{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kumar MS"],"funding":["NCATS NIH HHS","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["16013"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9784173"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(24)"],"pubmed_abstract":["ALS-linked mutations induce aberrant conformations within the SOD1 protein that are thought to underlie the pathogenic mechanism of SOD1-mediated ALS. Although clinical trials are underway for gene silencing of <i>SOD1</i>, these approaches reduce both wild-type and mutated forms of SOD1. Here, we sought to develop anti-SOD1 nanobodies with selectivity for mutant and misfolded forms of human SOD1 over wild-type SOD1. Characterization of two anti-SOD1 nanobodies revealed that these biologics stabilize mutant SOD1 in vitro. Further, SOD1 expression levels were enhanced and the physiological subcellular localization of mutant SOD1 was restored upon co-expression of anti-SOD1 nanobodies in immortalized cells. In human motor neurons harboring the <i>SOD1 A4V</i> mutation, anti-SOD1 nanobody exp"],"journal":["International journal of molecular sciences"],"pubmed_title":["Anti-SOD1 Nanobodies That Stabilize Misfolded SOD1 Proteins Also Promote Neurite Outgrowth in Mutant SOD1 Human Neurons."],"pmcid":["PMC9784173"],"funding_grant_id":["R01 NS108769","R01 GM137529","UL1 TR001453","R01 NS067206","R21 NS120126","R01 GM147677","R01 NS101895","R01 NS118145"],"pubmed_authors":["Kulick D","Gadd DH","Douthwright C","Yusuf I","Kumar MS","Golebiowski D","Bosco DA","Fowler-Magaw ME","Boopathy S","Rotunno M","Sena-Esteves M","Brown RH","O'Neil AL","Xu Z"],"additional_accession":[]},"is_claimable":false,"name":"Anti-SOD1 Nanobodies That Stabilize Misfolded SOD1 Proteins Also Promote Neurite Outgrowth in Mutant SOD1 Human Neurons.","description":"ALS-linked mutations induce aberrant conformations within the SOD1 protein that are thought to underlie the pathogenic mechanism of SOD1-mediated ALS. Although clinical trials are underway for gene silencing of <i>SOD1</i>, these approaches reduce both wild-type and mutated forms of SOD1. Here, we sought to develop anti-SOD1 nanobodies with selectivity for mutant and misfolded forms of human SOD1 over wild-type SOD1. Characterization of two anti-SOD1 nanobodies revealed that these biologics stabilize mutant SOD1 in vitro. Further, SOD1 expression levels were enhanced and the physiological subcellular localization of mutant SOD1 was restored upon co-expression of anti-SOD1 nanobodies in immortalized cells. In human motor neurons harboring the <i>SOD1 A4V</i> mutation, anti-SOD1 nanobody exp","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-04T21:55:14.655Z","creation":"2025-04-04T21:55:14.655Z"},"accession":"S-EPMC9784173","cross_references":{"pubmed":["36555655"],"doi":["10.3390/ijms232416013"]}}