<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>45</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>9(1)</volume><submitter>Guo SK</submitter><pubmed_abstract>Kinesin-3 and kinesin-1 molecular motors are two families of the kinesin superfamily. It has been experimentally revealed that in monomeric state kinesin-3 is inactive in motility and cargo-mediated dimerization results in superprocessive motion, with an average run length being more than 10-fold longer than that of kinesin-1. In contrast to kinesin-1 showing normally single-exponential distribution of run lengths, dimerized kinesin-3 shows puzzlingly Gaussian distribution of run lengths. Here, based on our proposed model, we studied computationally the dynamics of kinesin-3 and compared with that of kinesin-1, explaining quantitatively the available experimental data and revealing the origin of superprocessivity and Gaussian run length distribution of kinesin-3. Moreover, predicted results are provided on ATP-concentration dependence of run length distribution and force dependence of mean run length and dissociation rate of kinesin-3.</pubmed_abstract><journal>Scientific reports</journal><pagination>16973</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6861319</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Run length distribution of dimerized kinesin-3 molecular motors: comparison with dimeric kinesin-1.</pubmed_title><pmcid>PMC6861319</pmcid><pubmed_authors>Shi XX</pubmed_authors><pubmed_authors>Wang PY</pubmed_authors><pubmed_authors>Guo SK</pubmed_authors><pubmed_authors>Xie P</pubmed_authors><view_count>45</view_count></additional><is_claimable>false</is_claimable><name>Run length distribution of dimerized kinesin-3 molecular motors: comparison with dimeric kinesin-1.</name><description>Kinesin-3 and kinesin-1 molecular motors are two families of the kinesin superfamily. It has been experimentally revealed that in monomeric state kinesin-3 is inactive in motility and cargo-mediated dimerization results in superprocessive motion, with an average run length being more than 10-fold longer than that of kinesin-1. In contrast to kinesin-1 showing normally single-exponential distribution of run lengths, dimerized kinesin-3 shows puzzlingly Gaussian distribution of run lengths. Here, based on our proposed model, we studied computationally the dynamics of kinesin-3 and compared with that of kinesin-1, explaining quantitatively the available experimental data and revealing the origin of superprocessivity and Gaussian run length distribution of kinesin-3. Moreover, predicted results are provided on ATP-concentration dependence of run length distribution and force dependence of mean run length and dissociation rate of kinesin-3.</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Nov</publication><modification>2021-02-20T23:58:20Z</modification><creation>2020-05-21T19:15:51Z</creation></dates><accession>S-EPMC6861319</accession><cross_references><pubmed>31740721</pubmed><doi>10.1038/s41598-019-53550-2</doi></cross_references></HashMap>