2018
High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing
Mentes A, Huehn A, Liu X, Zwolak A, Dominguez R, Shuman H, Ostap EM, Sindelar CV. High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 1292-1297. PMID: 29358376, PMCID: PMC5819444, DOI: 10.1073/pnas.1718316115.Peer-Reviewed Original ResearchConceptsN-terminal subdomainHigh-resolution cryo-EM structuresADP stateNear-atomic resolution structuresCryo-EM structureCryo-electron microscopyHigh-resolution structuresIsoform-dependent mannerFilamentous actinResolution structureStructural basisMyosin IBActin filamentsStructural diversityRelease pathwayADP releaseActinPointed endPotent stabilizerMyosin
2014
High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation
Shang Z, Zhou K, Xu C, Csencsits R, Cochran JC, Sindelar CV. High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation. ELife 2014, 3: e04686. PMID: 25415053, PMCID: PMC4383081, DOI: 10.7554/elife.04686.Peer-Reviewed Original Research
2007
The beginning of kinesin's force-generating cycle visualized at 9-Å resolution
Sindelar CV, Downing KH. The beginning of kinesin's force-generating cycle visualized at 9-Å resolution. Journal Of Cell Biology 2007, 177: 377-385. PMID: 17470637, PMCID: PMC2064809, DOI: 10.1083/jcb.200612090.Peer-Reviewed Original ResearchConceptsSwitch II helixMicrotubule-binding proteinN-terminal extensionII helixNucleotide-free stateCryo-electron microscopySwitch IMicrotubule contactsResponse elementSingle-particle reconstructionConformational changesMicrotubulesActivation mechanismKinesinHigh-resolution characterizationHelixProtein