2000
Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
Kubori T, Sukhan A, Aizawa S, Galán J. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 10225-10230. PMID: 10944190, PMCID: PMC27824, DOI: 10.1073/pnas.170128997.Peer-Reviewed Original ResearchConceptsType III secretion systemProtein secretion systemSecretion systemNeedle complexType III protein secretion systemHost cellular functionsSpecialized protein secretion systemType III secretion export apparatusType III secretionPathogenicity island 1Secretion complexPathogen's benefitExport apparatusCellular functionsAnimal cellsNeedle-like projectionsBacterial proteinsBacterium's abilityNeedle substructureIsland 1Host cellsMolecular characterizationNonphagocytic cellsNeedle componentBacterial pathogensComplex Function for SicA, a Salmonella enterica Serovar Typhimurium Type III Secretion-Associated Chaperone
Tucker S, Galán J. Complex Function for SicA, a Salmonella enterica Serovar Typhimurium Type III Secretion-Associated Chaperone. Journal Of Bacteriology 2000, 182: 2262-2268. PMID: 10735870, PMCID: PMC111276, DOI: 10.1128/jb.182.8.2262-2268.2000.Peer-Reviewed Original Research
1999
Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization
Zhou D, Mooseker M, Galán J. Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization. Science 1999, 283: 2092-2095. PMID: 10092234, DOI: 10.1126/science.283.5410.2092.Peer-Reviewed Original Research
1998
The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
Fu Y, Galán J. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Molecular Microbiology 1998, 27: 359-368. PMID: 9484891, DOI: 10.1046/j.1365-2958.1998.00684.x.Peer-Reviewed Original ResearchConceptsActin cytoskeletonHost cell actin cytoskeletonFusion proteinHost cellsAmino acidsAmino-terminal halfCell actin cytoskeletonCultured cells resultsWild-type toxinCultured epithelial cellsEffector proteinsModular domainsStress fibersActive GSTCytoskeletonProteinCells resultsEpithelial cellsGSTSPTPProlonged incubationTranslocationCellsS. typhimuriumMicroinjection
1997
The invasion‐associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell
Collazo C, Galán J. The invasion‐associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell. Molecular Microbiology 1997, 24: 747-756. PMID: 9194702, DOI: 10.1046/j.1365-2958.1997.3781740.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, BacterialBacterial ProteinsBiological TransportCells, CulturedCytochalasin DIntestinesMembrane ProteinsSalmonella typhimuriumConceptsProtein secretion systemProtein translocationHost cellsSIP proteinHenle-407 cellsType III protein secretion systemType III secretion systemType III secretion apparatusType III systemSubset of targetsCentisome 63Secretion apparatusSecretion systemBacterial entryBacterial internalizationNull mutationSalmonella typhimuriumCytochalasin DTranslocation processTranslocationProteinMutationsPresence of gentamicinSipBS. typhimurium strain