{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Linsenmeier L"],"funding":["Werner-Otto-Stiftung","Deutsche Forschungsgemeinschaft","Creutzfeldt-Jakob Disease Foundation, Inc."],"pagination":["18"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5889536"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["<h4>Background</h4>Proteolytic processing of the prion protein (PrP<superscript>C</superscript>) by endogenous proteases generates bioactive membrane-bound and soluble fragments which may help to explain the pleiotropic roles of this protein in the nervous system and in brain diseases. Shedding of almost full-length PrP<superscript>C</superscript> into the extracellular space by the metalloprotease ADAM10 is of peculiar relevance since soluble PrP stimulates axonal outgrowth and is protective in neurodegenerative conditions such as Alzheimer’s and prion disease. However, molecular determinates and mechanisms regulating the shedding of PrP are entirely unknown.<h4>Methods</h4>We produced an antibody recognizing the neo-epitope of shed PrP generated by ADAM10 in biological samples and used i"],"journal":["Molecular neurodegeneration"],"pubmed_title":["Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein."],"pmcid":["PMC5889536"],"funding_grant_id":["SFB877 project A3","SFB877 project A12"],"pubmed_authors":["Puig B","Linsenmeier L","Mohammadi B","Altmeppen HC","Hartmann A","Endres K","Jackson WS","Saftig P","Tatzelt J","Uchiyama K","Sakaguchi S","Glatzel M","Wetzel S"],"additional_accession":[]},"is_claimable":false,"name":"Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.","description":"<h4>Background</h4>Proteolytic processing of the prion protein (PrP<superscript>C</superscript>) by endogenous proteases generates bioactive membrane-bound and soluble fragments which may help to explain the pleiotropic roles of this protein in the nervous system and in brain diseases. Shedding of almost full-length PrP<superscript>C</superscript> into the extracellular space by the metalloprotease ADAM10 is of peculiar relevance since soluble PrP stimulates axonal outgrowth and is protective in neurodegenerative conditions such as Alzheimer’s and prion disease. However, molecular determinates and mechanisms regulating the shedding of PrP are entirely unknown.<h4>Methods</h4>We produced an antibody recognizing the neo-epitope of shed PrP generated by ADAM10 in biological samples and used i","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2025-04-26T18:13:35.259Z","creation":"2019-03-26T23:29:20Z"},"accession":"S-EPMC5889536","cross_references":{"pubmed":["29625583"],"doi":["10.1186/s13024-018-0248-6"]}}