{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Montgomery NT"],"funding":["Shriners Hospitals for Children"],"pagination":["5987-5999"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5912474"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(16)"],"pubmed_abstract":["Type IV collagen is a major component of the basement membrane and interacts with numerous other basement membrane proteins. Many of these interactions are poorly characterized. Type IV collagen is abundantly post-translationally modified with 3-hydroxyproline (3-Hyp), but 3-Hyp's biochemical role in type IV collagen's interactions with other proteins is not well established. In this work, we present binding data consistent with a major role of 3-Hyp in interactions of collagen IV with glycoprotein VI and nidogens 1 and 2. The increased binding interaction between type IV collagen without 3-Hyp and glycoprotein VI has been the subject of some controversy, which we sought to explore, whereas the lack of binding of nidogens to type IV collagen without 3-Hyp is novel. Using tandem MS, we show"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2."],"pmcid":["PMC5912474"],"funding_grant_id":["85500","85100"],"pubmed_authors":["Montgomery NT","Pokidysheva EN","Bachinger HP","Zientek KD"],"additional_accession":[]},"is_claimable":false,"name":"Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2.","description":"Type IV collagen is a major component of the basement membrane and interacts with numerous other basement membrane proteins. Many of these interactions are poorly characterized. Type IV collagen is abundantly post-translationally modified with 3-hydroxyproline (3-Hyp), but 3-Hyp's biochemical role in type IV collagen's interactions with other proteins is not well established. In this work, we present binding data consistent with a major role of 3-Hyp in interactions of collagen IV with glycoprotein VI and nidogens 1 and 2. The increased binding interaction between type IV collagen without 3-Hyp and glycoprotein VI has been the subject of some controversy, which we sought to explore, whereas the lack of binding of nidogens to type IV collagen without 3-Hyp is novel. Using tandem MS, we show","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2025-04-05T16:05:01.733Z","creation":"2019-06-06T19:23:06Z"},"accession":"S-EPMC5912474","cross_references":{"pubmed":["29491144"],"doi":["10.1074/jbc.RA117.000406","10.1074/jbc.ra117.000406"]}}