Zhuan Qin
Associate Research ScientistCards
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Research
Publications
2025
Author Correction: 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. Author Correction: HIV-1 Env trimers asymmetrically engage CD4 receptors in membranes. Nature 2025, 639: e15-e15. PMID: 39994465, PMCID: PMC11903299, DOI: 10.1038/s41586-025-08802-9.Peer-Reviewed Original ResearchBPS2025 - Structure and inhibition of SARS-CoV-2 spike refolding in membranes
Mothes W, Grunst M, Qin Z, Dodero-Rojas E, Ding S, Prevost J, Chen Y, Hu Y, Pazgier M, Wu S, Xie X, Finzi A, Onuchic J, Whitford P, Li W. BPS2025 - Structure and inhibition of SARS-CoV-2 spike refolding in membranes. Biophysical Journal 2025, 124: 580a. DOI: 10.1016/j.bpj.2024.11.3011.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBetacoronavirusCell MembraneCOVID-19Cryoelectron MicroscopyElectron Microscope TomographyHumansMolecular Dynamics SimulationPeptidyl-Dipeptidase AProtein DomainsProtein MultimerizationProtein RefoldingSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationViral spike-receptor interactions monitored by cryo-electron tomograpy on membranes
Mothes W, Li W, Grunst M, Qin Z, Nand E. Viral spike-receptor interactions monitored by cryo-electron tomograpy on membranes. Biophysical Journal 2024, 123: 24a. DOI: 10.1016/j.bpj.2023.11.251.Peer-Reviewed Original Research
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 ResearchConceptsHIV-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 ResearchStructure of the native chemotaxis core signaling unit from phage E-protein lysed E. coli cells
Cassidy C, Qin Z, Frosio T, Gosink K, Yang Z, Sansom M, Stansfeld P, Parkinson J, Zhang P. Structure of the native chemotaxis core signaling unit from phage E-protein lysed E. coli cells. MBio 2023, 14: e00793-23. PMID: 37772839, PMCID: PMC10653900, DOI: 10.1128/mbio.00793-23.Peer-Reviewed Original ResearchConceptsCore signalling unitChemosensory arraysLyse E. coli cellsCryo-electron tomographyBacterial chemotaxisSignal transductionCell movementEscherichia coli</i>.Sensing machinerySensory signal transductionSignaling unitStructural basisMolecular mechanismsMechanistic hypothesesDesign new experimentsChemotaxisCellsComplete structurePhageMotilityTransductionMachineryUbiquitous behavior
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 ResearchConceptsChemosensory 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 ResearchConceptsPeriplasmic 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 Research
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