<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chowdhury AS</submitter><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>572-577</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10586751</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2022</volume><pubmed_abstract>Collagen α1(XI) is a minor fibrillar collagen involved in the critical regulation of collagen fibrils such as nucleation, assembly, and regulation of fibril diameter. The amino propeptide domain of the collagen α1(XI) is retained on the surface of the collagen fibril for an extended period of time and may play a crucial role in the interaction with extracellular matrix glycosaminoglycans and other proteins during the process of fibrillogenesis. Understanding the mechanism of action of this protein will ultimately help us understand the organization and assembly of the extracellular matrix that underlies the structural integrity of connective tissues.</pubmed_abstract><journal>Proceedings. International Conference on Computational Science and Computational Intelligence</journal><pubmed_title>Collagen a1(XI) structure prediction by Alphafold 2.</pubmed_title><pmcid>PMC10586751</pmcid><funding_grant_id>P20 GM109095</funding_grant_id><funding_grant_id>P20 GM103408</funding_grant_id><pubmed_authors>Oxford JT</pubmed_authors><pubmed_authors>Chowdhury AS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Collagen a1(XI) structure prediction by Alphafold 2.</name><description>Collagen α1(XI) is a minor fibrillar collagen involved in the critical regulation of collagen fibrils such as nucleation, assembly, and regulation of fibril diameter. The amino propeptide domain of the collagen α1(XI) is retained on the surface of the collagen fibril for an extended period of time and may play a crucial role in the interaction with extracellular matrix glycosaminoglycans and other proteins during the process of fibrillogenesis. Understanding the mechanism of action of this protein will ultimately help us understand the organization and assembly of the extracellular matrix that underlies the structural integrity of connective tissues.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-04T07:25:31.499Z</modification><creation>2025-04-04T07:25:31.499Z</creation></dates><accession>S-EPMC10586751</accession><cross_references><pubmed>37860747</pubmed><doi>10.1109/csci58124.2022.00108</doi></cross_references></HashMap>