1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
1996
CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS
Galán J, Bliska J. CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS. Annual Review Of Cell And Developmental Biology 1996, 12: 221-255. PMID: 8970727, DOI: 10.1146/annurev.cellbio.12.1.221.Peer-Reviewed Original ResearchConceptsHost cellsHost cell signal transduction pathwaysProtein secretion systemHost cellular functionsSpecialized protein secretion systemSignal transduction pathwaysBacterial pathogensHost cell interactionsSecretion systemTransduction pathwaysBacterial proteinsCell physiologyBiochemical interactionsDiverse groupPathogensNovel therapeutic approachesCellsProteinTranslocationBetter understandingInteractionPathwayPhysiologyTherapeutic approachesBasic aspectsA secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum
Kaniga K, Uralil J, Bliska J, Galán J. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum. Molecular Microbiology 1996, 21: 633-641. PMID: 8866485, DOI: 10.1111/j.1365-2958.1996.tb02571.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCell LineChromosomes, BacterialDisease Models, AnimalDNA, BacterialEpithelial CellsFemaleHumansMacrophagesMiceMice, Inbred BALB CMolecular Sequence DataProtein Tyrosine PhosphatasesSalmonella InfectionsSalmonella typhimuriumSequence Homology, Amino AcidVirulenceConceptsProtein tyrosine phosphataseTyrosine phosphataseEffector proteinsCatalytic domainHost cell signal transduction pathwaysBacterial pathogen Salmonella typhimuriumSignal transduction pathwaysCritical Cys residuesAmino-terminal regionCarboxy-terminal regionPathogen Salmonella typhimuriumCell regulatory moleculesSequence similarityEffector domainSignaling functionsExport proteinCys residuesRegulatory moleculesExoenzyme SSequence analysisPeptide substratesPhosphatase activityCatalytic mechanismProteinYersinia spp
1994
Salmonella entry into mammalian cells: different yet converging signal transduction pathways?
Galán J. Salmonella entry into mammalian cells: different yet converging signal transduction pathways? Trends In Cell Biology 1994, 4: 196-199. PMID: 14731677, DOI: 10.1016/0962-8924(94)90136-8.Peer-Reviewed Original ResearchSignal transduction pathwaysTransduction pathwaysHost cell signal transduction pathwaysCell signal transduction pathwaysDifferent signaling pathwaysCommon effector moleculesMammalian cellsSalmonella entryDifferent cell linesSignaling pathwaysDiverse pathwaysEffector moleculesCell linesPathwayCommon mechanismBacteriaSalmonella bacteriaCellsUptake