<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kollar V</submitter><funding>Hungarian Science Foundation</funding><pagination>838530</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2857871</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2010</volume><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</pubmed_abstract><journal>Journal of biomedicine &amp; biotechnology</journal><pubmed_title>Dynamic strength of titin's Z-disk end.</pubmed_title><pmcid>PMC2857871</pmcid><funding_grant_id>K73256</funding_grant_id><funding_grant_id>KFKT-1-2006-0021</funding_grant_id><funding_grant_id>F49514</funding_grant_id><funding_grant_id>OMFB-380/2006</funding_grant_id><pubmed_authors>Szatmari D</pubmed_authors><pubmed_authors>Grama L</pubmed_authors><pubmed_authors>Kollar V</pubmed_authors><pubmed_authors>Kellermayer MS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Dynamic strength of titin's Z-disk end.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010</publication><modification>2025-06-01T11:59:38.5Z</modification><creation>2019-03-27T00:30:16Z</creation></dates><accession>S-EPMC2857871</accession><cross_references><pubmed>20414364</pubmed><doi>10.1155/2010/838530</doi></cross_references></HashMap>