{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["17"],"submitter":["Romanowicz GE"],"pubmed_abstract":["Compromises to collagen and mineral lead to a decrease in whole bone quantity and quality in a variety of systemic diseases, yet, clinically, disease manifestations differ between craniofacial and long bones. Collagen alterations can occur through post-translational modification via lysyl oxidase (LOX), which catalyzes enzymatic collagen cross-link formation, as well as through non-enzymatic advanced glycation end products (AGEs) such as pentosidine and carboxymethyl-lysine (CML). Characterization of the cross-links and AGEs, and comparison of the mineral and collagen modifications in craniofacial and long bones represent a critical gap in knowledge. However, alterations to either the mineral or collagen in bone may contribute to disease progression and, subsequently, the anatomical site d"],"journal":["Bone reports"],"pagination":["101629"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9618783"],"repository":["biostudies-literature"],"pubmed_title":["Collagen cross-link profiles and mineral are different between the mandible and femur with site specific response to perturbed collagen."],"pmcid":["PMC9618783"],"pubmed_authors":["Lynch M","Kohn DH","Bielajew BJ","Terhune AH","Romanowicz GE","Mandair GS","Sexton B","McNerny EMB"],"additional_accession":[]},"is_claimable":false,"name":"Collagen cross-link profiles and mineral are different between the mandible and femur with site specific response to perturbed collagen.","description":"Compromises to collagen and mineral lead to a decrease in whole bone quantity and quality in a variety of systemic diseases, yet, clinically, disease manifestations differ between craniofacial and long bones. Collagen alterations can occur through post-translational modification via lysyl oxidase (LOX), which catalyzes enzymatic collagen cross-link formation, as well as through non-enzymatic advanced glycation end products (AGEs) such as pentosidine and carboxymethyl-lysine (CML). Characterization of the cross-links and AGEs, and comparison of the mineral and collagen modifications in craniofacial and long bones represent a critical gap in knowledge. However, alterations to either the mineral or collagen in bone may contribute to disease progression and, subsequently, the anatomical site d","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-05T13:27:30.992Z","creation":"2025-04-05T13:27:30.992Z"},"accession":"S-EPMC9618783","cross_references":{"pubmed":["36325166"],"doi":["10.1016/j.bonr.2022.101629"]}}