<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>17</volume><submitter>Romanowicz GE</submitter><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</pubmed_abstract><journal>Bone reports</journal><pagination>101629</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9618783</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Collagen cross-link profiles and mineral are different between the mandible and femur with site specific response to perturbed collagen.</pubmed_title><pmcid>PMC9618783</pmcid><pubmed_authors>Lynch M</pubmed_authors><pubmed_authors>Kohn DH</pubmed_authors><pubmed_authors>Bielajew BJ</pubmed_authors><pubmed_authors>Terhune AH</pubmed_authors><pubmed_authors>Romanowicz GE</pubmed_authors><pubmed_authors>Mandair GS</pubmed_authors><pubmed_authors>Sexton B</pubmed_authors><pubmed_authors>McNerny EMB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Collagen cross-link profiles and mineral are different between the mandible and femur with site specific response to perturbed collagen.</name><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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-05T13:27:30.992Z</modification><creation>2025-04-05T13:27:30.992Z</creation></dates><accession>S-EPMC9618783</accession><cross_references><pubmed>36325166</pubmed><doi>10.1016/j.bonr.2022.101629</doi></cross_references></HashMap>