{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tendulkar S"],"funding":["Science and Engineering Board","NHGRI NIH HHS","Indian Institute of Science Education and Research","Agharkar Research Institute","Council for Scientific and Industrial Research","NIGMS NIH HHS","NIH HHS"],"pagination":["2857-2875"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9433731"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(17)"],"pubmed_abstract":["Amyotrophic lateral sclerosis (ALS) is a fatal, late-onset, progressive motor neurodegenerative disorder. A key pathological feature of the disease is the presence of heavily ubiquitinated protein inclusions. Both the unfolded protein response and the ubiquitin-proteasome system appear significantly impaired in patients and animal models of ALS. We have studied cellular and molecular mechanisms involved in ALS using a vesicle-associated membrane protein-associated protein B (VAPB/ALS8) Drosophila model [Moustaqim-Barrette, A., Lin, Y.Q., Pradhan, S., Neely, G.G., Bellen, H.J. and Tsuda, H. (2014) The ALS 8 protein, VAP, is required for ER protein quality control. Hum. Mol. Genet., 23, 1975-1989], which mimics many systemic aspects of the human disease. Here, we show that VAPB, located on t"],"journal":["Human molecular genetics"],"pubmed_title":["Caspar, an adapter for VAPB and TER94, modulates the progression of ALS8 by regulating IMD/NFκB-mediated glial inflammation in a Drosophila model of human disease."],"pmcid":["PMC9433731"],"funding_grant_id":["U41 HG000739","P40 OD010949","R01 GM084947","P40 OD018537"],"pubmed_authors":["Thulasidharan A","Tendulkar S","Ratnaparkhi A","Ratnaparkhi GS","Hegde S","Kaduskar B","Garg L"],"additional_accession":[]},"is_claimable":false,"name":"Caspar, an adapter for VAPB and TER94, modulates the progression of ALS8 by regulating IMD/NFκB-mediated glial inflammation in a Drosophila model of human disease.","description":"Amyotrophic lateral sclerosis (ALS) is a fatal, late-onset, progressive motor neurodegenerative disorder. A key pathological feature of the disease is the presence of heavily ubiquitinated protein inclusions. Both the unfolded protein response and the ubiquitin-proteasome system appear significantly impaired in patients and animal models of ALS. We have studied cellular and molecular mechanisms involved in ALS using a vesicle-associated membrane protein-associated protein B (VAPB/ALS8) Drosophila model [Moustaqim-Barrette, A., Lin, Y.Q., Pradhan, S., Neely, G.G., Bellen, H.J. and Tsuda, H. (2014) The ALS 8 protein, VAP, is required for ER protein quality control. Hum. Mol. Genet., 23, 1975-1989], which mimics many systemic aspects of the human disease. Here, we show that VAPB, located on t","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-04T21:35:17.37Z","creation":"2024-11-10T06:30:29.572Z"},"accession":"S-EPMC9433731","cross_references":{"pubmed":["35377453"],"doi":["10.1093/hmg/ddac076"]}}