{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kollar V"],"funding":["Hungarian Science Foundation"],"pagination":["838530"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2857871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2010"],"pubmed_abstract":["Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end of the molecule, has been thought to be a hot spot for mechanosensing while also serving as anchorage for its sarcomeric attachment. Understanding the mechanics of titin's Z-disk region, particularly under the effect of binding proteins, is of great interest. Here we briefly review recent findings on the structure, molecular associations, and mechanics of titin's Z-disk region. In addition, we report experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical"],"journal":["Journal of biomedicine & biotechnology"],"pubmed_title":["Dynamic strength of titin's Z-disk end."],"pmcid":["PMC2857871"],"funding_grant_id":["K73256","KFKT-1-2006-0021","F49514","OMFB-380/2006"],"pubmed_authors":["Szatmari D","Grama L","Kollar V","Kellermayer MS"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic strength of titin's Z-disk end.","description":"Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end of the molecule, has been thought to be a hot spot for mechanosensing while also serving as anchorage for its sarcomeric attachment. Understanding the mechanics of titin's Z-disk region, particularly under the effect of binding proteins, is of great interest. Here we briefly review recent findings on the structure, molecular associations, and mechanics of titin's Z-disk region. In addition, we report experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010","modification":"2025-06-01T11:59:38.5Z","creation":"2019-03-27T00:30:16Z"},"accession":"S-EPMC2857871","cross_references":{"pubmed":["20414364"],"doi":["10.1155/2010/838530"]}}