| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| A L Lamb, A K Wernimont, R A Pufahl, T V O'Halloran, A C Rosenzwei. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. vol 39. issue 7. 2000-03-13. PMID:10677207. |
mutations in sod1 are linked to familial amyotrophic lateral sclerosis (fals), a fatal neurodegenerative disorder. |
2000-03-13 |
2023-08-12 |
human |
| R W Orrel. Amyotrophic lateral sclerosis: copper/zinc superoxide dismutase (SOD1) gene mutations. Neuromuscular disorders : NMD. vol 10. issue 1. 2000-03-07. PMID:10677867. |
amyotrophic lateral sclerosis: copper/zinc superoxide dismutase (sod1) gene mutations. |
2000-03-07 |
2023-08-12 |
Not clear |
| R W Orrel. Amyotrophic lateral sclerosis: copper/zinc superoxide dismutase (SOD1) gene mutations. Neuromuscular disorders : NMD. vol 10. issue 1. 2000-03-07. PMID:10677867. |
mutations of the sod1 gene, encoding the enzyme copper/zinc superoxide dismutase, have been identified in around 20% of patients with familial amyotrophic lateral sclerosis (als), and also in patients with apparently sporadic als. |
2000-03-07 |
2023-08-12 |
Not clear |
| S Kohno, Y Takahashi, H Miyajima, M Serizawa, K Mizoguch. A novel mutation (Cys6Gly) in the Cu/Zn superoxide dismutase gene associated with rapidly progressive familial amyotrophic lateral sclerosis. Neuroscience letters. vol 276. issue 2. 2000-02-15. PMID:10624810. |
autosomal-dominant familial amyotrophic lateral sclerosis (fals) is associated with mutation in the gene that encodes cu/zn superoxide dismutase (sod1). |
2000-02-15 |
2023-08-12 |
Not clear |
| M Azzouz, P Poindron, S Guettier, N Leclerc, C Andres, J M Warter, J Bor. Prevention of mutant SOD1 motoneuron degeneration by copper chelators in vitro. Journal of neurobiology. vol 42. issue 1. 2000-02-08. PMID:10623900. |
an animal model of familial amyotrophic lateral sclerosis (fals) has been generated by overexpression of human cuzn superoxide dismutase (sod1) containing a substitution of glycine to alanine at position 93 in transgenic g93a mice. |
2000-02-08 |
2023-08-12 |
mouse |
| D Liu, J Wen, J Liu, L L. The roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, DNA, and membrane phospholipids. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. vol 13. issue 15. 2000-01-06. PMID:10593879. |
to explore whether reactive oxygen species (ros) play a role in the pathogenesis of amyotrophic lateral sclerosis (als), a unique microdialysis or microcannula sampling technique was used in mice transfected with a mutant cu,zn-superoxide dismutase (sod1) gene from humans with familial als, mice transfected with the normal human sod1 gene, and normal mice. |
2000-01-06 |
2023-08-12 |
mouse |
| D Liu, J Wen, J Liu, L L. The roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, DNA, and membrane phospholipids. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. vol 13. issue 15. 2000-01-06. PMID:10593879. |
the elevated h(2)o(2) in mutant mice indicates impairment of its detoxification pathways, perhaps by changed interactions between sod1 and h(2)o(2) detoxification enzymes.-liu, d., wen, j., liu, j., li, l. the roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, dna, and membrane phospholipids. |
2000-01-06 |
2023-08-12 |
mouse |
| S Vukosavic, M Dubois-Dauphin, N Romero, S Przedborsk. Bax and Bcl-2 interaction in a transgenic mouse model of familial amyotrophic lateral sclerosis. Journal of neurochemistry. vol 73. issue 6. 1999-12-27. PMID:10582606. |
it has been proposed that mutations in copper/zinc-superoxide dismutase (sod1), the only proven cause of amyotrophic lateral sclerosis (als), induce the disease by a toxic property that promotes apoptosis. |
1999-12-27 |
2023-08-12 |
mouse |
| Y Kokubo, S Kuzuhara, Y Narita, K Kikugawa, R Nakano, T Inuzuka, S Tsuji, M Watanabe, T Miyazaki, S Murayama, Y Ihar. Accumulation of neurofilaments and SOD1-immunoreactive products in a patient with familial amyotrophic lateral sclerosis with I113T SOD1 mutation. Archives of neurology. vol 56. issue 12. 1999-12-16. PMID:10593307. |
accumulation of neurofilaments and sod1-immunoreactive products in a patient with familial amyotrophic lateral sclerosis with i113t sod1 mutation. |
1999-12-16 |
2023-08-12 |
Not clear |
| Y Kokubo, S Kuzuhara, Y Narita, K Kikugawa, R Nakano, T Inuzuka, S Tsuji, M Watanabe, T Miyazaki, S Murayama, Y Ihar. Accumulation of neurofilaments and SOD1-immunoreactive products in a patient with familial amyotrophic lateral sclerosis with I113T SOD1 mutation. Archives of neurology. vol 56. issue 12. 1999-12-16. PMID:10593307. |
to report neuropathologic features of argyrophilic inclusions in the anterior horn cells, motor cortex betz cells, and neurons of the medullary reticular formation, spinal posterior horn, and clarke column in a japanese case of familial amyotrophic lateral sclerosis with i113t substitution in exon 4 of the copper-zinc superoxide dismutase (sod1) gene. |
1999-12-16 |
2023-08-12 |
Not clear |
| M M Reinholz, C M Merkle, J F Podusl. Therapeutic benefits of putrescine-modified catalase in a transgenic mouse model of familial amyotrophic lateral sclerosis. Experimental neurology. vol 159. issue 1. 1999-10-07. PMID:10486188. |
dominant mutations in the copper/zinc superoxide dismutase (sod1) gene have been observed in 15-20% of familial amyotrophic lateral sclerosis (fals) cases. |
1999-10-07 |
2023-08-12 |
mouse |
| T Ratovitski, L B Corson, J Strain, P Wong, D W Cleveland, V C Culotta, D R Borchel. Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. Human molecular genetics. vol 8. issue 8. 1999-09-14. PMID:10400992. |
mutations in superoxide dismutase 1 (sod1) polypeptides cause a form of familial amyotrophic lateral sclerosis (fals). |
1999-09-14 |
2023-08-12 |
Not clear |
| S Nagano, Y Ogawa, T Yanagihara, S Sakod. Benefit of a combined treatment with trientine and ascorbate in familial amyotrophic lateral sclerosis model mice. Neuroscience letters. vol 265. issue 3. 1999-07-01. PMID:10327155. |
we previously reported that the common toxic gain-of-function in various mutant copper-zinc superoxide dismutases (sod1) seen in patients with familial amyotrophic lateral sclerosis (als) was an abnormal copper release from the enzyme protein. |
1999-07-01 |
2023-08-12 |
mouse |
| N Shibata, A Hirano, S Kato, R Nagai, S Horiuchi, T Komori, T Umahara, K Asayama, M Kobayash. Advanced glycation endproducts are deposited in neuronal hyaline inclusions: a study on familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Acta neuropathologica. vol 97. issue 3. 1999-06-30. PMID:10090670. |
to determine the role of advanced glycation endproducts (age) in the pathogenesis of familial amyotrophic lateral sclerosis (als) with superoxide dismutase-1 (sod1) mutation, we investigated the immunohistochemical localization of n(epsilon)-carboxymethyl-lysine (cml), one of the major age structures, in spinal cords from three familial als patients with a heterozygous ala to val substitution at codon 4 in the gene for sod1. |
1999-06-30 |
2023-08-12 |
Not clear |
| S Kato, S Horiuchi, K Nakashima, A Hirano, N Shibata, I Nakano, M Saito, M Kato, K Asayama, E Oham. Astrocytic hyaline inclusions contain advanced glycation endproducts in familial amyotrophic lateral sclerosis with superoxide dismutase 1 gene mutation: immunohistochemical and immunoelectron microscopical analyses. Acta neuropathologica. vol 97. issue 3. 1999-06-30. PMID:10090673. |
to clarify the neuropathological significance of the deposition of n(epsilon)-carboxymethyl lysine (cml), an advanced glycation endproduct, in astrocytic hyaline inclusions in familial amyotrophic lateral sclerosis (fals), autopsy specimens from five members of two different families who had the superoxide dismutase 1 (sod1) gene mutations were analysed. |
1999-06-30 |
2023-08-12 |
human |
| G Almer, S Vukosavic, N Romero, S Przedborsk. Inducible nitric oxide synthase up-regulation in a transgenic mouse model of familial amyotrophic lateral sclerosis. Journal of neurochemistry. vol 72. issue 6. 1999-06-14. PMID:10349851. |
mutations in copper/zinc superoxide dismutase (sod1) are associated with a familial form of amyotrophic lateral sclerosis (als), and their expression in transgenic mice produces an als-like syndrome. |
1999-06-14 |
2023-08-12 |
mouse |
| D Trotti, A Rolfs, N C Danbolt, R H Brown, M A Hedige. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nature neuroscience. vol 2. issue 5. 1999-05-25. PMID:10321246. |
sod1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. |
1999-05-25 |
2023-08-12 |
human |
| D Trotti, A Rolfs, N C Danbolt, R H Brown, M A Hedige. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nature neuroscience. vol 2. issue 5. 1999-05-25. PMID:10321246. |
the mechanism by which cu2+/zn2+ superoxide dismutase (sod1) mutants lead to motor neuron degeneration in familial amyotrophic lateral sclerosis (fals) is unknown. |
1999-05-25 |
2023-08-12 |
human |
| H Warita, Y Itoyama, K Ab. Selective impairment of fast anterograde axonal transport in the peripheral nerves of asymptomatic transgenic mice with a G93A mutant SOD1 gene. Brain research. vol 819. issue 1-2. 1999-05-17. PMID:10082867. |
transgenic mice that express a mutant cu/zn superoxide dismutase (sod1) gene have been provided a valuable model for human amyotrophic lateral sclerosis (als). |
1999-05-17 |
2023-08-12 |
mouse |
| T Nakanishi, M Kishikawa, A Miyazaki, A Shimizu, Y Ogawa, S Sakoda, T Ohi, H Shoj. Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry. Journal of neuroscience methods. vol 81. issue 1-2. 1999-05-12. PMID:9696308. |
mutations in cu/zn superoxide dismutase (sod1) cause a subset of cases of familial amyotrophic lateral sclerosis (fals). |
1999-05-12 |
2023-08-12 |
Not clear |