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als-linked sod1 (192) 192
animals (137) 137
humans (135) 135
amyotrophic lateral sclerosis (102) 102
index medicus (96) 96
superoxide dismutase - genetics (92) 92
mice (87) 87
amyotrophic lateral sclerosis - genetics (81) 81
neurosciences (81) 81
superoxide dismutase-1 (79) 79
amyotrophic-lateral-sclerosis (69) 69
superoxide dismutase - metabolism (69) 69
biochemistry & molecular biology (66) 66
mutation (63) 63
disease models, animal (60) 60
amyotrophic lateral sclerosis - pathology (53) 53
mice, transgenic (53) 53
amyotrophic lateral sclerosis - metabolism (52) 52
motor-neuron degeneration (50) 50
transgenic mice (49) 49
motor-neuron disease (46) 46
cu,zn-superoxide dismutase (38) 38
mouse model (37) 37
oxidative stress (36) 36
transgenic mouse model (34) 34
superoxide dismutase (33) 33
amyotrophic lateral sclerosis - physiopathology (32) 32
spinal-cord (30) 30
amyotrophic lateral sclerosis - enzymology (27) 27
aggregation (26) 26
frontotemporal lobar degeneration (26) 26
motor neurons - pathology (26) 26
mutant sod1 (26) 26
mitochondria (25) 25
neurodegeneration (25) 25
wild-type (23) 23
superoxide dismutase - chemistry (22) 22
superoxide-dismutase (22) 22
disease progression (21) 21
motor-neurons (21) 21
protein folding (21) 21
als (20) 20
disease (20) 20
mice, inbred c57bl (20) 20
nervous system diseases (20) 20
proteins (20) 20
analysis (19) 19
clinical neurology (19) 19
familial als (19) 19
neurodegenerative diseases (19) 19
protein aggregation (19) 19
sod1 (19) 19
spinal cord - pathology (19) 19
superoxide (19) 19
alzheimers-disease (18) 18
cell biology (18) 18
cu/zn-superoxide-dismutase (18) 18
female (18) 18
motor neurons - metabolism (18) 18
mutations (18) 18
research (18) 18
apoptosis (17) 17
cu,zn superoxide-dismutase (17) 17
male (17) 17
neurology (17) 17
neurons (17) 17
cell line (16) 16
cu/zn superoxide-dismutase (16) 16
degeneration (16) 16
molecular-weight complexes (16) 16
toxicity (16) 16
wild-type sod1 (15) 15
amyotrophic lateral sclerosis - drug therapy (14) 14
cell-death (14) 14
pharmacology & pharmacy (14) 14
physiological aspects (14) 14
rodents (14) 14
spinal cord (14) 14
spinal cord - metabolism (14) 14
dna-binding proteins - metabolism (13) 13
genetics & heredity (13) 13
mitochondria - metabolism (13) 13
motor neurons (13) 13
mutation - genetics (13) 13
parkinsons-disease (13) 13
pathology (13) 13
rats (13) 13
alpha-synuclein (12) 12
biophysics (12) 12
development and progression (12) 12
medicine, research & experimental (12) 12
nervous system (12) 12
protein binding (12) 12
animal models (11) 11
axonal-transport (11) 11
blotting, western (11) 11
genetic aspects (11) 11
models, biological (11) 11
spinal muscular-atrophy (11) 11
amyotrophic lateral sclerosis - therapy (10) 10
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1. Full Text Is SOD1 loss of function involved in amyotrophic lateral sclerosis?
by Saccon, Rachele A and Bunton-Stasyshyn, Rosie K. A and Fisher, Elizabeth M.C and Fratta, Pietro
Brain, ISSN 0006-8950, 2013, Volume 136, Issue 8, pp. 2342 - 2358
Mutations in the gene superoxide dismutase 1 (SOD1) are causative for familial forms of the neurodegenerative disease amyotrophic lateral sclerosis. When the... 
Amyotrophic lateral sclerosis | Loss of function | Superoxide dismutase 1 | Motor neuron disease | motor neuron disease | OXIDATIVE STRESS | MARIE-TOOTH-DISEASE | CU,ZN-SUPEROXIDE DISMUTASE | MOTOR-NEURON LOSS | ALS-LINKED SOD1 | CU/ZN SUPEROXIDE-DISMUTASE | loss of function | amyotrophic lateral sclerosis | NEUROSCIENCES | CLINICAL NEUROLOGY | SPINAL MUSCULAR-ATROPHY | WILD-TYPE SOD1 | MITOCHONDRIAL DYSFUNCTION | MUTANT SOD1 | superoxide dismutase 1 | Phenotype | Superoxide Dismutase - genetics | Animals | Amyotrophic Lateral Sclerosis - genetics | Humans | Amyotrophic Lateral Sclerosis - metabolism | Mice, Transgenic | Mice | Mutation | Superoxide Dismutase-1 | Superoxide Dismutase - metabolism | Index Medicus | Abridged Index Medicus | Review
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2. Full Text Metal-deficient SOD1 in amyotrophic lateral sclerosis
by Hilton, James B and White, Anthony R and Crouch, Peter J
Journal of Molecular Medicine, ISSN 0946-2716, 5/2015, Volume 93, Issue 5, pp. 481 - 487
Mutations to the ubiquitous antioxidant enzyme Cu/Zn superoxide dismutase (SOD1) were the first established genetic cause of the fatal, adult-onset... 
Human Genetics | Biomedicine | Protein misfolding | Amyotrophic lateral sclerosis (ALS) | Zinc (Zn) | Internal Medicine | Molecular Medicine | Motor neuron disease (MND) | Cu/Zn superoxide dismutase (SOD1) | Diacetylbis(4-methylthiosemicarbazonato)copper II | Copper (Cu) | Diacetylbis(4-methylthiosemicarbazonato)copper | MOTOR-NEURONS | MEDICINE, RESEARCH & EXPERIMENTAL | ALS-LINKED SOD1 | POSTTRANSLATIONAL MODIFICATIONS | FAMILIAL ALS | Diacetylbis(4-methylthiosemicarbazonato)copper(II) | ZINC SUPEROXIDE-DISMUTASE | WILD-TYPE SOD1 | IN-VIVO | GENETICS & HEREDITY | MUTANT SOD1 | TRANSGENIC MOUSE MODEL | TYROSINE NITRATION | Protein Aggregates | Superoxide Dismutase - genetics | Amyotrophic Lateral Sclerosis - genetics | Humans | Rodentia | Metals - metabolism | Animals | Amyotrophic Lateral Sclerosis - metabolism | Superoxide Dismutase-1 | Copper - deficiency | Superoxide Dismutase - metabolism | Disease Models, Animal | Zinc - deficiency | Gene mutations | Physiological aspects | Amyotrophic lateral sclerosis | Development and progression | Superoxide dismutase | Genetic aspects | Research | Index Medicus | Zn superoxide dismutase (SOD1) | Diacetylbis(4-methylthiosemicarbazonato)copperII | Review
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3. Full Text Early Excitability Changes in Lumbar Motoneurons of Transgenic SOD1(G85R) and SOD1(G93A-Low) Mice
by Pambo-Pambo, A and Durand, J and Gueritaud, JP
JOURNAL OF NEUROPHYSIOLOGY, ISSN 0022-3077, 12/2009, Volume 102, Issue 6, pp. 3627 - 3642
Pambo-Pambo A, Durand J, Gueritaud JP. Early excitability changes in lumbar motoneurons of transgenic SOD1(G85R) and SOD1(G93A-Low) mice. J Neurophysiol 102:... 
PLATEAU POTENTIALS | PHYSIOLOGY | MOTOR-NEURON DEGENERATION | CALCIUM-CHANNELS | SPIKE FREQUENCY ADAPTATION | ALS-LINKED SOD1 | MOUSE MODEL | ELECTROPHYSIOLOGICAL PROPERTIES | PERSISTENT SODIUM CURRENT | SPINAL MOTONEURONS | NEUROSCIENCES | SUPEROXIDE-DISMUTASE GENE
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4. Full Text Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouse
by Wang, Lijun and Deng, Han-Xiang and Grisotti, Gabriella and Zhai, Hong and Siddique, Teepu and Roos, Raymond P
Human Molecular Genetics, ISSN 0964-6906, 5/2009, Volume 18, Issue 9, pp. 1642 - 1651
Approximately 10% of amyotrophic lateral sclerosis (ALS) cases are familial (FALS), and ∼25% of FALS cases are caused by mutations in Cu/Zn superoxide... 
MOTOR-NEURON DEGENERATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS-LINKED SOD1 | MITOCHONDRIA | GENETICS & HEREDITY | MUTANT SOD1 | TOXICITY | AMYOTROPHIC-LATERAL-SCLEROSIS | SUPEROXIDE-DISMUTASE 1 | AGGREGATION | TRANSGENIC MICE | CELL-DEATH | Gene Expression | Superoxide Dismutase - genetics | Spinal Cord - metabolism | Amyotrophic Lateral Sclerosis - genetics | Humans | Mice, Inbred C57BL | Male | Mice, Transgenic | Mutation, Missense | Disease Progression | Superoxide Dismutase - chemistry | Amyotrophic Lateral Sclerosis - pathology | Animals | Spinal Cord - pathology | Female | Amyotrophic Lateral Sclerosis - enzymology | Mice | Superoxide Dismutase-1 | Dimerization | Superoxide Dismutase - metabolism | Disease Models, Animal | Index Medicus
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5. Full Text Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice—a model of familial amyotrophic lateral sclerosis
by Poon, H. Fai and Hensley, Kenneth and Thongboonkerd, Visith and Merchant, Michael L and Lynn, Bert C and Pierce, William M and Klein, Jon B and Calabrese, Vittorio and Butterfield, D. Allan
Free Radical Biology and Medicine, ISSN 0891-5849, 2005, Volume 39, Issue 4, pp. 453 - 462
Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron degenerative disease characterized by the loss of neuronal function in the motor cortex, brain... 
ALS | Enzyme activity decline | Redox proteomics | Free radicals | Oxidatively modified proteins | Mechanisms of neurodegeneration | oxidatively modified proteins | free radicals | ALZHEIMERS-DISEASE BRAIN | enzyme activity decline | BIOCHEMISTRY & MOLECULAR BIOLOGY | COPPER/ZINC SUPEROXIDE-DISMUTASE | ALS-LINKED SOD1 | AXONAL DYSTROPHY GAD | redox proteomics | CARBOXY-TERMINAL HYDROLASE | mechanisms of neurodegeneration | HISTAMINE-RELEASING FACTOR | MOTOR-NEURON DEGENERATION | ENDOCRINOLOGY & METABOLISM | BODY-LIKE INCLUSIONS | CU,ZN-SUPEROXIDE DISMUTASE MUTANT | CONTROLLED TUMOR PROTEIN | Superoxide Dismutase - genetics | Spinal Cord - metabolism | Oxidation-Reduction | Electrophoresis, Gel, Two-Dimensional | Mice, Transgenic | Blotting, Western | Nerve Tissue Proteins - metabolism | Point Mutation | Animals | Amyotrophic Lateral Sclerosis - metabolism | Proteomics | Biomarkers, Tumor - metabolism | Ubiquitin Thiolesterase - metabolism | Mice | Disease Models, Animal | Ubiquitin | Enzymes | Neurosciences | Neurons | Amyotrophic lateral sclerosis | Zinc compounds | Analysis | Genetic aspects | Genetic engineering | Kidney diseases | Free radicals (Chemistry) | Mass spectrometry
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6. Full Text Experimental transmissibility of mutant SOD1 motor neuron disease
by Ayers, Jacob I and Fromholt, Susan and Koch, Morgan and DeBosier, Adam and McMahon, Ben and Xu, Guilian and Borchelt, David R
Acta Neuropathologica, ISSN 0001-6322, 12/2014, Volume 128, Issue 6, pp. 791 - 803
By unknown mechanisms, the symptoms of amyotrophic lateral sclerosis (ALS) seem to spread along neuroanatomical pathways to engulf the motor nervous system.... 
Pathology | Neurosciences | Transmissibility | Medicine & Public Health | Superoxide dismutase 1 | Motor neuron disease | Amyotrophic lateral sclerosis | Seeding | ALS-LINKED SOD1 | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | NEUROSCIENCES | FAMILIAL ALS | CLINICAL NEUROLOGY | SCRAPIE | WILD-TYPE SOD1 | PRION PROTEINS | SUPEROXIDE-DISMUTASE | MINK ENCEPHALOPATHY | AGGREGATION | TRANSGENIC MICE | Superoxide Dismutase - genetics | Amyotrophic Lateral Sclerosis - physiopathology | Paralysis - metabolism | Spinal Cord - pathology | Inclusion Bodies - metabolism | Motor Neuron Disease - physiopathology | Superoxide Dismutase - metabolism | Disease Models, Animal | Animals, Newborn | Genetic Predisposition to Disease | Mice, Inbred C57BL | Bacterial Proteins - genetics | Kaplan-Meier Estimate | Mice, Transgenic | Mice, Inbred C3H | Motor Neuron Disease - pathology | Animals | Inclusion Bodies - pathology | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Spinal Cord - physiopathology | Mutation | Superoxide Dismutase-1 | Microscopy, Fluorescence | Luminescent Proteins - metabolism | Proteins | Development and progression | Superoxide | Genetic engineering | Neurons | Index Medicus
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7. Full Text In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants
by Luchinat, Enrico and Barbieri, Letizia and Rubino, Jeffrey T and Kozyreva, Tatiana and Cantini, Francesca and Banci, Lucia
Nature Communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, pp. 5502 - 5502
Mutations in the superoxide dismutase 1 (SOD1) gene are related to familial cases of amyotrophic lateral sclerosis (fALS). Here we exploit in-cell NMR to... 
DISULFIDE REDUCTION | COPPER CHAPERONE | PROTEIN AGGREGATION | MULTIDISCIPLINARY SCIENCES | ALS-LINKED SOD1 | MOUSE MODEL | HUMAN SUPEROXIDE-DISMUTASE | AMYOTROPHIC-LATERAL-SCLEROSIS | FAMILIAL FORM | MOLECULAR-WEIGHT COMPLEXES | TRANSGENIC MICE | Superoxide Dismutase - genetics | Molecular Chaperones - metabolism | Zinc - metabolism | Amyotrophic Lateral Sclerosis - genetics | Humans | Amyotrophic Lateral Sclerosis - metabolism | Copper - metabolism | HEK293 Cells | Nuclear Magnetic Resonance, Biomolecular | Superoxide Dismutase-1 | Protein Folding | Superoxide Dismutase - metabolism | Index Medicus
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8. Full Text Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants
by Banerjee, Victor and Shani, Tom and Katzman, Bella and Vyazmensky, Maria and Papo, Niv and Israelson, Adrian and Engel, Stanislav
ACS Chemical Neuroscience, ISSN 1948-7193, 11/2016, Volume 7, Issue 11, pp. 1595 - 1606
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder that leads to the death of the upper and lower motor neurons. Superoxide dismutase 1 (SOD1)... 
stability patches | amyloid aggregation | Amyotrophic lateral sclerosis (ALS) | gain-of-function | steered molecular dynamics (SMD) | superoxide dismutase 1 (SOD1) | MOLECULAR-DYNAMICS | CHEMISTRY, MEDICINAL | MALATE-DEHYDROGENASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS-LINKED SOD1 | TOXICITY | NEUROSCIENCES | MISFOLDED SOD1 | IN-VITRO | MOTOR-NEURON DEGENERATION | WILD-TYPE SOD1 | MOUSE MODEL | HOT-SPOTS | Recombinant Proteins - metabolism | Amino Acid Sequence | Microscopy, Electron, Transmission | Escherichia coli | Humans | Protein Multimerization | Recombinant Proteins - genetics | Molecular Dynamics Simulation | Protein Folding | Peptides - metabolism | Superoxide Dismutase-1 - metabolism | Surface Properties | Amyotrophic Lateral Sclerosis - metabolism | Superoxide Dismutase-1 - genetics | Protein Interaction Domains and Motifs | Kinetics | Protein Stability | Protein Aggregation, Pathological - genetics | Protein Aggregation, Pathological - metabolism
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9. Full Text Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice
by Xu, Guilian and Ayers, Jacob I and Roberts, Brittany L and Brown, Hilda and Fromholt, Susan and Green, Cameron and Borchelt, David R
Human Molecular Genetics, ISSN 0964-6906, 02/2015, Volume 24, Issue 4, pp. 1019 - 1035
Co-expression of wild-type human superoxide dismutase 1 (WT-hSOD1) with ALS mutant hSOD1 accelerates disease onset relative to mice expressing only mutant... 
SUPEROXIDE-DISMUTASE-1 | PROTEIN | MOTOR-NEURON DEGENERATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS-LINKED SOD1 | DISEASE | GENETICS & HEREDITY | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | SUPEROXIDE-DISMUTASE 1 | FAMILIAL ALS | AGGREGATION | Cell Line | Gene Expression | Superoxide Dismutase - genetics | Amyotrophic Lateral Sclerosis - genetics | Humans | Protein Multimerization | RNA, Messenger - genetics | Male | Mice, Transgenic | Mutant Proteins - metabolism | RNA, Messenger - metabolism | Amyotrophic Lateral Sclerosis - mortality | Protein Transport | Motor Neurons - metabolism | Superoxide Dismutase - chemistry | Animals | Amyotrophic Lateral Sclerosis - metabolism | Protein Binding | Female | Mice | Mutation | Superoxide Dismutase-1 | Superoxide Dismutase - metabolism | Disease Models, Animal | Index Medicus
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10. Full Text Amyotrophic Lateral Sclerosis-Associated SOD1 Mutant Proteins Bind and Aggregate with Bcl-2 in Spinal Cord Mitochondria
by Pasinelli, Piera and Belford, Mary Elizabeth and Lennon, Niall and Bacskai, Brian J and Hyman, Bradley T and Trotti, Davide and Brown, Robert H
Neuron, ISSN 0896-6273, 2004, Volume 43, Issue 1, pp. 19 - 30
Familial amyotrophic lateral sclerosis (ALS)-linked mutations in the copper-zinc superoxide dismutase (SOD1) gene cause motor neuron death in about 3% of ALS... 
PROGRAMMED CELL-DEATH | OXIDATIVE DAMAGE | APOPTOTIC DEATH | ALS-LINKED SOD1 | MICE | MUTATIONS | TRANSGENIC MOUSE MODEL | NEUROSCIENCES | MOTOR-NEURON DEATH | SUPEROXIDE-DISMUTASE GENE | DEGENERATION | Mitochondria - enzymology | Liver - pathology | Protein Binding - genetics | Superoxide Dismutase - genetics | Anterior Horn Cells - metabolism | Liver - enzymology | Molecular Weight | Humans | Apoptosis - genetics | Proto-Oncogene Proteins c-bcl-2 - metabolism | Superoxide Dismutase - toxicity | Motor Neuron Disease - metabolism | Protein Isoforms - metabolism | Anterior Horn Cells - enzymology | Mitochondria - genetics | Motor Neuron Disease - genetics | Motor Neuron Disease - physiopathology | Superoxide Dismutase - metabolism | Mitochondria - metabolism | Protein Structure, Tertiary - genetics | Binding Sites - genetics | Mutation - genetics | Macromolecular Substances | Animals | Cell Line, Tumor | Mice | Superoxide Dismutase-1 | Proto-Oncogene Proteins c-bcl-2 - genetics | Protein Isoforms - genetics | Amyotrophic lateral sclerosis | Spinal cord | Mutation | Apoptosis
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11. Full Text Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis
by Parone, Philippe A and Da Cruz, Sandrine and Han, Joo Seok and McAlonis-Downes, Melissa and Vetto, Anne P and Lee, Sandra K and Tseng, Eva and Cleveland, Don W
Journal of Neuroscience, ISSN 0270-6474, 03/2013, Volume 33, Issue 11, pp. 4657 - 4671
Mitochondria have been proposed as targets for toxicity in amyotrophic lateral sclerosis (ALS), a progressive, fatal adult-onset neurodegenerative disorder... 
PERMEABILITY TRANSITION PORE | WILD-TYPE | PROLONGS SURVIVAL | CU/ZN-SUPEROXIDE-DISMUTASE | CYCLOPHILIN-D | CU,ZN-SUPEROXIDE DISMUTASE | INTRACELLULAR CALCIUM | ALS-LINKED SOD1 | SPINAL-CORD | NEUROSCIENCES | DISEASE PROGRESSION | Superoxide Dismutase - genetics | Immunoprecipitation | Calcium - metabolism | Cyclophilins - deficiency | Humans | Glial Fibrillary Acidic Protein - metabolism | Motor Neurons - pathology | Motor Neurons - ultrastructure | Cell Death - genetics | Mitochondria - genetics | Adenosine Triphosphate - metabolism | Microfilament Proteins - metabolism | Neuromuscular Junction - pathology | Superoxide Dismutase - metabolism | Disease Models, Animal | Calcium-Binding Proteins - metabolism | Microscopy, Electron, Transmission | Amyotrophic Lateral Sclerosis - genetics | Mice, Inbred C57BL | Mice, Transgenic | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Amyotrophic Lateral Sclerosis - mortality | Antibodies - pharmacology | Superoxide Dismutase - immunology | Amyotrophic Lateral Sclerosis - pathology | Animals | Axons - pathology | Mice | Superoxide Dismutase-1 | Chromatography, Gel | In Vitro Techniques | Hand Strength - physiology
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12. Full Text Oral Treatment with Cu-II(atsm) Increases Mutant SOD1 In Vivo but Protects Motor Neurons and Improves the Phenotype of a Transgenic Mouse Model of Amyotrophic Lateral Sclerosis
by Roberts, BR and Lim, NKH and McAllum, EJ and Donnelly, PS and Hare, DJ and Doble, PA and Turner, BJ and Price, KA and Lim, SC and Paterson, BM and Hickey, JL and Rhoads, TW and Williams, JR and Kanninen, KM and Hung, LW and Liddell, JR and Grubman, A and Monty, JF and Llanos, RM and Kramer, DR and Mercer, JFB and Bush, AI and Masters, CL and Duce, JA and Li, QX and Beckman, JS and Barnham, KJ and White, AR and Crouch, PJ
JOURNAL OF NEUROSCIENCE, ISSN 0270-6474, 06/2014, Volume 34, Issue 23, pp. 8021 - 8031
Mutations in the metallo-protein Cu/Zn-superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis (ALS) in humans and an expression level-dependent... 
PROLONGS SURVIVAL | WILD-TYPE SOD1 | ALS-LINKED SOD1 | CU/ZN SUPEROXIDE-DISMUTASE | SPINAL-CORD | BINDING-SITE | POSTTRANSLATIONAL MODIFICATIONS | HEXANUCLEOTIDE REPEAT | NEUROSCIENCES | MASS-SPECTROMETRY | FAMILIAL ALS
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13. Full Text E6-AP association promotes SOD1 aggresomes degradation and suppresses toxicity
by Mishra, Amit and Maheshwari, Megha and Chhangani, Deepak and Fujimori-Tonou, Noriko and Endo, Fumito and Joshi, Ajay Prakash and Jana, Nihar Ranjan and Yamanaka, Koji
Neurobiology of Aging, ISSN 0197-4580, 2013, Volume 34, Issue 4, pp. 1310.e11 - 1310.e23
Abstract Protein aggregation and ordered fibrillar amyloid deposition inside and outside of the central nervous system cells is the common pathologic hallmark... 
Neurology | Internal Medicine | Cytotoxicity | Amyotrophic lateral sclerosis | E6-AP | SOD1 | CONFERS PROTECTION | UNFOLDED PROTEIN | PROTEASOMAL DEGRADATION | ALS-LINKED SOD1 | CU/ZN SUPEROXIDE-DISMUTASE | HEAT-SHOCK | AMYOTROPHIC-LATERAL-SCLEROSIS | NEUROSCIENCES | UBIQUITIN LIGASE E6-AP | GERIATRICS & GERONTOLOGY | CO-CHAPERONE CHIP | MUTANT SOD1 | Cell Survival | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Mice, Transgenic | Amyotrophic Lateral Sclerosis - pathology | Animals | Amyotrophic Lateral Sclerosis - metabolism | Cell Aggregation | Mice | Neurons - metabolism | Superoxide Dismutase-1 | Inclusion Bodies - metabolism | Superoxide Dismutase - metabolism | Ubiquitin | Nervous system diseases | Neurosciences | Ligases | Analysis | Heat shock proteins | Superoxide | Universities and colleges | Paralysis | Index Medicus
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