2022
Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment
Rajendran M, Queralt-Martín M, Gurnev P, Rosencrans W, Rovini A, Jacobs D, Abrantes K, Hoogerheide D, Bezrukov S, Rostovtseva T. Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment. Cellular And Molecular Life Sciences 2022, 79: 368. PMID: 35718804, PMCID: PMC11072225, DOI: 10.1007/s00018-022-04389-w.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelVDAC poreProtein-membrane bindingRegulating mitochondrial functionProximity ligation assayInvolvement of alpha-synucleinMembrane bindingMitochondrial respirationMitochondrial functionHeLa cellsLigation assayLipid membranesHexokinase 2MitochondriaTranslocation processComplex inhibitionAnion channelFluorescence correlation spectroscopyAlpha-synucleinMolecular levelMitochondrial toxicityASynTranslocationPeptide therapeuticsTherapeutic target
2018
Peptidoglycan editing by a specific ld-transpeptidase controls the muramidase-dependent secretion of typhoid toxin
Geiger T, Pazos M, Lara-Tejero M, Vollmer W, Galán JE. Peptidoglycan editing by a specific ld-transpeptidase controls the muramidase-dependent secretion of typhoid toxin. Nature Microbiology 2018, 3: 1243-1254. PMID: 30250245, PMCID: PMC7464686, DOI: 10.1038/s41564-018-0248-x.Peer-Reviewed Original ResearchConceptsProtein export mechanismProtein secretion mechanismsTyphoid toxinEssential virulence factorBacterial poleMammalian cellsPeptidoglycan layerMost bacterial pathogensOuter membraneExport mechanismSecretion mechanismToxin secretionBacterial speciesTranslocation processTrans sideVirulence factorsBacterial pathogensExtracellular spaceTransport pathwaysTarget cellsToxinTyphoid feverCellsSubsequent releaseSecretion
2011
The RSC chromatin remodelling ATPase translocates DNA with high force and small step size
Sirinakis G, Clapier CR, Gao Y, Viswanathan R, Cairns BR, Zhang Y. The RSC chromatin remodelling ATPase translocates DNA with high force and small step size. The EMBO Journal 2011, 30: 2364-2372. PMID: 21552204, PMCID: PMC3116276, DOI: 10.1038/emboj.2011.141.Peer-Reviewed Original ResearchConceptsATP-dependent chromatinHigh-resolution optical tweezersDNA-histone interactionsBp/sDNA translocation processRSC chromatinATPase domainTranslocase systemDiverse functionsATP hydrolysisBare DNATranslocation processBiophysical knowledgeDNAChromatinNucleosomesMechanical forcesBPForce generationRemodellersTranslocaseProcessivityTranslocationATPaseOptical tweezers
2005
Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*
Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH. Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*. Journal Of Biological Chemistry 2005, 280: 22892-22898. PMID: 15849200, DOI: 10.1074/jbc.m500035200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCaseinsChromatographyCross-Linking ReagentsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndopeptidase ClpEscherichia coliEscherichia coli ProteinsGlycineHydrolysisModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedMutationPeptidesProtein BindingProtein DenaturationProtein FoldingProtein TransportSequence Homology, Amino AcidTemperatureConceptsHslU ATPasePore motifHslVU complexHslV peptidaseCentral poreATP-dependent proteaseProtein unfoldingProteolytic active sitesHslU hexamerProteolytic chamberHslV dodecamerUnfolded proteinsHslV.HslUGly residueTranslocation processAmino acidsDegradation of caseinMotifProteinATP cleavageSame structural featuresATPase activityTranslocationATPase
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 ResearchConceptsProtein 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
1994
Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
Mothes W, Prehn S, Rapoport T. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. The EMBO Journal 1994, 13: 3973-3982. PMID: 8076593, PMCID: PMC395317, DOI: 10.1002/j.1460-2075.1994.tb06713.x.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAmino Acid SequenceAzirinesBenzoatesBiological TransportCell CompartmentationCross-Linking ReagentsDNA Mutational AnalysisEndoplasmic ReticulumLysineMembrane ProteinsModels, BiologicalMolecular Sequence DataProlactinProtein BiosynthesisProtein PrecursorsSEC Translocation ChannelsStructure-Activity RelationshipUltraviolet RaysConceptsSec61 alphaNascent chainsProtein interactsSignal sequenceProtein-conducting channelSecretory protein preprolactinNascent polypeptide chainsEndoplasmic reticulum membranePhoto-crosslinking approachSec61p complexER membraneMembrane proteinsMembrane environmentSecretory proteinsPolypeptide segmentsReticulum membranePolypeptide chainTranslocation processHydrophobic coreRibosomesProtein environmentProteinTranslocationPhotoreactive groupSequence
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