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1. Full Text Cellular Toxicity of Polyglutamine Expansion Proteins: Mechanism of Transcription Factor Deactivation
by Schaffar, Gregor and Breuer, Peter and Boteva, Raina and Behrends, Christian and Tzvetkov, Nikolay and Strippel, Nadine and Sakahira, Hideki and Siegers, Katja and Hayer-Hartl, Manajit and Hartl, F.Ulrich
Molecular cell, ISSN 1097-2765, 07/2004, Volume 15, Issue 1, pp. 95 - 105
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Molecular Chaperones - metabolism | Exons | Neurodegenerative Diseases - etiology | Peptides - genetics | TATA-Box Binding Protein - metabolism | Nerve Tissue Proteins - toxicity | Cell Nucleus - metabolism | Peptides - metabolism | TATA-Box Binding Protein - genetics | Trans-Activators - genetics | Nuclear Proteins - genetics | CREB-Binding Protein | Molecular Chaperones - genetics | HSP70 Heat-Shock Proteins - genetics | Neurodegenerative Diseases - genetics | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Neurodegenerative Diseases - metabolism | Transcription Factors - genetics | Mutation - genetics | Nerve Tissue Proteins - genetics | Nuclear Proteins - toxicity | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Macromolecular Substances | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Animals | Nuclear Proteins - antagonists & inhibitors | Cell Line, Tumor | Trinucleotide Repeat Expansion - genetics | Protein Conformation | Trans-Activators - metabolism | Mice | TATA-Box Binding Protein - antagonists & inhibitors | Trans-Activators - antagonists & inhibitors | Saccharomyces cerevisiae | Oligomers | Nervous system diseases | DNA binding proteins | Index Medicus
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2. Full Text Therapeutic modulation of eIF2α phosphorylation rescues TDP-43 toxicity in amyotrophic lateral sclerosis disease models
by Kim, Hyung-Jun and Raphael, Alya R and Ladow, Eva S and Mcgurk, Leeanne and Weber, Ross A and Trojanowski, John Q and Lee, Virginia M.-Y and Finkbeiner, Steven and Gitler, Aaron D and Bonini, Nancy M
Nature genetics, ISSN 1061-4036, 2014, Volume 46, Issue 2, pp. 152 - 160
Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Immunohistochemistry | Retina - metabolism | Spinal Cord - metabolism | Humans | Immunoblotting | DNA-Binding Proteins - metabolism | Ataxins | RNA Interference | Retina - ultrastructure | Poly(A)-Binding Proteins - metabolism | Eukaryotic Initiation Factor-2 - metabolism | Indoles - pharmacology | Phosphorylation - drug effects | Spinal Cord - cytology | Gene Ontology | Luminescent Proteins | Adenine - analogs & derivatives | Amyotrophic Lateral Sclerosis - genetics | Adenine - pharmacology | DNA-Binding Proteins - genetics | Motor Neurons - metabolism | Nerve Tissue Proteins - metabolism | Animals | High-Throughput Screening Assays | Analysis of Variance | Small Molecule Libraries | Saccharomyces cerevisiae Proteins - metabolism | Drosophila melanogaster | Saccharomyces cerevisiae | Index Medicus
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3. Full Text TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
by Brian S. Johnson and David Snead and Jonathan J. Lee and J. Michael McCaffery and James Shorter and Aaron D. Gitler
The Journal of biological chemistry, ISSN 0021-9258, 07/2009, Volume 284, Issue 30, pp. 20329 - 20339
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Protein Structure, Tertiary | Neurons - pathology | Mutagenesis, Site-Directed | Saccharomyces cerevisiae - genetics | Humans | Mutant Proteins - genetics | Mutant Proteins - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Protein Folding | DNA-Binding Proteins - metabolism | Amyotrophic Lateral Sclerosis - pathology | Mutant Proteins - chemistry | Index Medicus | Molecular Basis of Cell and Developmental Biology
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4. Full Text C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration
by May, Stephanie and Hornburg, Daniel and Schludi, Martin H and Arzberger, Thomas and Rentzsch, Kristin and Schwenk, Benjamin M and Grässer, Friedrich A and Mori, Kohji and Kremmer, Elisabeth and Banzhaf-Strathmann, Julia and Mann, Matthias and Meissner, Felix and Edbauer, Dieter
Acta neuropathologica, ISSN 0001-6322, 10/2014, Volume 128, Issue 4, pp. 485 - 503
Pathology | Neurosciences | Medicine & Public Health | Neurodegeneration | FTLD | Proteomics | ALS | Unc119 | C9orf72 | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Frontotemporal Lobar Degeneration - pathology | RNA-Binding Proteins - genetics | DNA Repeat Expansion - physiology | DNA Repeat Expansion - genetics | Microtubule-Associated Proteins - metabolism | Humans | Ubiquitin - metabolism | Green Fluorescent Proteins - genetics | Cerebral Cortex - cytology | DNA-Binding Proteins - metabolism | Caspases - metabolism | Transfection | Frontotemporal Lobar Degeneration - metabolism | HEK293 Cells | Dipeptides - metabolism | Green Fluorescent Proteins - metabolism | Gene Expression Regulation - genetics | Amyotrophic Lateral Sclerosis - genetics | Dipeptides - pharmacology | RNA-Binding Proteins - chemistry | Cells, Cultured | Rats | Gene Expression Regulation - drug effects | Amyotrophic Lateral Sclerosis - pathology | Animals | Amyotrophic Lateral Sclerosis - metabolism | Frontotemporal Lobar Degeneration - genetics | Adaptor Proteins, Signal Transducing - metabolism | Dipeptides - genetics | RNA-Binding Proteins - metabolism | Ubiquitin | Amyotrophic lateral sclerosis | Glycine | Neurons | Analysis | Index Medicus | Original Paper
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5. Full Text Repression of the low affinity iron transporter gene FET4: A novel mechanism against cadmium toxicity orchestrated by Yap1 via Rox1
by Caetano, Soraia M and Menezes, Regina and Amaral, Catarina and Rodrigues-Pousada, Claudina and Pimentel, Catarina
The Journal of biological chemistry, ISSN 0021-9258, 07/2015, Volume 290, Issue 30, pp. 18584 - 18595
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Cation Transport Proteins - biosynthesis | Saccharomyces cerevisiae Proteins - biosynthesis | Cadmium - metabolism | Iron-Binding Proteins - metabolism | DNA-Binding Proteins - metabolism | Cation Transport Proteins - metabolism | Cation Transport Proteins - genetics | Biological Transport - genetics | Repressor Proteins - metabolism | Gene Expression Regulation, Fungal | Cadmium - toxicity | Stress, Physiological - genetics | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Iron - metabolism | Iron-Binding Proteins - biosynthesis | Transcription Factors - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Iron-Binding Proteins - genetics | Copper Transport Proteins | Mutation | Saccharomyces cerevisiae | Exoribonucleases - metabolism | Index Medicus | Rox1 | Yap1 | stress response | yeast metabolism | gene regulation | metal | iron | cadmium | Metabolism | Fet4
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6. Full Text Identification of a Primary Target of Thalidomide Teratogenicity
by Takumi Ito and Hideki Ando and Yoshimasa Imamura and Yuki Yamaguchi and Hiroshi Handa and Takayuki Suzuki and Toshihiko Ogura and Kentaro Hotta
Science (American Association for the Advancement of Science), ISSN 0036-8075, 3/2010, Volume 327, Issue 5971, pp. 1345 - 1350
Receptors | Messenger RNA | Delta cells | Ubiquitins | Substrate specificity | Teratogenicity | HeLa cells | Pectorals | Cellular immunity | Embryos | Research Article | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Embryology: invertebrates and vertebrates. Teratology | Pharmacology. Drug treatments | Biological and medical sciences | Medical sciences | Drug toxicity and drugs side effects treatment | Miscellaneous (drug allergy, mutagens, teratogens...) | Teratology. Teratogens | Teratogens - toxicity | Thalidomide - metabolism | Peptide Hydrolases - genetics | Forelimb - embryology | Humans | Fibroblast Growth Factors - genetics | Ubiquitin-Protein Ligases - antagonists & inhibitors | Zebrafish - embryology | Embryo, Nonmammalian - drug effects | DNA-Binding Proteins - metabolism | Fibroblast Growth Factors - metabolism | Ubiquitination | Forelimb - abnormalities | Gene Expression Regulation, Developmental | Cullin Proteins - metabolism | Peptide Hydrolases - metabolism | Zebrafish Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Mutant Proteins - metabolism | Chick Embryo | Thalidomide - toxicity | Zebrafish - genetics | Animals | Carrier Proteins - metabolism | HeLa Cells | Zebrafish Proteins - genetics | Embryonic Development - drug effects | Teratogens - metabolism | Dosage and administration | Research | Teratogenic agents | Thalidomide | Protein binding | Pharmacology | Birth defects | Developmental biology | DNA damage | Binding sites | Index Medicus
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7. Full Text Differential toxicity of TAR DNA‐binding protein 43 isoforms depends on their submitochondrial localization in neuronal cells
by Salvatori, Illari and Ferri, Alberto and Scaricamazza, Silvia and Giovannelli, Ilaria and Serrano, Alessia and Rossi, Simona and D'Ambrosi, Nadia and Cozzolino, Mauro and Giulio, Andrea Di and Moreno, Sandra and Valle, Cristiana and Carrì, Maria Teresa
Journal of neurochemistry, ISSN 0022-3042, 09/2018, Volume 146, Issue 5, pp. 585 - 597
localization | neurodegeneration | Complex I | amyotrophic lateral sclerosis | TDP‐43 | mitochondria | TDP-43 | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Immunoprecipitation | Humans | Cytosol - drug effects | RNA, Messenger - metabolism | Electron Transport Complex IV - metabolism | DNA-Binding Proteins - metabolism | Cell Nucleus - metabolism | Neurons - ultrastructure | Protein Isoforms - metabolism | Transfection | RNA, Mitochondrial - metabolism | Chaperonin 60 - metabolism | Neurons - metabolism | Protein Isoforms - ultrastructure | Neurons - drug effects | Chaperonin 60 - genetics | Subcellular Fractions - drug effects | RNA, Messenger - genetics | Cytosol - ultrastructure | RNA, Mitochondrial - genetics | Mitochondria - metabolism | Electron Transport Complex IV - genetics | Mitochondria - drug effects | Cell Nucleus - ultrastructure | DNA-Binding Proteins - genetics | Microscopy, Electron | Mutation - genetics | DNA-Binding Proteins - chemistry | Subcellular Fractions - metabolism | DNA-Binding Proteins - ultrastructure | Mutation - drug effects | Oxygen Consumption - drug effects | Oligonucleotides - toxicity | Cytosol - metabolism | Cell Nucleus - drug effects | Cell Line, Transformed | Protein Isoforms - genetics | Oligomers | Nervous system diseases | Neurons | Analysis | DNA | Binding proteins | Protein binding | Oxidative stress | Neurodegenerative diseases | Toxicity | Amyotrophic lateral sclerosis | Metabolism | Ribonucleic acid--RNA | Neurological diseases | Proteins | Electron transport chain | Mitochondria | Aggregates | Coding | Neurodegeneration | Morphology | Isoforms | Localization | Cytoplasm | Deoxyribonucleic acid--DNA | Index Medicus
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8. Full Text The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity
by Wang, Wenzhang and Wang, Luwen and Lu, Junjie and Siedlak, Sandra L and Fujioka, Hisashi and Liang, Jingjing and Jiang, Sirui and Ma, Xiaopin and Jiang, Zhen and Da Rocha, Edroaldo Lummertz and Sheng, Max and Choi, Heewon and Lerou, Paul H and Li, Hu and Wang, Xinglong
Nature medicine, ISSN 1078-8956, 08/2016, Volume 22, Issue 8, pp. 869 - 878
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Cell Biology | Research & Experimental Medicine | Humans | Middle Aged | Male | NADH Dehydrogenase - genetics | Electron Transport Complex I - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Electron Transport Complex I - genetics | Aged, 80 and over | Adult | Female | Neurons - metabolism | Frontotemporal Dementia - genetics | Amyotrophic Lateral Sclerosis - genetics | Mice, Transgenic | Mitochondria - metabolism | DNA-Binding Proteins - genetics | NADH Dehydrogenase - metabolism | Phenotype | Animals | Amyotrophic Lateral Sclerosis - metabolism | Aged | Mice | Mutation | RNA, Messenger | Molecular targeted therapy | Care and treatment | Gene mutations | Innovations | Nervous system | Development and progression | Degeneration | Genetic aspects | Binding proteins | Properties | Gene expression | Health aspects | Proteins | Genetics | Mitochondria | Cytoplasm | Index Medicus
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9. Full Text Endocytosis regulates TDP-43 toxicity and turnover
by Liu, Guangbo and Coyne, Alyssa N and Pei, Fen and Vaughan, Spencer and Chaung, Matthew and Zarnescu, Daniela C and Buchan, J. Ross
Nature communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 2092 - 14
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Drosophila | Humans | Endocytosis - physiology | DNA-Binding Proteins - metabolism | Motor Neurons - metabolism | Amyotrophic Lateral Sclerosis - pathology | Animals | Cell Nucleus - metabolism | Protein Aggregation, Pathological - pathology | HEK293 Cells | Frontal Lobe - cytology | Locomotion - physiology | Frontal Lobe - pathology | RNA-Binding Proteins - metabolism | Disease Models, Animal | Proteins | Pathology | Motor neurons | RNA-binding protein | Endocytosis | Toxicity | Amyotrophic lateral sclerosis | Aberration | Localization | Ribonucleic acid--RNA | Index Medicus
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