<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Soppina P</submitter><funding>Department of Science and Technology, Govt. of India</funding><funding>Department of Biotechnology, Ministry of Science and Technology, Govt. of India</funding><funding>Indian Council of Medical Research, Govt. of India</funding><funding>Science and Engineering Research Board, Department of Science and Technology, Government of India</funding><pagination>177</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9364601</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>20(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood.&lt;h4>Results&lt;/h4>We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-</pubmed_abstract><journal>BMC biology</journal><pubmed_title>Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.</pubmed_title><pmcid>PMC9364601</pmcid><funding_grant_id>SR/WOS-A/LS-73/2017</funding_grant_id><funding_grant_id>BT/PR15214/BRB/10/1449/2015</funding_grant_id><funding_grant_id>5/13/13/2019/NCD-III</funding_grant_id><funding_grant_id>ECR/2016/000913</funding_grant_id><funding_grant_id>BT/RLF/Re-entry/45/2015</funding_grant_id><pubmed_authors>Soppina V</pubmed_authors><pubmed_authors>Patel N</pubmed_authors><pubmed_authors>Naik PK</pubmed_authors><pubmed_authors>Soppina P</pubmed_authors><pubmed_authors>Sivaramakrishnan S</pubmed_authors><pubmed_authors>Rai A</pubmed_authors><pubmed_authors>Shewale DJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.</name><description>&lt;h4>Background&lt;/h4>Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood.&lt;h4>Results&lt;/h4>We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2025-04-04T22:35:54.284Z</modification><creation>2025-02-19T03:31:35.281Z</creation></dates><accession>S-EPMC9364601</accession><cross_references><pubmed>35948971</pubmed><doi>10.1186/s12915-022-01370-8</doi></cross_references></HashMap>