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1. Full Text Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
by Lukavsky, Peter J and Daujotyte, Dalia and Tollervey, James R and Ule, Jernej and Stuani, Cristiana and Buratti, Emanuele and Baralle, Francisco E and Damberger, Fred F and Allain, Frédéric H.-T
Nature Structural and Molecular Biology, ISSN 1545-9993, 12/2013, Volume 20, Issue 12, pp. 1443 - 1449
TDP-43 encodes an alternative-splicing regulator with tandem RNA-recognition motifs (RRMs). The protein regulates cystic fibrosis transmembrane regulator... 
PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | CELL BIOLOGY | BIOPHYSICS | STRUCTURAL BASIS | NUCLEAR FACTOR TDP-43 | IN-VIVO | CFTR EXON-9 | BINDING | EXPRESSION | Protein Structure, Tertiary | Amino Acid Sequence | DNA-Binding Proteins - physiology | RNA-Binding Proteins - physiology | Humans | RNA-Binding Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | DNA-Binding Proteins - chemistry | DNA-Binding Proteins - metabolism | RNA Splicing - physiology | Base Composition | Nuclear Magnetic Resonance, Biomolecular | Cystic Fibrosis Transmembrane Conductance Regulator - genetics | Binding Sites | RNA-Binding Proteins - metabolism | Research | Binding proteins | Genetic regulation | Identification and classification | RNA splicing | Proteins | Cystic fibrosis | Molecular structure | Ribonucleic acid--RNA | Neurodegeneration
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2. Full Text Transcription and Splicing Factor TDP-43: Role in Regulation of Gene Expression in Testis
by Reddi, Prabhakara P
Seminars in Reproductive Medicine, ISSN 1526-8004, 03/2017, Volume 35, Issue 2, pp. 167 - 172
Abstract TDP-43 ( T AR D NA binding P rotein of 43 kD) is a transcription factor and RNA-binding protein with diverse functions. We cloned TDP-43 from the... 
Review Article | spermatogenesis | transcription | infertility | TDP-43 | RNA-POLYMERASE-II | SP-10 GENE | NUCLEAR | PROTEIN | INSULATOR | CTCF | SPERMATID-SPECIFIC TRANSCRIPTION | GENOME | OBSTETRICS & GYNECOLOGY | REPRODUCTIVE BIOLOGY | PROMOTER | BINDING | Testis - metabolism | Signal Transduction | Spermatogenesis | Humans | Male | DNA-Binding Proteins - genetics | DNA-Binding Proteins - metabolism | Infertility, Male - physiopathology | Animals | Infertility, Male - genetics | Fertility | Gene Expression Regulation, Developmental | Infertility, Male - metabolism
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3. Full Text Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
by Zuccato, Elisabetta and Baralle, Francisco E and Dörk, Thilo and Pagani, Franco and Buratti, Emanuele and Romano, Maurizio
The EMBO Journal, ISSN 0261-4189, 04/2001, Volume 20, Issue 7, pp. 1774 - 1784
Alternative splicing of human cystic fibrosis transmembrane conductance regulator (CFTR) exon 9 is regulated by a combination of cis‐acting elements... 
alternative splicing | ASF | TDP‐43 | cystic fibrosis | CFTR exon 9 | SF2 | Alternative splicing | Cystic fibrosis | TDP-43 | SPLICING FACTORS | DISSEMINATED BRONCHIECTASIS | VAS-DEFERENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | POLYPYRIMIDINE TRACT | TRACT-BINDING-PROTEIN | CONGENITAL ABSENCE | PRE-MESSENGER-RNA | CELL BIOLOGY | PARTIAL PENETRANCE | FUNCTIONAL-ANALYSIS | CYSTIC-FIBROSIS GENE | Alternative Splicing | Exons | Humans | Molecular Sequence Data | RNA-Binding Proteins | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Tissue Distribution | Glutathione Transferase - genetics | Transfection | Nuclear Proteins - genetics | RNA, Antisense | Amino Acid Sequence | Rabbits | Glutathione Transferase - metabolism | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Polymorphism, Genetic | Animals | Serine-Arginine Splicing Factors | Recombinant Fusion Proteins - genetics | Repetitive Sequences, Nucleic Acid | Cystic Fibrosis Transmembrane Conductance Regulator - genetics | HeLa Cells | RNA, Messenger | CFTR exon 9
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4. Full Text TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
by Mackenzie, Ian RA, Prof and Rademakers, Rosa, PhD and Neumann, Manuela, Dr
Lancet Neurology, The, ISSN 1474-4422, 2010, Volume 9, Issue 10, pp. 995 - 1007
Summary Abnormal intracellular protein aggregates comprise a key characteristic in most neurodegenerative diseases, including amyotrophic lateral sclerosis... 
Neurology | GENE-MUTATIONS | VALOSIN-CONTAINING-PROTEIN | LOBAR DEGENERATION | ALZHEIMERS-DISEASE | NUCLEAR FACTOR TDP-43 | IN-VIVO | TAR-DNA-BINDING | UBIQUITIN-POSITIVE INCLUSIONS | MOTOR-NEURON DISEASE | C-TERMINAL FRAGMENTS | CLINICAL NEUROLOGY | Frontotemporal Dementia - genetics | DNA-Binding Proteins - physiology | Amyotrophic Lateral Sclerosis - genetics | Humans | Amyotrophic Lateral Sclerosis - diagnosis | RNA-Binding Protein FUS - genetics | DNA-Binding Proteins - genetics | Frontotemporal Dementia - diagnosis | Mutation - genetics | DNA-Binding Proteins - chemistry | Frontotemporal Dementia - metabolism | RNA-Binding Protein FUS - chemistry | Animals | Genetic Markers - genetics | Amyotrophic Lateral Sclerosis - metabolism | RNA-Binding Protein FUS - physiology | Genetic Markers - physiology | Physiological aspects | Amyotrophic lateral sclerosis
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5. Full Text Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
by Moran, Jacqueline and Liang, Tiffany Y and Sedaghat, Yalda and Sun, Eveline and Polymenidou, Magdalini and Bennett, C Frank and Kordasiewicz, Holly and Ling, Shuo-Chien and Shiue, Lily and Cleveland, Don W and Wancewicz, Edward and Huelga, Stephanie C and Mazur, Curt and Yeo, Gene W and Lagier-Tourenne, Clotilde and Donohue, John Paul and Hutt, Kasey R
Nature Neuroscience, ISSN 1097-6256, 04/2011, Volume 14, Issue 4, pp. 459 - 468
We used cross-linking and immunoprecipitation coupled with high-throughput sequencing to identify binding sites in 6,304 genes as the brain RNA targets for... 
REGULATOR | GENE | NUCLEAR FACTOR TDP-43 | BINDING-PROTEIN | TARDBP MUTATIONS | TAU | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | EXPRESSION | ASSOCIATION | NEUROSCIENCES | Neurons - pathology | Amyotrophic Lateral Sclerosis - physiopathology | Humans | Nerve Degeneration - physiopathology | 3' Untranslated Regions - genetics | Nerve Degeneration - genetics | RNA Precursors - antagonists & inhibitors | DNA-Binding Proteins - deficiency | Nerve Degeneration - metabolism | RNA, Messenger - antagonists & inhibitors | Female | Neurons - metabolism | Alternative Splicing - genetics | Amyotrophic Lateral Sclerosis - genetics | Mice, Inbred C57BL | RNA, Messenger - genetics | Mice, Transgenic | RNA Precursors - genetics | DNA-Binding Proteins - genetics | Animals | Oligonucleotides, Antisense - genetics | Amyotrophic Lateral Sclerosis - metabolism | Mice | DNA-Binding Proteins - biosynthesis | Homeostasis - genetics | Messenger RNA | Gene mutations | Physiological aspects | Amyotrophic lateral sclerosis | Genetic aspects | Research | DNA binding proteins | Health aspects | Risk factors
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6. Full Text Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies
by Lionel M. Igaz and Linda K. Kwong and Alice Chen-Plotkin and Matthew J. Winton and Travis L. Unger and Yan Xu and Manuela Neumann and John Q. Trojanowski and Virginia M.-Y. Lee
Journal of Biological Chemistry, ISSN 0021-9258, 03/2009, Volume 284, Issue 13, pp. 8516 - 8524
The disease protein in frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U) and amyotrophic lateral sclerosis (ALS) was identified... 
REGULATOR | INCLUSIONS | GENE | DETERMINANTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR FACTOR TDP-43 | DISEASE | TARDBP MUTATIONS | CFTR EXON-9 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | Dementia - pathology | Amyotrophic Lateral Sclerosis - genetics | Humans | Cytoplasm - metabolism | Protein Structure, Tertiary - genetics | DNA-Binding Proteins - genetics | Dementia - genetics | Cytoplasm - pathology | DNA-Binding Proteins - metabolism | Amyotrophic Lateral Sclerosis - pathology | Dementia - metabolism | Phosphorylation - genetics | Animals | Cell Nucleus - metabolism | Cell Nucleus - genetics | Cell Nucleus - pathology | Amyotrophic Lateral Sclerosis - metabolism | Protein Structure, Quaternary - genetics | Cytoplasm - genetics | Mice | Ubiquitination - genetics
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7. Full Text Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
by Zupan, Bla and König, Julian and Patani, Rickie and Chandran, Siddharthan and Curk, Toma and Rot, Gregor and Kayikci, Melis and Rogelj, Boris and Briese, Michael and Hortobágyi, Tibor and upunski, Vera and Cereda, Matteo and Shaw, Christopher E and Ule, Jernej and Nishimura, Agnes L and Tollervey, James R
Nature Neuroscience, ISSN 1097-6256, 04/2011, Volume 14, Issue 4, pp. 452 - 458
TDP-43 is a predominantly nuclear RNA-binding protein that forms inclusion bodies in frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis... 
APOPTOSIS | EVOLUTION | ROLES | PHOSPHORYLATION | NUCLEAR FACTOR TDP-43 | AMYOTROPHIC-LATERAL-SCLEROSIS | BINDING PROTEIN | IDENTIFICATION | BCL-2 FAMILY | EXPRESSION | NEUROSCIENCES | Cell Line | RNA-Binding Proteins - genetics | DNA-Binding Proteins - physiology | Gene Expression Regulation - genetics | Alternative Splicing - genetics | Humans | RNA, Messenger - genetics | DNA-Binding Proteins - genetics | RNA, Messenger - metabolism | RNA, Untranslated - genetics | RNA Splicing - physiology | RNA, Messenger - biosynthesis | Cell Line, Tumor | RNA-Binding Proteins - metabolism | Brain Chemistry - genetics | Protein Isoforms - genetics | Physiological aspects | Brain | Genetic aspects | Research | DNA binding proteins | RNA
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8. Full Text Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
by Manuela Neumann and Deepak M. Sampathu and Linda K. Kwong and Adam C. Truax and Matthew C. Micsenyi and Thomas T. Chou and Jennifer Bruce and Theresa Schuck and Murray Grossman and Christopher M. Clark and Leo F. McCluskey and Bruce L. Miller and Eliezer Masliah and Ian R. Mackenzie and Howard Feldman and Wolfgang Feiden and Hans A. Kretzschmar and John Q. Trojanowski and Virginia M.-Y. Lee
Science, ISSN 0036-8075, 10/2006, Volume 314, Issue 5796, pp. 130 - 133
Ubiquitin-positive, tau- and α-synuclein--negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and... 
Proteins | Pathology | Nervous system diseases | Spinal cord | Neurodegenerative diseases | Neurons | Ubiquitins | Antibodies | Amyotrophic lateral sclerosis | Frontotemporal lobar degeneration | Reports | DEMENTIA | CHROMOSOME-17 | GENE | EXON-9 | 17Q21 | MULTIDISCIPLINARY SCIENCES | NUCLEAR FACTOR TDP-43 | TAU | MOTOR-NEURON DISEASE | MUTATIONS | FAMILY | Neurons - pathology | Ubiquitin - analysis | Phosphorylation | Hippocampus - chemistry | Humans | Cerebral Cortex - pathology | Molecular Sequence Data | DNA-Binding Proteins - analysis | Immunoblotting | Dementia - genetics | Motor Neurons - pathology | Dementia - metabolism | Spinal Cord - chemistry | Spinal Cord - pathology | Cerebral Cortex - chemistry | Amino Acid Sequence | DNA-Binding Proteins - immunology | Dementia - pathology | Neurons - chemistry | Hippocampus - pathology | Antibodies, Monoclonal | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Motor Neurons - chemistry | Amyotrophic Lateral Sclerosis - pathology | Peptide Fragments - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Fluorescent Antibody Technique | Brain Chemistry | Immunohistochemistry | Research | Ubiquitin-proteasome system | Analysis
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9. Full Text TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
by Cohen, Todd J and Lee, Virginia M.Y and Trojanowski, John Q
Trends in Molecular Medicine, ISSN 1471-4914, 2011, Volume 17, Issue 11, pp. 659 - 667
Given the critical role for TDP-43 in diverse neurodegenerative diseases including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration... 
Pathology | MEDICINE, RESEARCH & EXPERIMENTAL | RIBONUCLEOPROTEIN COMPLEXES | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | DNA-BINDING PROTEIN | FRONTOTEMPORAL LOBAR DEGENERATION | CELL BIOLOGY | MESSENGER-RNA | NUCLEAR FACTOR TDP-43 | C-TERMINAL FRAGMENTS | STRESS GRANULES | TRANSGENIC MICE | Humans | TDP-43 Proteinopathies - metabolism | Gene Expression Regulation | Stress, Physiological | Mutation, Missense | DNA-Binding Proteins - genetics | RNA, Messenger - metabolism | DNA-Binding Proteins - chemistry | Protein Interaction Mapping | DNA-Binding Proteins - metabolism | TDP-43 Proteinopathies - genetics | Animals | Protein Interaction Domains and Motifs | Inclusion Bodies - metabolism | TDP-43 Proteinopathies - physiopathology
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10. Full Text Structural determinants of the cellular localization and shuttling of TDP-43
by Ayala, Youhna M and Zago, Paola and D'Ambrogio, Andrea and Xu, Ya-Fei and Petrucelli, Leonard and Buratti, Emanuele and Baralle, Francisco E
Journal of Cell Science, ISSN 0021-9533, 11/2008, Volume 121, Issue 22, pp. 3778 - 3785
TDP-43 (also known as TARDBP) regulates different processes of gene expression, including transcription and splicing, through RNA and DNA binding. Moreover,... 
RNA recognition motifs | Nuclear-cytoplasmic shuttling | hnRNP | PROTEIN | EXPORT | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | CELL BIOLOGY | REGULATOR | NUCLEAR FACTOR TDP-43 | TARDBP MUTATIONS | CFTR EXON-9 | HNRNP A1 | BINDING-PROPERTIES | Cytoplasm - chemistry | Protein Structure, Tertiary | Cell Line | Sequence Deletion | Nuclear Localization Signals - genetics | Humans | Cytoplasm - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Amino Acid Motifs | Protein Transport | DNA-Binding Proteins - metabolism | Cell Nucleus - metabolism | Cell Nucleus - genetics | Cell Nucleus - chemistry | Cytoplasm - genetics | HeLa Cells
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11. Full Text Phase to Phase with TDP-43
by Sun, Yulong and Chakrabartty, Avijit
Biochemistry, ISSN 0006-2960, 02/2017, Volume 56, Issue 6, pp. 809 - 823
TDP-43 is a dimeric nuclear protein that plays a central role in RNA metabolism. In recent years, this protein has become a focal point of research in the... 
PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR FACTOR TDP-43 | TARDBP GENE-MUTATIONS | AMYOTROPHIC-LATERAL-SCLEROSIS | RNA RECOGNITION MOTIF | MOTOR-NEURON DISEASE | FRONTOTEMPORAL LOBAR DEGENERATION | DNA-BINDING PROTEIN | AMYLOIDOGENIC CORE REGION | STRESS GRANULES | Neurons - pathology | RNA-Binding Proteins - genetics | Humans | Phase Transition | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Nerve Tissue Proteins - chemistry | Protein Aggregation, Pathological - pathology | Neurons - metabolism | Protein Interaction Domains and Motifs | Protein Aggregation, Pathological - genetics | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Proteins - chemistry | Models, Molecular | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Nerve Tissue Proteins - genetics | Protein Folding | Nerve Tissue Proteins - metabolism | Amyotrophic Lateral Sclerosis - pathology | Animals | Amyotrophic Lateral Sclerosis - metabolism | Protein Conformation | Mutation | Protein Aggregation, Pathological - metabolism | RNA-Binding Proteins - metabolism | Proteins |