{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["286(9)"],"submitter":["Karpuj MV"],"pubmed_abstract":["We demonstrate that the levels of native as well as transfected prion protein (PrP) are lowered in various cell lines exposed to phosphorothioate oligodeoxynucleotides (PS-DNA) and can be rapidly reverted to their normal amounts by removal of PS-DNA. This transient modulation was independent of the glycosylation state of PrP, and in addition, all three PrP glycoforms were susceptible to PS-DNA treatment. Deletion of the N-terminal domain (amino acids 23-99), but not of the other domains of PrP, abrogated its PS-DNA-mediated down-regulation. PrP versions localized in the mitochondria, cytoplasm, or nucleus were not modulated by PS-DNA, indicating that PrP surface exposure is required for executing this effect. Proteins that in their native forms were not responsive to PS-DNA, such as thymoc"],"journal":["The Journal of biological chemistry"],"pagination":["6911-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3044946"],"repository":["biostudies-literature"],"pubmed_title":["Conditional modulation of membrane protein expression in cultured cells mediated by prion protein recognition of short phosphorothioate oligodeoxynucleotides."],"pmcid":["PMC3044946"],"pubmed_authors":["Schatzl HM","Karpuj MV","Tiran A","Rambold A","Gelibter-Niv S","Tatzelt J","Nunziante M"],"additional_accession":[]},"is_claimable":false,"name":"Conditional modulation of membrane protein expression in cultured cells mediated by prion protein recognition of short phosphorothioate oligodeoxynucleotides.","description":"We demonstrate that the levels of native as well as transfected prion protein (PrP) are lowered in various cell lines exposed to phosphorothioate oligodeoxynucleotides (PS-DNA) and can be rapidly reverted to their normal amounts by removal of PS-DNA. This transient modulation was independent of the glycosylation state of PrP, and in addition, all three PrP glycoforms were susceptible to PS-DNA treatment. Deletion of the N-terminal domain (amino acids 23-99), but not of the other domains of PrP, abrogated its PS-DNA-mediated down-regulation. PrP versions localized in the mitochondria, cytoplasm, or nucleus were not modulated by PS-DNA, indicating that PrP surface exposure is required for executing this effect. Proteins that in their native forms were not responsive to PS-DNA, such as thymoc","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Mar","modification":"2026-04-30T07:18:25.076Z","creation":"2026-04-07T15:53:25.476Z"},"accession":"S-EPMC3044946","cross_references":{"pubmed":["21156803"],"doi":["10.1074/jbc.m110.194662","10.1074/jbc.M110.194662"]}}