2001
Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
Stebbins C, Galán J. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 2001, 414: 77-81. PMID: 11689946, DOI: 10.1038/35102073.Peer-Reviewed Original ResearchConceptsEffector proteinsSecretion systemType III protein secretion systemBacterial type III secretionSpecific cytosolic chaperonesSuch effector proteinsType III secretion systemSecretion-competent stateVirulence effector proteinsProtein secretion systemChaperone-binding domainHost cell cytosolType III secretionType III apparatusCytosolic chaperonesUnfolded polypeptidesSecretion machineryCognate chaperoneÅ resolutionChaperonesCell cytosolChaperone moleculesEffective translocationBacterial pathogensHydrophobic interfaceStructural mimicry in bacterial virulence
Stebbins C, Galán J. Structural mimicry in bacterial virulence. Nature 2001, 412: 701-705. PMID: 11507631, DOI: 10.1038/35089000.Peer-Reviewed Original ResearchConceptsAmino acid sequence similarityConvergent evolutionCellular functionsSequence similarityDirect homologuesBacterial virulenceHost proteinsNew effectorsMicrobial pathogensFunctional mimicryStructural mimicryMolecular levelVirulence factorsMimicryStructural studiesHost factorsImportant mechanismHost activityHomologuesVirulenceEffectorsProteinPathogensSimilarity
2000
Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1
Stebbins C, Galán J. Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1. Molecular Cell 2000, 6: 1449-1460. PMID: 11163217, DOI: 10.1016/s1097-2765(00)00141-6.Peer-Reviewed Original ResearchMeSH KeywordsAluminum CompoundsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding SitesCdc42 GTP-Binding ProteinCrystallography, X-RayDimerizationEvolution, MolecularFluoridesGTPase-Activating ProteinsGuanosine DiphosphateMacromolecular SubstancesModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein Tyrosine PhosphatasesRac1 GTP-Binding ProteinRecombinant Fusion ProteinsSalmonella typhimuriumSequence AlignmentSignal TransductionBiophysical characterization of SipA, an actin‐binding protein from Salmonella enterica
Mitra K, Zhou D, Galán J. Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica. FEBS Letters 2000, 482: 81-84. PMID: 11018527, DOI: 10.1016/s0014-5793(00)02040-8.Peer-Reviewed Original ResearchConceptsActin dynamicsCoiled-coil domainF-actin stabilityActin-binding proteinsActin cytoskeleton reorganizationNon-phagocytic cellsBacterial entryCytoskeleton reorganizationAdjacent actin monomersC-terminal fragmentBiophysical characterizationF-actinCellular responsesHost cellsBacterial uptakeActin monomersProteinSalmonella entericaHelical conformationSalmonella enterica infectionsIntestinal epitheliumEnterica infectionsEssential stepSIPACells