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Superoxide dismutas...
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Bergemalm, DanielUmeå universitet,Klinisk kemi
(författare)
Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice
- Artikel/kapitelEngelska2010
Förlag, utgivningsår, omfång ...
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2010-04-19
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Wiley,2010
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printrdacarrier
Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:umu-42155
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-42155URI
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https://doi.org/10.1111/j.1471-4159.2010.06753.xDOI
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https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-79022URI
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https://res.slu.se/id/publ/61127URI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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QC 20120216
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Mutant superoxide dismutase-1 (SOD1) causes amyotrophic lateral sclerosis (ALS) through a cytotoxic mechanism of unknown nature. A hallmark in ALS patients and transgenic mouse models carrying human SOD1 (hSOD1) mutations are hSOD1-immunoreactive inclusions in spinal cord ventral horns. The hSOD1 inclusions may block essential cellular functions or cause toxicity through sequestering of other proteins. Inclusions from four different transgenic mouse models were examined after density gradient ultracentrifugation. The inclusions are complex structures with heterogeneous densities and are disrupted by detergents. The aggregated hSOD1 was mainly composed of subunits that lacked the native stabilizing intra-subunit disulfide bond. A proportion of subunits formed hSOD1 oligomers or was bound to other proteins through disulfide bonds. Dense inclusions could be isolated and the protein composition was analyzed using proteomic techniques. Mutant hSOD1 accounted for half of the protein. Ten other proteins were identified. Two were cytoplasmic chaperones, four were cytoskeletal proteins, and 4 were proteins that normally reside in the endoplasmic reticulum (ER). The presence of ER proteins in inclusions containing the primarily cytosolic hSOD1 further supports the notion that ER stress is involved in ALS.
Ämnesord och genrebeteckningar
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Forsberg, KarinUmeå universitet,Patologi,Thomas Brännström(Swepub:umu)nonkin02
(författare)
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Srivastava, VaibhavSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för skoglig genetik och växtfysiologi,Department of Forest Genetics and Plant Physiology(Swepub:slu)52285
(författare)
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Graffmo, Karin SUmeå universitet,Patologi(Swepub:umu)kanerl79
(författare)
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Andersen, Peter MUmeå universitet,Neurologi(Swepub:umu)pean0001
(författare)
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Brännström, ThomasUmeå universitet,Patologi(Swepub:umu)thbr0001
(författare)
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Wingsle, GunnarSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för skoglig genetik och växtfysiologi,Department of Forest Genetics and Plant Physiology(Swepub:slu)48677
(författare)
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Marklund, Stefan LUmeå universitet,Klinisk kemi(Swepub:umu)stma0003
(författare)
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Umeå universitetKlinisk kemi
(creator_code:org_t)
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Sveriges lantbruksuniversitet
Sammanhörande titlar
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Ingår i:Journal of Neurochemistry: Wiley114:2, s. 408-4180022-30421471-4159
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