about
sameAs
P688
Differential localization of placental extracellular superoxide dismutase as pregnancy progressesSuperoxide dismutase isoenzymes in the normal and diseased human corneaExpression of superoxide dismutase in whole lens prevents cataract formationDifferential effects of superoxide dismutase isoform expression on hydroperoxide-induced apoptosis in PC-12 cellsMitochondrial damage due to SOD1 deficiency in SH-SY5Y neuroblastoma cells: a rationale for the redundancy of SOD1Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosisActivation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivoBinding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric proteinMitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutaseMutation of SOD1 in ALS: a gain of a loss of functionModulation of 3-hydroxy-3-methylglutaryl-CoA reductase gene expression by CuZn superoxide dismutase in human fibroblasts and HepG2 cellsSOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS modelSuperoxide dismutase 1 knock-down induces senescence in human fibroblastsThe copper chaperone CCS directly interacts with copper/zinc superoxide dismutaseRapid endocytosis of copper-zinc superoxide dismutase into human endothelial cells: role for its vascular activityGene transfer of CuZn superoxide dismutase enhances the synthesis of vascular endothelial growth factorMitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generationEffects of ALS-related SOD1 mutants on dynein- and KIF5-mediated retrograde and anterograde axonal transportGlycolaldehyde induces apoptosis in a human breast cancer cell lineOverexpression of human copper, zinc-superoxide dismutase (SOD1) prevents postischemic injuryCuZn-superoxide dismutase, extracellular superoxide dismutase, and glutathione peroxidase in blood from individuals homozygous for Asp90Ala CuZu-superoxide dismutase mutationImplication of copper zinc superoxide dismutase (SOD-1) in human placenta developmentCopper,zinc superoxide dismutase is primarily a cytosolic protein in human cellsEarly thymic T cell development in young transgenic mice overexpressing human Cu/Zn superoxide dismutase, a model of Down syndromeDJ-1 is a copper chaperone acting on SOD1 activationSIRT5 desuccinylates and activates SOD1 to eliminate ROSStructural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsEndothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferasesMolecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosisA new transcriptional role for matrix metalloproteinase-12 in antiviral immunityProgressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALSInitiation and elongation in fibrillation of ALS-linked superoxide dismutase.Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.
P921
Q22254715-FB15F3F8-7F85-4469-8350-20B8A66ED237Q24291622-7BB504E4-2AD5-4CE3-8867-24722731E462Q24293031-D60FE89F-10BA-489F-98E9-D53241547BD5Q24293297-5DD667A6-6C84-47A4-8632-9D81A33FB3C2Q24294416-3ACCE135-0E7B-447F-A999-C9705C642316Q24297625-7ED91AF7-4DB1-4571-8776-DC784523C373Q24298397-36DB414A-3F9F-45D1-9147-B8EED5716431Q24300789-13E7380E-1010-4E16-A173-549B53EF55F0Q24305099-B223A2E6-F6DF-4D1B-BE6B-ED6CAEFD9359Q24305971-E9F36141-CD8D-4533-A297-8983930DAB24Q24306617-728A582F-766C-47A4-83DB-64A99455A124Q24307703-794AAEC5-5DF3-431D-8C9E-C9B48C76C95EQ24310059-D96E1F0B-5D51-42F8-A4B4-C2C4539A4092Q24310363-85499677-D6FE-473A-BD27-47F14B09B3B5Q24310687-4A55883A-3420-4B3C-BC13-1D7DCA902C53Q24314945-549CB354-1CAB-4FB8-B28D-1CC0D0D201E9Q24314962-4F059181-A493-47B0-B9F4-77E91ADD2312Q24315910-8F3D036C-275A-47E8-A258-CE85DD51F897Q24315999-63F5732B-2770-43E4-AF45-1A313080205EQ24323877-ACC5BA24-F010-41B7-B567-00ED84563539Q24336053-B1834A70-2665-4D71-B542-06BD604F80BAQ24337120-8B68F2AB-7DAA-453A-A1E7-0588FE3A011FQ24337522-3CFA24DB-CD76-4ED6-9847-DE77ECD0D7EBQ24337642-F45A4B12-36AD-4E20-811B-0CB46FD5C4B9Q24338208-6BD9A093-5C73-4315-8A2A-A9FF2017979AQ24338611-7EE36FDB-6FB2-4E7C-BB91-D85777EBBC5EQ27654799-3748E5F0-111D-4F10-A1D9-E3DB5A573C03Q28115819-96E7F317-EBE6-45CF-BED7-DD1C0DCDDD3DQ28115951-86FF70BE-0131-47DA-AE1E-323E47ABD620Q28910180-4FA0117D-BE21-4434-A725-C688A770E1EEQ33403156-CA067898-C092-4B8E-978D-E04138EC3F09Q34572921-CF4E74E9-1D62-4B4D-B62E-B5E64F785C05Q35854965-91E77E37-2CE0-4E71-B50A-E272B495CE94Q36978868-4873AD91-9065-4C13-8063-3EF65B33CE3BQ37416520-0EECABF9-D9C5-4261-8E15-45DFCEAE6007
P921
description
Säugetierprotein
@de
mammalian protein found in Homo sapiens
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in SOD1
@nl
protèin
@ace
protéine
@fr
بروتين في الإنسان العاقل
@ar
name
SOD1
@fr
SOD1
@nl
Superoksididismutaasi 1
@fi
Superoxide dismutase 1
@en
Супероксиддисмутаза 1
@ru
type
label
SOD1
@fr
SOD1
@nl
Superoksididismutaasi 1
@fi
Superoxide dismutase 1
@en
Супероксиддисмутаза 1
@ru
altLabel
Cu/Zn superoxide dismutase
@en
SOD, soluble
@en
SOD1
@en
SOD1
@fi
SOD1
@ru
epididymis secretory protein Li 44
@en
hSod1
@en
indophenoloxidase A
@en
superoxide dismutase 1, soluble
@en
superoxide dismutase [Cu-Zn]
@en
prefLabel
SOD1
@fr
SOD1
@nl
Superoksididismutaasi 1
@fi
Superoxide dismutase 1
@en
Супероксиддисмутаза 1
@ru
P638
P680
P681
P682
P352
P486
P637
P646
P31
P352
P361
P486
D000072105
P637
P638
P646
/m/03cc418
P680
P681
P682
P702
P703
P705
ENSP00000270142
ENSP00000374645