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 ResearchMeSH KeywordsAdenosine TriphosphateCryoelectron MicroscopyDyneinsMicrotubulesModels, MolecularTetrahymena thermophilaConceptsOuter arm dyneinMicrotubule doubletsDistinct microtubule-binding domainsHigh-resolution structuresAction of dyneinsMicrotubule-binding domainNative tracksATP hydrolysisDynein motorsHydrolyze ATPConformational changesNucleotide cycleMotor coordination mechanismATP turnoverDyneinHead interactionsMechanical forces
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