Zhuan Qin
Associate Research ScientistCards
Appointments
Microbial Pathogenesis
Primary
Contact Info
About
Titles
Associate Research Scientist
Appointments
Microbial Pathogenesis
Associate Research ScientistPrimary
Other Departments & Organizations
- Microbial Pathogenesis
- Mothes Lab
Research
Research at a Glance
Yale Co-Authors
Frequent collaborators of Zhuan Qin's published research.
Publications Timeline
A big-picture view of Zhuan Qin's research output by year.
Jun Liu, PhD
Walther Mothes, PhD
Wenwei Li
María Lara-Tejero, DVM, PhD
Pradeep Uchil, PhD
10Publications
198Citations
Publications
2024
Structure and inhibition of SARS-CoV-2 spike refolding in membranes
Grunst M, Qin Z, Dodero-Rojas E, Ding S, Prévost J, Chen Y, Hu Y, Pazgier M, Wu S, Xie X, Finzi A, Onuchic J, Whitford P, Mothes W, Li W. Structure and inhibition of SARS-CoV-2 spike refolding in membranes. Science 2024, 385: 757-765. PMID: 39146425, PMCID: PMC11449073, DOI: 10.1126/science.adn5658.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBetacoronavirusCell MembraneCOVID-19Cryoelectron MicroscopyElectron Microscope TomographyHumansMolecular Dynamics SimulationPeptidyl-Dipeptidase AProtein DomainsProtein MultimerizationProtein RefoldingSARS-CoV-2Spike Glycoprotein, CoronavirusVirus Internalization
2023
HIV-1 Env trimers asymmetrically engage CD4 receptors in membranes
Li W, Qin Z, Nand E, Grunst M, Grover J, Bess J, Lifson J, Zwick M, Tagare H, Uchil P, Mothes W. HIV-1 Env trimers asymmetrically engage CD4 receptors in membranes. Nature 2023, 623: 1026-1033. PMID: 37993716, PMCID: PMC10686830, DOI: 10.1038/s41586-023-06762-6.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsHIV-1 Env trimersCD4 moleculeHuman immunodeficiency virus-1 (HIV-1) infectionEnv trimersAntibody-mediated immune responsesEnv-CD4 interactionVirus-1 infectionVaccine immunogen designViral envelope glycoproteinsHIV-1Immune responseCD4 receptorImmunogen designEnvelope glycoproteinVirus-like particlesCD4EnvHost cell membraneStructure of the native chemotaxis core signaling unit from phage E-protein lysed E. coli cells.
Cassidy CK, Qin Z, Frosio T, Gosink K, Yang Z, Sansom MSP, Stansfeld PJ, Parkinson JS, Zhang P. Structure of the native chemotaxis core signaling unit from phage E-protein lysed E. coli cells. MBio 2023, 14: e0079323. PMID: 37772839, DOI: 10.1128/mbio.00793-23.Peer-Reviewed Original Research
2021
Studying bacterial chemosensory array with CryoEM
Qin Z, Zhang P. Studying bacterial chemosensory array with CryoEM. Biochemical Society Transactions 2021, 49: 2081-2089. PMID: 34495335, PMCID: PMC8589424, DOI: 10.1042/bst20210080.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsChemosensory arraysBacterial chemosensory arrayThousands of proteinsGradients of nutrientsCell polesLipid nanodiscsChemosensory systemCryoEMBacterial minicellsStructural studiesBacteria cellsBacterial ghostsRecent advancesMinicellsStructural analysisNanodiscsProteinBacteriaNutrientsCellsVivo
2019
Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi
Zhang K, Qin Z, Chang Y, Liu J, Malkowski MG, Shipa S, Li L, Qiu W, Zhang J, Li C. Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi. Molecular Microbiology 2019, 111: 1652-1670. PMID: 30883947, PMCID: PMC6561814, DOI: 10.1111/mmi.14243.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPeriplasmic flagellaFliD mutantFlagellin proteinMajor flagellin proteinLyme disease spirochete Borrelia burgdorferiFlagellar cap proteinFlagellar cap protein FliDFlagellar filament assemblyFlagella-deficient mutantsMutant cellsCAP mutantsFlaB proteinsPeriplasmFilament assemblyCap proteinB. burgdorferiFlagellar filamentsGenetic studiesMutantsBorrelia burgdorferiHtrASerine proteasesFliDFlagellin polymerizationSpirochete Borrelia burgdorferiRole of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system
Lara-Tejero M, Qin Z, Hu B, Butan C, Liu J, Galán JE. Role of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system. PLOS Pathogens 2019, 15: e1007565. PMID: 30668610, PMCID: PMC6358110, DOI: 10.1371/journal.ppat.1007565.Peer-Reviewed Original ResearchCitationsAltmetric
2018
Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex
Qin Z, Tu J, Lin T, Norris SJ, Li C, Motaleb MA, Liu J. Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex. PLOS Biology 2018, 16: e3000050. PMID: 30412577, PMCID: PMC6248999, DOI: 10.1371/journal.pbio.3000050.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCryo-electron tomographyPeriplasmic flagellaATPase complexFlagellar C-ringType III secretion systemCytoplasmic ATPase complexLyme disease spirochete Borrelia burgdorferiMotility of spirochetesExport apparatusSecretion systemStructural insightsBorrelia burgdorferiFlagellaSpirochete Borrelia burgdorferiPathogenic spirochetesC-ringNovel therapeutic strategiesUnique mechanismDistinct morphologiesB. burgdorferiComplexesMultiple spokesAssemblyTherapeutic strategiesBurgdorferiVisualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis
Qin Z, Hu B, Liu J. Visualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis. Methods In Molecular Biology 2018, 1729: 187-199. PMID: 29429093, DOI: 10.1007/978-1-4939-7577-8_17.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsCryo-electron tomographyChemoreceptor arraysCheW coupling proteinLarge macromolecular assembliesChemotaxis arraysSubtomogram analysisCheA kinaseBacterial chemoreceptorsCellular contextCoupling proteinMacromolecular assembliesChemotaxis signalingMolecular levelSitu structurePrecise architectureBacterial minicellsMinicellsUnique toolKinaseSignalingProteinSubtomogramsAssemblyConcertAmplification
2017
In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography
Zhu S, Qin Z, Wang J, Morado DR, Liu J. In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography. Methods In Molecular Biology 2017, 1593: 229-242. PMID: 28389958, DOI: 10.1007/978-1-4939-6927-2_18.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsCryo-electron tomographyFlagellar motorIntact flagellar motorBacterial flagellar motorMolecular machinerySitu structural analysisExtensive structural analysisMolecular machinesLarge complexesStructural analysisUnprecedented detailBorrelia burgdorferiStructural determinationMachineryOrganismsBacteriaPowerful techniqueCellsComplexesBurgdorferi
2016
Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography
Qin Z, Lin WT, Zhu S, Franco AT, Liu J. Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography. Journal Of Bacteriology 2016, 199: 10.1128/jb.00695-16. PMID: 27849173, PMCID: PMC5237115, DOI: 10.1128/jb.00695-16.Peer-Reviewed Original ResearchCitationsAltmetricConceptsCryo-electron tomographyChemotaxis arraysUnipolar flagellaBacterial pathogensFlagella-driven motilityMultiple unipolar flagellaNovel structural insightsFlagellar assemblyChemotaxis machineryFlagellar poleAssembly intermediatesFlagellar rotationFlagellar motorCell envelopeStructural insightsMembrane sheathSheathed flagellumMolecular mechanismsUnique motilityH. pylori cellsFlagellaSitu structureHigh-viscosity environmentsPylori cellsMotility
Get In Touch
Contacts
Email