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http://purl.uniprot.org/citations/27119146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27119146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27119146http://www.w3.org/2000/01/rdf-schema#comment"Collagen is a major component of the extracellular matrix and its integrity is essential for connective tissue and organ function. The importance of proteins involved in intracellular collagen post-translational modification, folding and transport was recently highlighted from studies on recessive forms of osteogenesis imperfecta (OI). Here we describe the critical role of SC65 (Synaptonemal Complex 65, P3H4), a leprecan-family member, as part of an endoplasmic reticulum (ER) complex with prolyl 3-hydroxylase 3. This complex affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility. This is the first indication of a prolyl-hydroxylase complex in the ER controlling lysyl-hydroxylase activity during collagen synthesis."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1006002"xsd:string
http://purl.uniprot.org/citations/27119146http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1006002"xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Tackett A.J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Tackett A.J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Weis M."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Weis M."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Rai J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Rai J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Morello R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Morello R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Mackintosh S.G."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Mackintosh S.G."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Eyre D.R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Eyre D.R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Suva L.J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Suva L.J."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Hudson D.M."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Hudson D.M."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Besio R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Besio R."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Burdine M.S."xsd:string
http://purl.uniprot.org/citations/27119146http://purl.uniprot.org/core/author"Burdine M.S."xsd:string