{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Karch CM"],"funding":["NINDS NIH HHS"],"pagination":["1092-100"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3971727"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["113(5)"],"pubmed_abstract":["Amyotrophic lateral sclerosis is a progressively paralytic neurodegenerative disease that can be caused by mutations in Cu,Zn-superoxide dismutase 1 (SOD1). Transgenic mice that over-express mutant SOD1 develop paralysis and accumulate aggregates of mutant protein in the brainstem and spinal cord. The present study uses a cell culture model to demonstrate alpha B-crystallin is capable of reducing aggregation of mutant SOD1. To test the role of alpha B-crystallin in modulating SOD1 aggregation in vivo, alpha B-crystallin deficient mice were bred to mice expressing two different SOD1 mutants (G37R and L126Z). Although completely eliminating alpha B-crystallin reduced the interval to disease endstage by 20-30 days in mice expressing either mutant, there were no detectable changes in the level"],"journal":["Journal of neurochemistry"],"pubmed_title":["An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis."],"pmcid":["PMC3971727"],"funding_grant_id":["P01 NS049134","NS044278","R01 NS044278"],"pubmed_authors":["Karch CM","Borchelt DR"],"additional_accession":[]},"is_claimable":false,"name":"An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis.","description":"Amyotrophic lateral sclerosis is a progressively paralytic neurodegenerative disease that can be caused by mutations in Cu,Zn-superoxide dismutase 1 (SOD1). Transgenic mice that over-express mutant SOD1 develop paralysis and accumulate aggregates of mutant protein in the brainstem and spinal cord. The present study uses a cell culture model to demonstrate alpha B-crystallin is capable of reducing aggregation of mutant SOD1. To test the role of alpha B-crystallin in modulating SOD1 aggregation in vivo, alpha B-crystallin deficient mice were bred to mice expressing two different SOD1 mutants (G37R and L126Z). Although completely eliminating alpha B-crystallin reduced the interval to disease endstage by 20-30 days in mice expressing either mutant, there were no detectable changes in the level","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jun","modification":"2025-04-04T01:27:15.502Z","creation":"2019-03-27T01:24:15Z"},"accession":"S-EPMC3971727","cross_references":{"pubmed":["20067574"],"doi":["10.1111/j.1471-4159.2010.06572.x"]}}