2022
Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis
An S, Anneken A, Xi Z, Choi C, Schlessinger J, Toomre D. Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2208947119. PMID: 36417441, PMCID: PMC9860279, DOI: 10.1073/pnas.2208947119.Peer-Reviewed Original ResearchConceptsPI-3K/Akt pathwayAkt pathwayAkt activationDocking protein Gab1EGF-stimulated activationEpithelial cellsLive-cell imagingPhosphoinositide-3 kinaseCell survival pathwaysExocyst complexExocyst functionSmall molecule inhibitorsVesicle tethersExocytic fusionProtein Gab1EGF stimulationExocystSurvival pathwaysExocytosisInhibitors resultsPathwayImportant pathwayEGFR inhibitionMinute time scaleVesicles
2017
Diverse p53/DNA binding modes expand the repertoire of p53 response elements
Vyas P, Beno I, Xi Z, Stein Y, Golovenko D, Kessler N, Rotter V, Shakked Z, Haran T. Diverse p53/DNA binding modes expand the repertoire of p53 response elements. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 10624-10629. PMID: 28912355, PMCID: PMC5635862, DOI: 10.1073/pnas.1618005114.Peer-Reviewed Original ResearchConceptsP53 response elementNatural response elementsResponse elementTetrameric complexCanonical p53 response elementBulk genomic DNAAdjacent spacer sequencesCanonical binding siteP53 binding siteExpression of genesBinding sitesCellular outcomesTranscription factorsDNA sitesP53 bindsSpacer sequencesP53 actsP53 dimersSpecific complexDimer bindsGenomic DNABase pairsPhysiological relevanceFunctional significanceSecond bindsLong‐Term Live‐Cell STED Nanoscopy of Primary and Cultured Cells with the Plasma Membrane HIDE Probe DiI‐SiR
Thompson A, Omar M, Rivera‐Molina F, Xi Z, Koleske A, Toomre D, Schepartz A. Long‐Term Live‐Cell STED Nanoscopy of Primary and Cultured Cells with the Plasma Membrane HIDE Probe DiI‐SiR. Angewandte Chemie 2017, 129: 10544-10548. DOI: 10.1002/ange.201704783.Peer-Reviewed Original Research
2015
29 Structural and binding properties of DNA response elements bound to p53 proteins and the role of spacer sequences in p53-DNA interactions
Vyas P, Beno I, Xi Z, Kessler N, Kitayner M, Crothers D, Shakked Z, Haran T. 29 Structural and binding properties of DNA response elements bound to p53 proteins and the role of spacer sequences in p53-DNA interactions. Journal Of Biomolecular Structure And Dynamics 2015, 33: 16-17. DOI: 10.1080/07391102.2015.1032569.Peer-Reviewed Original Research
2013
Single Neuronal Snare Complexes Zipper in Three Distinct Stages
Gao Y, Zorman S, Gundersen G, Xi Z, Ma L, Sirinakis G, Rothman J, Zhang Y. Single Neuronal Snare Complexes Zipper in Three Distinct Stages. Biophysical Journal 2013, 104: 89a. DOI: 10.1016/j.bpj.2012.11.531.Peer-Reviewed Original Research
2012
Combined versatile high-resolution optical tweezers and single-molecule fluorescence microscopy
Sirinakis G, Ren Y, Gao Y, Xi Z, Zhang Y. Combined versatile high-resolution optical tweezers and single-molecule fluorescence microscopy. Review Of Scientific Instruments 2012, 83: 093708. PMID: 23020384, PMCID: PMC3465359, DOI: 10.1063/1.4752190.Peer-Reviewed Original ResearchConceptsOptical tweezersSingle-molecule fluorescence microscopyDual-trap optical tweezersForce modeHigh-resolution optical tweezersConstant force modeSingle-molecule fluorescence detectionFluorescence microscopySingle-molecule approachOptical trappingDNA hairpin moleculesSingle-molecule fluorescenceSimilar microscopesSingle-molecule levelImaging configurationsΛ-DNA moleculesTweezersMolecular machinesDNA moleculesEasy data interpretationFluorescence signalHairpin moleculesSpatiotemporal resolutionMicroscopyComplementary oligonucleotidesSingle Reconstituted Neuronal SNARE Complexes Zipper in Three Distinct Stages
Gao Y, Zorman S, Gundersen G, Xi Z, Ma L, Sirinakis G, Rothman JE, Zhang Y. Single Reconstituted Neuronal SNARE Complexes Zipper in Three Distinct Stages. Science 2012, 337: 1340-1343. PMID: 22903523, PMCID: PMC3677750, DOI: 10.1126/science.1224492.Peer-Reviewed Original ResearchChapter One DNA Translocation of ATP-Dependent Chromatin Remodeling Factors Revealed by High-Resolution Optical Tweezers
Zhang Y, Sirinakis G, Gundersen G, Xi Z, Gao Y. Chapter One DNA Translocation of ATP-Dependent Chromatin Remodeling Factors Revealed by High-Resolution Optical Tweezers. Methods In Enzymology 2012, 513: 3-28. PMID: 22929763, DOI: 10.1016/b978-0-12-391938-0.00001-x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateBase SequenceBinding SitesChromatin Assembly and DisassemblyDNADNA HelicasesElectrophoresis, Polyacrylamide GelEscherichia coliMicroscopy, Atomic ForceMolecular Sequence DataNucleic Acid ConformationNucleosomesOptical TweezersPlasmidsTandem Repeat SequencesConceptsChromatin remodelingChromatin structureDNA translocationATP-dependent chromatin remodeling factorsATP-dependent chromatin remodelingATP-dependent chromatinChromatin remodeling factorsDNA moleculesOptical tweezersHigh-resolution optical tweezersSingle-molecule assaysRemodeler ATPasesDNA translocasesRemodeling factorsSingle DNA moleculesDNA substratesSingle-molecule levelATP hydrolysisBiological functionsBare DNASingle-molecule experimentsMolecular mechanismsDetailed protocolTranslocationMolecular motorsDirect Observation of Helix Staggering, Sliding, and Coiled Coil Misfolding
Zhang Y, Xi Z, Gao Y, Sirinakis G, Guo H. Direct Observation of Helix Staggering, Sliding, and Coiled Coil Misfolding. Biophysical Journal 2012, 102: 175a. DOI: 10.1016/j.bpj.2011.11.949.Peer-Reviewed Original Research
2010
Anomalous DNA binding by E2 regulatory protein driven by spacer sequence TATA
Xi Z, Zhang Y, Hegde RS, Shakked Z, Crothers DM. Anomalous DNA binding by E2 regulatory protein driven by spacer sequence TATA. Nucleic Acids Research 2010, 38: 3827-3833. PMID: 20185566, PMCID: PMC2887970, DOI: 10.1093/nar/gkq114.Peer-Reviewed Original Research
2004
Predicting indirect readout effects in protein–DNA interactions
Zhang Y, Xi Z, Hegde RS, Shakked Z, Crothers DM. Predicting indirect readout effects in protein–DNA interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 8337-8341. PMID: 15148366, PMCID: PMC420395, DOI: 10.1073/pnas.0402319101.Peer-Reviewed Original Research