2017
Structural Perspectives on Sigma-1 Receptor Function
Alon A, Schmidt H, Zheng S, Kruse A. Structural Perspectives on Sigma-1 Receptor Function. Advances In Experimental Medicine And Biology 2017, 964: 5-13. PMID: 28315261, DOI: 10.1007/978-3-319-50174-1_2.Peer-Reviewed Original ResearchConceptsER-resident transmembrane proteinCarboxy-terminal domainDrug-like small moleculesOverall foldsLigand moleculesTransmembrane proteinsMolecular structureCrystal structureHuman diseasesLigand recognitionMolecular viewReceptor arrangementSmall moleculesProtomersSigma-1LigandReceptor structureProteinMoleculesReceptor functionSigma-1 receptorStructureOligomerizationReceptorsCrystal
2001
Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells
Murli S, Watson R, Galán J. Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells. Cellular Microbiology 2001, 3: 795-810. PMID: 11736992, DOI: 10.1046/j.1462-5822.2001.00158.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsBacterial Proteinscdc42 GTP-Binding ProteinCell NucleusCytoskeletonInterleukin-8Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPhosphorylationPhosphotyrosineProtein Tyrosine PhosphatasesProtein-Tyrosine KinasesSalmonellaSalmonella typhimuriumSignal TransductionSubstrate SpecificityTransfectionTyrosineVimentinConceptsTyrosine phosphatase activityBacterial proteinsCellular responsesPhosphatase activityTyrosine kinaseHost cellsType III secretion systemIntermediate filament protein vimentinCarboxy-terminal domainRho family GTPases Cdc42Actin cytoskeleton reorganizationCellular transcription factorsMAP kinase activationInteraction of SalmonellaMembrane rufflesGAP activitySpecialized organellesGTPases Cdc42Secretion systemTranscription factorsCytoskeleton reorganizationKinase activationProtein vimentinBacterial uptakeProtein
2000
Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2
Haffner C, Di Paolo G, Rosenthal J, De Camilli P. Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2. Current Biology 2000, 10: 471-474. PMID: 10801423, DOI: 10.1016/s0960-9822(00)00446-2.Peer-Reviewed Original ResearchConceptsClathrin adaptor AP-2Adaptor AP-2AP-2Synaptojanin 1Unique carboxy-terminal regionClathrin coat dynamicsAlpha-adaptin subunitCarboxy-terminal domainCarboxy-terminal extensionAmino-terminal domainSynaptic vesicle recyclingCarboxy-terminal regionBinding of clathrinReceptor-mediated endocytosisChinese hamster ovary cellsActin functionPolyphosphoinositide phosphataseEar domainClathrin coatHamster ovary cellsVesicle recyclingVariety of tissuesTransferrin uptakePleiotropic rolesClathrin
1995
A kinase–cyclin pair in the RNA polymerase II holoenzyme
Liao S, Zhang J, Jeffery D, Koleske A, Thompson C, Chao D, Viljoen M, van Vuuren H, Young R. A kinase–cyclin pair in the RNA polymerase II holoenzyme. Nature 1995, 374: 193-196. PMID: 7877695, DOI: 10.1038/374193a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCyclin-Dependent Kinase 8Cyclin-Dependent KinasesCyclinsFungal ProteinsMolecular Sequence DataMutationProtein Serine-Threonine KinasesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticConceptsRNA polymerase II holoenzymeSRB proteinsKinase functionRNA polymerase II carboxy-terminal domainCyclin-like proteinGeneral transcription factorsRNA polymerase IISuppressors of mutationsNormal transcriptional responseCarboxy-terminal domainPolymerase IITranscriptional regulatorsTranscriptional responseGalactose inductionTranscription factorsRegulatory proteinsTranscription systemHoloenzymeRegulatory roleKinaseProteinBiochemical evidenceGenesVivoSrb11
1993
A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
Thompson C, Koleske A, Chao D, Young R. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 1993, 73: 1361-1375. PMID: 8324825, DOI: 10.1016/0092-8674(93)90362-t.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesDNA Mutational AnalysisDNA-Binding ProteinsFungal ProteinsGene Expression RegulationMediator ComplexMolecular Sequence DataMultienzyme ComplexesRecombinant ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription, GeneticConceptsTATA-binding proteinRNA polymerase II carboxy-terminal domainCarboxy-terminal domainMultisubunit complexLarge multisubunit complexFunctional preinitiation complexRNA polymerase IIEfficient transcription initiationTranscription initiation complexSRB proteinsCTD proteinsExtragenic suppressorsCTD functionPolymerase IIPreinitiation complexTranscription initiationInitiation complexComplex bindsTruncation mutationsSRB2Srb5ProteinBiochemical evidenceComplexesSRB4
1992
A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID
Koleske A, Buratowski S, Nonet M, Young R. A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID. Cell 1992, 69: 883-894. PMID: 1591782, DOI: 10.1016/0092-8674(92)90298-q.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBlotting, WesternChromatography, AffinityFungal ProteinsGenes, SuppressorMediator ComplexMolecular Sequence DataMutationRecombinant Fusion ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factor TFIIDTranscription FactorsTranscription, GeneticConceptsCarboxy-terminal domainRNA polymerase II carboxy-terminal domainNovel transcription factorTranscription initiation complexInitiation complexTranscription factorsFunctional linkConditional growth phenotypesTranscription initiation apparatusRNA polymerase IITATA-binding factorDominant suppressorsPolymerase IIGrowth phenotypeTranscription initiationGene expressionAllele specificitySRB2Truncation mutationsSame functionSimilar defectsTFIIDSuppressorEfficient establishmentMechanism of action
1987
A new lamin in Xenopus somatic tissues displays strong homology to human lamin A.
Wolin S, Krohne G, Kirschner M. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. The EMBO Journal 1987, 6: 3809-3818. PMID: 3428277, PMCID: PMC553853, DOI: 10.1002/j.1460-2075.1987.tb02717.x.Peer-Reviewed Original ResearchConceptsHuman lamin ACDNA clonesXenopus laminSomatic tissuesLamin AMajor lamin proteinsCarboxy-terminal domainAdult somatic cellsHuman lamin A.Major laminsDistinct structural classesLamin proteinsNuclear laminaLamin LIIIEmbryonic developmentSomatic cellsSomatic laminsStrong homologyLamin A.Lamin LILaminsMajor polypeptidesGerm cellsProteinClones
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