2023
An integrated platform for high-throughput nanoscopy
Barentine A, Lin Y, Courvan E, Kidd P, Liu M, Balduf L, Phan T, Rivera-Molina F, Grace M, Marin Z, Lessard M, Rios Chen J, Wang S, Neugebauer K, Bewersdorf J, Baddeley D. An integrated platform for high-throughput nanoscopy. Nature Biotechnology 2023, 41: 1549-1556. PMID: 36914886, PMCID: PMC10497732, DOI: 10.1038/s41587-023-01702-1.Peer-Reviewed Original ResearchConceptsLarge data volumesUser-defined extensionsPlugin frameworkData compressionData volumeCamera frameFrame rateAnalysis platformAcquisition taskPlatformIntegrated acquisitionThroughputSingle-molecule localization microscopyTypical throughputHundreds of cellsThree-dimensional fluorescenceFrameworkTens of cellsLocalization microscopyWorkflow
2016
Spatial organization shapes the turnover of a bacterial transcriptome
Moffitt JR, Pandey S, Boettiger AN, Wang S, Zhuang X. Spatial organization shapes the turnover of a bacterial transcriptome. ELife 2016, 5: e13065. PMID: 27198188, PMCID: PMC4874777, DOI: 10.7554/elife.13065.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliMicroscopy, FluorescenceRNA Processing, Post-TranscriptionalSequence Analysis, RNASpatial AnalysisTranscriptomeConceptsBacterial transcriptomesSpatial organizationE. coli transcriptomeCo-translational insertionInner membrane proteinProtein mRNASignal recognition particlePost-transcriptional fatePost-transcriptional regulationSuper-resolution microscopyRNA degradosomePeriplasmic proteinsSignal peptideRNA sequencingTranscriptomeMembrane enrichmentSelective destabilizationMRNARNAProteinDegradosomeEukaryotesMembraneProkaryotesPowerful means
2014
Characterization and development of photoactivatable fluorescent proteins for single-molecule–based superresolution imaging
Wang S, Moffitt JR, Dempsey GT, Xie XS, Zhuang X. Characterization and development of photoactivatable fluorescent proteins for single-molecule–based superresolution imaging. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 8452-8457. PMID: 24912163, PMCID: PMC4060684, DOI: 10.1073/pnas.1406593111.Peer-Reviewed Original ResearchAnimalsBacterial ProteinsBlotting, WesternCell Line, TumorChlorocebus aethiopsCOS CellsDNA-Binding ProteinsEscherichia coli ProteinsHumansLuminescent ProteinsMicroscopy, FluorescencePhotonsProtein MultimerizationReceptors, Cell SurfaceRecombinant Fusion ProteinsSpectrometry, FluorescenceVimentinZyxin
2011
The bacterial actin MreB rotates, and rotation depends on cell-wall assembly
van Teeffelen S, Wang S, Furchtgott L, Huang KC, Wingreen NS, Shaevitz JW, Gitai Z. The bacterial actin MreB rotates, and rotation depends on cell-wall assembly. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 15822-15827. PMID: 21903929, PMCID: PMC3179079, DOI: 10.1073/pnas.1108999108.Peer-Reviewed Original ResearchConceptsCytoskeletal proteinsRod-like cell shapeCell wall synthesis machineryActin homolog MreBPeptidoglycan cell wallCell wall assemblyMultiple cytoskeletal proteinsMreB dynamicsBacterial morphogenesisCytoskeletal dynamicsSynthesis machineryCellular functionsCellular processesMotor proteinsCell shapeCell wallCytoskeletal motorsBacterial cellsMreBPersistent mannerProteinInsertion siteBiophysical simulationsBacteriaRod shape