Qinhui Rao
Associate Research ScientistCards
About
Research
Publications
2023
Author Correction: Cryo-EM structure of an active central apparatus
Han L, Rao Q, Yang R, Wang Y, Chai P, Xiong Y, Zhang K. Author Correction: Cryo-EM structure of an active central apparatus. Nature Structural & Molecular Biology 2023, 30: 564-564. PMID: 36899097, PMCID: PMC10113143, DOI: 10.1038/s41594-023-00961-5.Peer-Reviewed Original ResearchHigh-Resolution Structural Analysis of Dyneins by Cryo-electron Microscopy
Chai P, Rao Q, Wang Y, Zhang K. High-Resolution Structural Analysis of Dyneins by Cryo-electron Microscopy. Methods In Molecular Biology 2023, 2623: 257-279. PMID: 36602691, PMCID: PMC10371436, DOI: 10.1007/978-1-0716-2958-1_16.ChaptersConceptsCryo-electron microscopyHigh-resolution structural informationLarge molecular machineHigh-resolution structuresCryo-EM approachResolution structural analysisProtein complexesStructural biologistsCellular cargoMolecular machinesDyneinDepth mechanistic understandingMolecular motorsMechanistic understandingCiliary motilityFlexible conformationIntricate architectureStructural informationMacromolecular structureForce generatorStructural analysisBiologistsSimilar structureCargoMicroscopy
2022
Multi-curve fitting and tubulin-lattice signal removal for structure determination of large microtubule-based motors
Chai P, Rao Q, Zhang K. Multi-curve fitting and tubulin-lattice signal removal for structure determination of large microtubule-based motors. Journal Of Structural Biology 2022, 214: 107897. PMID: 36089228, PMCID: PMC10321216, DOI: 10.1016/j.jsb.2022.107897.Peer-Reviewed Original ResearchCryo-EM structure of an active central apparatus
Han L, Rao Q, Yang R, Wang Y, Chai P, Xiong Y, Zhang K. Cryo-EM structure of an active central apparatus. Nature Structural & Molecular Biology 2022, 29: 472-482. PMID: 35578022, PMCID: PMC9113940, DOI: 10.1038/s41594-022-00769-9.Peer-Reviewed Original ResearchConceptsCentral apparatusDiverse cellular activitiesKinesin-like proteinCryo-EM structureArmadillo repeat proteinsCryo-electron microscopyHigh-resolution structuresEukaryotic speciesProtein subunitsMotile ciliaBridge proteinsPair of microtubulesRegulatory roleCellular activitiesProteinDynamic conformational behaviorCiliary motilityCiliaCiliary beatingStructural frameworkConformational behaviorSubunitsMicrotubulesRegulatorSpecies
2021
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism
Rao Q, Han L, Wang Y, Chai P, Kuo YW, Yang R, Hu F, Yang Y, Howard J, Zhang K. Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism. Nature Structural & Molecular Biology 2021, 28: 799-810. PMID: 34556869, PMCID: PMC8500839, DOI: 10.1038/s41594-021-00656-9.Peer-Reviewed Original ResearchConceptsOuter arm dyneinMicrotubule doubletsDistinct microtubule-binding domainsHigh-resolution structuresAction of dyneinsMicrotubule-binding domainNative tracksATP hydrolysisDynein motorsHydrolyze ATPConformational changesNucleotide cycleMotor coordination mechanismATP turnoverDyneinHead interactionsMechanical forcesThe activation mechanisms of master kinases in the DNA damage response
Xiao J, Rao Q, Xu Y. The activation mechanisms of master kinases in the DNA damage response. Genome Instability & Disease 2021, 2: 211-224. DOI: 10.1007/s42764-021-00045-y.Peer-Reviewed Original ResearchDNA damage responsePIKK regulatory domainDNA-PKDamage responseMultiple DNA repair pathwaysDNA damageStructures of ATMCryo-electron microscopyDNA repair pathwaysSeries of proteinsKinase structureMaster kinaseRegulatory domainRepair pathwaysGenetic informationCritical kinaseMolecular mechanismsSophisticated mechanismsExtrinsic stimuliActivation mechanismKinaseCritical roleATRPathwayEukaryotesCryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination
Rao Q, Wang Y, Chai P, Kuo Y, Han L, Yang R, Yang Y, Howard J, Zhang K. Cryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.03099.Peer-Reviewed Original ResearchOuter arm dyneinMicrotubule-bound stateInner arm dyneinsCentral pair complexMicrotubule-binding domainMicrotubule doubletsIntermediate chainATP hydrolysisFundamental cellular processesHeavy chainCryo-EM structureCryo-EM analysisCryo-electron tomographyKey motor proteinCryo-electron microscopyLight chainCellular processesEukaryotic ciliaT. thermophilaEmbryonic developmentAdjacent microtubule doubletsCellular motilityMotor proteinsAxonemal dyneinsMotile cilia
2017
Cryo-EM structure of human ATR-ATRIP complex
Rao Q, Liu M, Tian Y, Wu Z, Hao Y, Song L, Qin Z, Ding C, Wang H, Wang J, Xu Y. Cryo-EM structure of human ATR-ATRIP complex. Cell Research 2017, 28: 143-156. PMID: 29271416, PMCID: PMC5799817, DOI: 10.1038/cr.2017.158.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAtaxia Telangiectasia Mutated ProteinsCarrier ProteinsChromatography, AffinityChromatography, GelCryoelectron MicroscopyDNA DamageDNA-Binding ProteinsHumansIsoxazolesMutationNuclear ProteinsPhosphorylationProtein BindingProtein Conformation, alpha-HelicalProtein FoldingProtein KinasesProtein MultimerizationPyrazinesSignal TransductionTOR Serine-Threonine KinasesConceptsATR-ATRIP complexCryo-electron microscopy structureATR protein kinasesTerminal catalytic coreCryo-EM structureDNA repair pathwaysMicroscopy structureReplication stressFunctional diversityProtein kinaseCatalytic coreRepair pathwaysStructural basisN-terminusATRIPCatalytic pocketEM mapsDistinct conformationsDNA damageConformational flexibilityInhibitory elementsATRComplex formationCritical roleComplexes
2015
Structural insight into substrate preference for TET-mediated oxidation
Hu L, Lu J, Cheng J, Rao Q, Li Z, Hou H, Lou Z, Zhang L, Li W, Gong W, Liu M, Sun C, Yin X, Li J, Tan X, Wang P, Wang Y, Fang D, Cui Q, Yang P, He C, Jiang H, Luo C, Xu Y. Structural insight into substrate preference for TET-mediated oxidation. Nature 2015, 527: 118-122. PMID: 26524525, DOI: 10.1038/nature15713.Peer-Reviewed Original Research
2013
Crystal Structure of TET2-DNA Complex: Insight into TET-Mediated 5mC Oxidation
Hu L, Li Z, Cheng J, Rao Q, Gong W, Liu M, Shi Y, Zhu J, Wang P, Xu Y. Crystal Structure of TET2-DNA Complex: Insight into TET-Mediated 5mC Oxidation. Cell 2013, 155: 1545-1555. PMID: 24315485, DOI: 10.1016/j.cell.2013.11.020.Peer-Reviewed Original ResearchConceptsCatalytic cavityCys-rich domainMutations of TET2CpG contextTET proteinsHuman TET2Zinc fingerCatalytic domainSubstrate preferenceÅ resolutionStructural basisCpG dinucleotideBiological processesMyeloid malignancesHuman cancersDNATET2MutationsCrystal structureMethyl groupTetImportant roleDomainProteinResidues