2021
Trio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts
Bircher JE, Koleske AJ. Trio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts. Journal Of Cell Science 2021, 134: jcs248393. PMID: 33568469, PMCID: PMC7888718, DOI: 10.1242/jcs.248393.Peer-Reviewed Original ResearchConceptsFamily proteinsCellular contextProtein-protein interaction domainsHuman diseasesProtein trafficking pathwaysLarge multidomain proteinCell surface receptorsTrio proteinsUNC-73Cell morphogenesisProtein traffickingTrafficking pathwaysMultidomain proteinsInteraction domainInteraction partnersKey regulatorBiological contextTissue organizationCell migrationSurface receptorsProteinTrio familiesRecent discoveryMorphogenesisRegulator
2017
Domain-Targeted Metabolomics Delineates the Heterocycle Assembly Steps of Colibactin Biosynthesis
Trautman EP, Healy AR, Shine EE, Herzon SB, Crawford JM. Domain-Targeted Metabolomics Delineates the Heterocycle Assembly Steps of Colibactin Biosynthesis. Journal Of The American Chemical Society 2017, 139: 4195-4201. PMID: 28240912, PMCID: PMC5831107, DOI: 10.1021/jacs.7b00659.Peer-Reviewed Original ResearchConceptsNonribosomal peptide synthetasesPolyketide synthasesModular polyketide synthasesSite-directed mutagenesisCombination of genesCellular metabolic levelsColibactin biosynthesisMultidomain proteinsProtein domainsPeptide synthetasesCatalytic domainControl pathwaysProtein biochemicalPathway analysisCertain Escherichia coliComplete deletionHybrid pathwayEscherichia coliFunctional readoutBiosynthesisCatalytic mechanismCellular levelMetabolic levelPathwayGenes
2009
Allostery and conformational free energy changes in human tryptophanyl‐tRNA synthetase from essential dynamics and structure networks
Bhattacharyya M, Ghosh A, Hansia P, Vishveshwara S. Allostery and conformational free energy changes in human tryptophanyl‐tRNA synthetase from essential dynamics and structure networks. Proteins Structure Function And Bioinformatics 2009, 78: 506-517. PMID: 19768679, DOI: 10.1002/prot.22573.Peer-Reviewed Original ResearchConceptsHuman tryptophanyl-tRNA synthetaseTryptophanyl-tRNA synthetaseConcept of allosteryProtein structure networksProtein complexesMultidomain proteinsAllosteric communicationFunctional insightsProtein biosynthesisCognate tRNAAllosteric mechanismAllosteryConformational free energy changesEnzymatic catalysisConformational mobilityFlexible regionsMolecular levelAmino acidsProteinStructure networkMolecular-level understandingFree energy landscapePopulation shiftsMolecular dynamics simulationsFree energy change
2008
RIM1α and RIM1β Are Synthesized from Distinct Promoters of the RIM1 Gene to Mediate Differential But Overlapping Synaptic Functions
Kaeser P, Kwon H, Chiu C, Deng L, Castillo P, Südhof T. RIM1α and RIM1β Are Synthesized from Distinct Promoters of the RIM1 Gene to Mediate Differential But Overlapping Synaptic Functions. Journal Of Neuroscience 2008, 28: 13435-13447. PMID: 19074017, PMCID: PMC2701653, DOI: 10.1523/jneurosci.3235-08.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsExcitatory Postsynaptic PotentialsGTP-Binding ProteinsHippocampusMiceMice, KnockoutNeuronal PlasticityNeurotransmitter AgentsOrgan Culture TechniquesPatch-Clamp TechniquesPresynaptic TerminalsPromoter Regions, GeneticProtein IsoformsReverse Transcriptase Polymerase Chain ReactionSynapsesSynaptic TransmissionSynaptic VesiclesConceptsRIM1 geneActive zone proteinsKnock-out miceSynaptic vesicle primingPresynaptic long-term plasticitySynaptic vesicle proteinsNeurotransmitter releaseLong-term presynaptic plasticityVesicle primingActive zoneMultidomain proteinsSynaptotagmin-1Vesicle proteinsRIM1alphaN-terminusRIM1Plasma membranePresynaptic plasticityDeletionGenesSynaptic functionPresynaptic terminalsProteinIsoformsShort-term synaptic plasticity
2006
Biochemical and Structural Domain Analysis of Xeroderma Pigmentosum Complementation Group C Protein †
Bunick CG, Miller MR, Fuller BE, Fanning E, Chazin WJ. Biochemical and Structural Domain Analysis of Xeroderma Pigmentosum Complementation Group C Protein †. Biochemistry 2006, 45: 14965-14979. PMID: 17154534, PMCID: PMC2579963, DOI: 10.1021/bi061370o.Peer-Reviewed Original ResearchConceptsXPC functionXeroderma pigmentosum complementation group C proteinFirst functional roleComplementation group C proteinFunctional roleProtease protection assaysStructural domain analysesFull-length proteinXeroderma pigmentosum (XP) diseaseLimited proteolysis experimentsN-terminal portionMultidomain proteinsGlobal genomeMutational defectsProtein interactionsAberrant DNAC-terminal fragmentMolecular basisExcision repairProteolysis experimentsBiochemical characterizationC proteinSequence analysisStructural domainsProtection assays
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