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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004319naa a2200541 4500
001oai:DiVA.org:umu-42155
003SwePub
008110406s2010 | |||||||||||000 ||eng|
009oai:DiVA.org:kth-79022
009oai:slubar.slu.se:61127
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-421552 URI
0247 a https://doi.org/10.1111/j.1471-4159.2010.06753.x2 DOI
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-790222 URI
0247 a https://res.slu.se/id/publ/611272 URI
040 a (SwePub)umud (SwePub)kthd (SwePub)slu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Bergemalm, Danielu Umeå universitet,Klinisk kemi4 aut0 (Swepub:umu)dalbem99
2451 0a Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice
264 c 2010-04-19
264 1b Wiley,c 2010
338 a print2 rdacarrier
500 a QC 20120216
520 a 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.
650 7a LANTBRUKSVETENSKAPERx Lantbruksvetenskap, skogsbruk och fiskex Jordbruksvetenskap0 (SwePub)401012 hsv//swe
650 7a AGRICULTURAL SCIENCESx Agriculture, Forestry and Fisheriesx Agricultural Science0 (SwePub)401012 hsv//eng
653 a amyotrophic lateral sclerosis;endoplasmic reticulum;inclusion;proteomics;superoxide dismutase-1;transgenic mice
653 a MEDICINE
653 a MEDICIN
653 a medicin
653 a Medicine
7001 a Forsberg, Karinu Umeå universitet,Patologi,Thomas Brännström4 aut0 (Swepub:umu)nonkin02
7001 a Srivastava, Vaibhavu Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för skoglig genetik och växtfysiologi,Department of Forest Genetics and Plant Physiology4 aut0 (Swepub:slu)52285
7001 a Graffmo, Karin Su Umeå universitet,Patologi4 aut0 (Swepub:umu)kanerl79
7001 a Andersen, Peter Mu Umeå universitet,Neurologi4 aut0 (Swepub:umu)pean0001
7001 a Brännström, Thomasu Umeå universitet,Patologi4 aut0 (Swepub:umu)thbr0001
7001 a Wingsle, Gunnaru Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för skoglig genetik och växtfysiologi,Department of Forest Genetics and Plant Physiology4 aut0 (Swepub:slu)48677
7001 a Marklund, Stefan Lu Umeå universitet,Klinisk kemi4 aut0 (Swepub:umu)stma0003
7102 a Umeå universitetb Klinisk kemi4 org
7102 a Sveriges lantbruksuniversitet
7730 t Journal of Neurochemistryd : Wileyg 114:2, s. 408-418q 114:2<408-418x 0022-3042x 1471-4159
8564 u https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1471-4159.2010.06753.x
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-42155
8564 8u https://doi.org/10.1111/j.1471-4159.2010.06753.x
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-79022
8564 8u https://res.slu.se/id/publ/61127

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