation Protein* , 2008, Journal of Biological Chemistry.

[172]  P. Matthias,et al.  The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. , 2007, Genes & development.

[173]  R. Kaufman,et al.  Inhibition of the ubiquitin-proteasome system induces stress granule formation. , 2007, Molecular biology of the cell.

[174]  E. Zapletalová,et al.  Analysis of point mutations in the SMN1 gene in SMA patients bearing a single SMN1 copy , 2007, Neuromuscular Disorders.

[175]  S. Segerstrom,et al.  Psychological health in patients with amyotrophic lateral sclerosis , 2007, Amyotrophic lateral sclerosis : official publication of the World Federation of Neurology Research Group on Motor Neuron Diseases.

[176]  Bruce L. Miller,et al.  Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis , 2006, Science.

[177]  R. Burry,et al.  HuD Distribution Changes in Response to Heat Shock but Not Neurotrophic Stimulation , 2006, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[178]  G. Hicks,et al.  TLS, EWS and TAF15: a model for transcriptional integration of gene expression. , 2006, Briefings in functional genomics & proteomics.

[179]  S. Lefebvre,et al.  Distinct domains of the spinal muscular atrophy protein SMN are required for targeting to Cajal bodies in mammalian cells , 2006, Journal of Cell Science.

[180]  D. Handy,et al.  The Short N-terminal Domains of STIM1 and STIM2 Control the Activation Kinetics of Orai1 Channels* , 2006, The Journal of Biological Chemistry.

[181]  J. Shulman,et al.  TOR-Mediated Cell-Cycle Activation Causes Neurodegeneration in a Drosophila Tauopathy Model , 2006, Current Biology.

[182]  E. Androphy,et al.  Splicing of a Critical Exon of Human Survival Motor Neuron Is Regulated by a Unique Silencer Element Located in the Last Intron , 2006, Molecular and Cellular Biology.

[183]  B. Gold,et al.  New insights on the evolution of the SMN1 and SMN2 region: simulation and meta-analysis for allele and haplotype frequency calculations , 2004, European Journal of Human Genetics.

[184]  Y. Hua,et al.  Survival motor neuron protein facilitates assembly of stress granules , 2004, FEBS letters.

[185]  M. Berciano,et al.  Targeting SMN to Cajal bodies and nuclear gems during neuritogenesis , 2004, Chromosoma.

[186]  R. Miller,et al.  Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND) , 2003, Amyotrophic lateral sclerosis and other motor neuron disorders : official publication of the World Federation of Neurology, Research Group on Motor Neuron Diseases.

[187]  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.

[188]  L. Rowland How amyotrophic lateral sclerosis got its name: the clinical-pathologic genius of Jean-Martin Charcot. , 2001, Archives of neurology.

[189]  G. Neri,et al.  Premature termination mutations in exon 3 of the SMN1 gene are associated with exon skipping and a relatively mild SMA phenotype , 2001, European Journal of Human Genetics.

[190]  C. Lorson,et al.  The exon 2b region of the spinal muscular atrophy protein, SMN, is involved in self-association and SIP1 binding. , 2000, Human molecular genetics.

[191]  G. Morris,et al.  The relationship between SMN, the spinal muscular atrophy protein, and nuclear coiled bodies in differentiated tissues and cultured cells. , 2000, Experimental cell research.

[192]  A. Shevchenko,et al.  Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. , 1999, The Journal of cell biology.

[193]  C. Lorson,et al.  A single nucleotide in the SMN gene regulates splicing and is responsible for spinal muscular atrophy. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[194]  D. Parsons,et al.  Intragenic telSMN mutations: frequency, distribution, evidence of a founder effect, and modification of the spinal muscular atrophy phenotype by cenSMN copy number. , 1998, American journal of human genetics.

[195]  Arnold Munnich,et al.  Correlation between severity and SMN protein level in spinal muscular atrophy , 1997, Nature Genetics.

[196]  B. Wirth,et al.  Missense mutations in exon 6 of the survival motor neuron gene in patients with spinal muscular atrophy (SMA). , 1997, Human molecular genetics.

[197]  M. Höglund,et al.  Expression patterns of the human sarcoma-associated genes FUS and EWS and the genomic structure of FUS. , 1996, Genomics.

[198]  A. Munnich,et al.  Structure and organization of the human survival motor neurone (SMN) gene. , 1996, Genomics.

[199]  D Harrich,et al.  Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs , 1995, Journal of virology.

[200]  J. Weissenbach,et al.  Identification and characterization of a spinal muscular atrophy-determining gene , 1995, Cell.

[201]  N. Mandahl,et al.  Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma , 1993, Nature.

[202]  R. Larson,et al.  Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma , 1993, Nature Genetics.

[203]  S. Mellgren,et al.  Familial amyotrophic lateral sclerosis , 1980 .

[204]  J. Buchan,et al.  Stress Granules and ALS: A Case of Causation or Correlation? , 2018, Advances in neurobiology.

[205]  E. Buratti Functional Significance of TDP-43 Mutations in Disease. , 2015, Advances in genetics.

[206]  B. Wolozin Physiological protein aggregation run amuck: stress granules and the genesis of neurodegenerative disease. , 2014, Discovery medicine.

[207]  Emily A. Scarborough,et al.  Prion-like domain mutations in hnRNPs cause multisystem proteinopathy and ALS , 2013 .

[208]  R. Morimoto,et al.  The heat shock response: systems biology of proteotoxic stress in aging and disease. , 2011, Cold Spring Harbor symposia on quantitative biology.

[209]  J. Mandel,et al.  Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly. , 2009, Molecular biology of the cell.

[210]  P. Anderson,et al.  Mammalian stress granules and processing bodies. , 2007, Methods in enzymology.

[211]  D. Doudet Neurodegenerative Disease , 2007, Molecular Imaging and Biology.

[212]  Hurng‐Yi Wang,et al.  Structural diversity and functional implications of the eukaryotic TDP gene family. , 2004, Genomics.

[213]  E. Buratti,et al.  Characterization and Functional Implications of the RNA Binding Properties of Nuclear Factor TDP-43, a Novel Splicing Regulator of CFTR Exon 9* , 2001 .