2018
Structural basis of the filamin A actin-binding domain interaction with F-actin
Iwamoto DV, Huehn A, Simon B, Huet-Calderwood C, Baldassarre M, Sindelar CV, Calderwood DA. Structural basis of the filamin A actin-binding domain interaction with F-actin. Nature Structural & Molecular Biology 2018, 25: 918-927. PMID: 30224736, PMCID: PMC6173970, DOI: 10.1038/s41594-018-0128-3.Peer-Reviewed Original ResearchMeSH KeywordsActinsCryoelectron MicroscopyFilaminsHumansModels, MolecularMutation, MissenseProtein DomainsConceptsActin-binding domainCalponin homology domainHomology domainF-actinActin cross-linking proteinFunction mutationsTandem calponin homology domainsDisease-associated mutantsCryo-electron microscopyHigh-resolution structuresNumerous genetic diseasesSequence conservationHigher-order structureLinking proteinStructural basisDomain interactionsCell shapeActin filamentsMolecular understandingN-terminalFunctional studiesGenetic diseasesMissense mutationsMutationsAtomic resolutionHigh-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
Site-specific cation release drives actin filament severing by vertebrate cofilin
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17821-17826. PMID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.Peer-Reviewed Original ResearchConceptsFilament severingActin filamentsActin filament severingKey regulatory functionsConcentration of endsActin filament fragmentationEukaryotic cellsCation-binding sitesProtein cofilinDeletion mutantsS. cerevisiaeSubunit exchangeFilament turnoverActin polymerizationEssential functionsSite-specific interactionsCofilinMolecular mechanismsAssembly dynamicsRegulatory functionsActin moleculesFilament fragmentationFilament structureSustained motilitySeveringHigh-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
2012
Optimal noise reduction in 3D reconstructions of single particles using a volume-normalized filter
Sindelar CV, Grigorieff N. Optimal noise reduction in 3D reconstructions of single particles using a volume-normalized filter. Journal Of Structural Biology 2012, 180: 26-38. PMID: 22613568, PMCID: PMC3498508, DOI: 10.1016/j.jsb.2012.05.005.Peer-Reviewed Original ResearchConceptsParticle mapsOptimal noise reductionWiener filterError reduction schemeConventional Wiener filterNoise reductionNovel filterInversion methodNew filterHigh noise levelsParticle densityParticle volumeFilterParticlesNoise ratioNoise levelTheoretical analysisSingle particleAccurate implementationSpectral signalsSSNRInterior regionImage dataSignalsFourier inversion method
2011
An adaptation of the Wiener filter suitable for analyzing images of isolated single particles
Sindelar CV, Grigorieff N. An adaptation of the Wiener filter suitable for analyzing images of isolated single particles. Journal Of Structural Biology 2011, 176: 60-74. PMID: 21757012, PMCID: PMC3184790, DOI: 10.1016/j.jsb.2011.06.010.Peer-Reviewed Original ResearchConceptsWiener filterConventional Wiener filterCryo-EM applicationsNew filterFourier ring correlationParticle areaEstimation schemeFilterLeast-squares senseEstimation methodNoise ratioSpecific applicationsSingle particleParticlesImage fieldError reductionNumeric testsApplicationsImaging conditionsSimulated dataInput data
2010
An atomic-level mechanism for activation of the kinesin molecular motors
Sindelar CV, Downing KH. An atomic-level mechanism for activation of the kinesin molecular motors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 4111-4116. PMID: 20160108, PMCID: PMC2840164, DOI: 10.1073/pnas.0911208107.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
1998
Effects of salt bridges on protein structure and design
Sindelar C, Hendsch Z, Tidor B. Effects of salt bridges on protein structure and design. Protein Science 1998, 7: 1898-1914. PMID: 9761471, PMCID: PMC2144171, DOI: 10.1002/pro.5560070906.Peer-Reviewed Original ResearchMeSH KeywordsModels, MolecularMolecular Sequence DataMutationProtein ConformationProteinsSaltsStatic Electricity