2025
SLC25A38 is required for mitochondrial pyridoxal 5’-phosphate (PLP) accumulation
Pena I, Shi J, Chang S, Yang J, Block S, Adelmann C, Keys H, Ge P, Bathla S, Witham I, Sienski G, Nairn A, Sabatini D, Lewis C, Kory N, Vander Heiden M, Heiman M. SLC25A38 is required for mitochondrial pyridoxal 5’-phosphate (PLP) accumulation. Nature Communications 2025, 16: 978. PMID: 39856062, PMCID: PMC11760969, DOI: 10.1038/s41467-025-56130-3.Peer-Reviewed Original ResearchConceptsPyridoxal 5'-phosphateGenome-wide CRISPR interference screenPyridoxal 5'-phosphate-dependent enzymeCRISPR interference screenSerine hydroxymethyltransferase-2Active form of vitamin B6One-carbon unitsImpaired cellular proliferationAmino acid metabolismOne-carbon metabolismInterference screenEssential proteinsMolecular machineryNucleotide synthesisCongenital sideroblastic anemiaProliferation defectSLC25A38Acid metabolismErythroleukemia cellsOrnithine aminotransferaseActive formK562 cellsEnzymatic reactionsCellular proliferationPolyamine synthesis
2022
Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging
Cabral‐Miranda F, Tamburini G, Martinez G, Ardiles A, Medinas D, Gerakis Y, Hung M, Vidal R, Fuentealba M, Miedema T, Duran‐Aniotz C, Diaz J, Ibaceta‐Gonzalez C, Sabusap C, Bermedo‐Garcia F, Mujica P, Adamson S, Vitangcol K, Huerta H, Zhang X, Nakamura T, Sardi S, Lipton S, Kennedy B, Henriquez J, Cárdenas J, Plate L, Palacios A, Hetz C. Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging. The EMBO Journal 2022, 41: embj2022111952. PMID: 36314651, PMCID: PMC9670206, DOI: 10.15252/embj.2022111952.Peer-Reviewed Original ResearchConceptsUnfolded protein responseER stress sensor IRE1Stress sensor IRE1IRE1/XBP1 signalingTranscription factor XBP1Mammalian brain agingNeurodegenerative diseasesProteostasis networkEndoplasmic reticulum stressProteomic profilingProtein responseCell senescenceGenetic disruptionBrain agingXBP1 expressionReticulum stressMammalian brainMajor risk factorActive formHealthy brain agingSynaptic functionXBP1Age-related cognitive declinePathwayHippocampal tissue
2018
Mutations in Plasmodium falciparum actin-binding protein coronin confer reduced artemisinin susceptibility
Demas A, Sharma A, Wong W, Early A, Redmond S, Bopp S, Neafsey D, Volkman S, Hartl D, Wirth D. Mutations in Plasmodium falciparum actin-binding protein coronin confer reduced artemisinin susceptibility. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 12799-12804. PMID: 30420498, PMCID: PMC6294886, DOI: 10.1073/pnas.1812317115.Peer-Reviewed Original ResearchConceptsCRISPR/Cas9-mediated gene editingDomain protein familyWhole genome sequence analysisProtein familySecond geneFunctional validationMutant formsDifferent genesMolecular mechanismsParental linesSequence analysisType of resistanceGene editingAfrican parasitesArtemisinin susceptibilityMechanisms of resistanceGenesGenetic determinantsParental parasitesMutationsSurvival assaysIndependent selectionParasite clonesProteinActive form
2014
Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation
Langemeyer L, Bastos R, Cai Y, Itzen A, Reinisch KM, Barr FA. Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation. ELife 2014, 3: e01623. PMID: 24520163, PMCID: PMC3919270, DOI: 10.7554/elife.01623.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAspartic AcidBacterial ProteinsCatalytic DomainDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsEnzyme ActivationGlutamineGuanine Nucleotide Exchange FactorsHeLa CellsHumansHydrolysisListeriaModels, MolecularMutagenesis, Site-DirectedMutationProtein Conformationrab GTP-Binding Proteinsrab1 GTP-Binding Proteinsrab5 GTP-Binding ProteinsSignal TransductionTransfectionConceptsActive site residuesGTP hydrolysis mechanismNucleotide-free formActive site glutamineSwitch II regionDifferent RabsRab activationRab GTPasesGTPase activationGlutamine mutantNucleotide exchangeGDP releaseRabActivation mechanismActivation pathwayActive formPathwayResiduesActivationII regionRAPlasticityGTPasesRab5GEF
2013
Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system
Park S, Groisman EA. Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system. Molecular Microbiology 2013, 91: 135-144. PMID: 24256574, PMCID: PMC3890429, DOI: 10.1111/mmi.12449.Peer-Reviewed Original ResearchConceptsTransporter MgtATwo-component systems PhoP/PhoQPhoP-dependent genesAntimicrobial peptide C18G.PhoP/PhoQSalmonella enterica serovar TyphimuriumSensor PhoQEnterica serovar TyphimuriumVirulence functionsRepressing signalsGene setsPhoQMgtAGenesSerovar TyphimuriumElicit expressionPeriplasmPhoPActive formFull transcriptionExpressionPhoQ.TranscriptionCytoplasmicProtein
2009
E6AP promotes the degradation of the PML tumor suppressor
Louria-Hayon I, Alsheich-Bartok O, Levav-Cohen Y, Silberman I, Berger M, Grossman T, Matentzoglu K, Jiang Y, Muller S, Scheffner M, Haupt S, Haupt Y. E6AP promotes the degradation of the PML tumor suppressor. Cell Death & Differentiation 2009, 16: 1156-1166. PMID: 19325566, DOI: 10.1038/cdd.2009.31.Peer-Reviewed Original ResearchConceptsPML-NBsNuclear bodiesTumor suppressorPromyelocytic leukemia (PML) tumor suppressorE3 ligase E6APPML tumor suppressorPML nuclear bodiesPML protein expressionUbiquitination assaysCertain human cancersStress signalsPML proteinImportant regulatorPML stabilityDNA damageE6APCell typesHuman cancersProtein expressionActive formNull micePhysiological levelsSuppressorGrowth inhibitionPMLBacterial proteins as potential drugs in the treatment of leukemia
Kwan JM, Fialho AM, Kundu M, Thomas J, Hong CS, Gupta T, Chakrabarty AM. Bacterial proteins as potential drugs in the treatment of leukemia. Leukemia Research 2009, 33: 1392-1399. PMID: 19250673, DOI: 10.1016/j.leukres.2009.01.024.Peer-Reviewed Original ResearchConceptsBacterial proteinsSerine/threonine kinaseLeukemia cell linesCaspase recruitment domainCell linesAkt-Ser-473Cell cycle arrestG2/M phaseThreonine kinaseLike domainCARD domainRecruitment domainProtein stabilizationCycle arrestM phaseHL60 cellsProteinActive formPeripheral blood mononuclear cellsBlood mononuclear cellsLeukemia cellsCancer typesAzurinCytotoxic effectsTreatment of leukemia
2008
Expression and function of striatal enriched protein tyrosine phosphatase is profoundly altered in cerebral ischemia
Braithwaite SP, Xu J, Leung J, Urfer R, Nikolich K, Oksenberg D, Lombroso PJ, Shamloo M. Expression and function of striatal enriched protein tyrosine phosphatase is profoundly altered in cerebral ischemia. European Journal Of Neuroscience 2008, 27: 2444-2452. PMID: 18445231, PMCID: PMC2738830, DOI: 10.1111/j.1460-9568.2008.06209.x.Peer-Reviewed Original ResearchConceptsStriatal enriched protein tyrosine phosphataseProtein tyrosine phosphataseTyrosine phosphatasePost-transcriptional levelNovel speciesPhosphorylation stateImportant proteinsMature formKey substrateNMDA receptor subunitsReceptor subunitsActive formSynaptic functionComplex cascadeCritical roleERKMRNA levelsProteinMRNAPERKPhosphataseCleavageCentral nervous systemNervous systemSubunits
2000
Homocysteine stimulates MAP kinase in bovine aortic smooth muscle cells
Woo D, Dudrick S, Sumpio B. Homocysteine stimulates MAP kinase in bovine aortic smooth muscle cells. Surgery 2000, 128: 59-66. PMID: 10876187, DOI: 10.1067/msy.2000.106531.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell DivisionCells, CulturedDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsFlavonoidsHomocysteineMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMuscle, Smooth, VascularPhosphorylationConceptsMAP kinase phosphorylationMAP kinaseKinase phosphorylationBASMC proliferationBovine aortic smooth muscle cellsAortic smooth muscle cellsCell proliferationExtracellular signal-regulated protein kinases 1Mitogen-activated protein kinaseSmooth muscle cell proliferationProtein kinase 1Smooth muscle cellsMuscle cell proliferationMAP kinase activationDegree of phosphorylationL-homocysteineMuscle cellsProtein kinaseKinase studiesKinase activationKinase 1Hallmark of atherosclerosisKinasePhosphorylationActive form
1998
Characterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*
Matsushita M, Nairn A. Characterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*. Journal Of Biological Chemistry 1998, 273: 21473-21481. PMID: 9705275, DOI: 10.1074/jbc.273.34.21473.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCalmodulinCloning, MolecularEnzyme ActivationKineticsMolecular Sequence DataPhosphorylationProtein Serine-Threonine KinasesRatsConceptsProtein kinase IAbsence of CaMKinase ICalmodulin-dependent protein kinase IDetailed structure-function analysisDependent protein kinase IDependent protein kinase kinaseProtein kinase kinaseStructure-function analysisMechanism of regulationSpecific amino acidsEnzyme activityKinase kinaseAutoinhibited stateRegulatory domainCatalytic coreCaMKIMutant formsBasal enzyme activitySecond enzymeCaMKKAmino acidsAdditional mutationsMutationsActive formCyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases
Egan E, Solomon M. Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases. Molecular And Cellular Biology 1998, 18: 3659-3667. PMID: 9632748, PMCID: PMC108948, DOI: 10.1128/mcb.18.7.3659.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCDC2 Protein KinaseCDC2-CDC28 KinasesCell Cycle ProteinsCyclin ACyclin BCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationPhosphorylationProtein BindingProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsThreonineXenopusXenopus Proteins
1997
Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain
Uellner R, Zvelebil M, Hopkins J, Jones J, MacDougall L, Morgan B, Podack E, Waterfield M, Griffiths G. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain. The EMBO Journal 1997, 16: 7287-7296. PMID: 9405358, PMCID: PMC1170329, DOI: 10.1093/emboj/16.24.7287.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCytotoxicity, ImmunologicGlycosylationHexosaminidasesHumansIsoenzymesKiller Cells, NaturalLiposomesLymphocyte ActivationMembrane GlycoproteinsModels, MolecularMolecular Sequence DataPerforinPhospholipase C deltaPhospholipidsPore Forming Cytotoxic ProteinsProtein ConformationProtein Processing, Post-TranslationalRatsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTransfectionType C PhospholipasesConceptsC2 domainPro-pieceProteolytic cleavagePlasma membrane of target cellsBind phospholipid membranesMembrane of target cellsCalcium-dependent mannerSecreted proteinsIntracellular transportC-terminusPhospholipid membranesNK cell line YTPlasma membraneCleaved formInactive precursorAcidic compartmentsIncreased lytic activityConcanamycin AActive formLytic activityKilling assayE-64CleavageEpitope mappingPore formation
1996
Effect of ethanol on cholecystokinin-stimulated zymogen conversion in pancreatic acinar cells
Katz M, Carangelo R, Miller LJ, Gorelick F. Effect of ethanol on cholecystokinin-stimulated zymogen conversion in pancreatic acinar cells. American Journal Of Physiology 1996, 270: g171-g175. PMID: 8772515, DOI: 10.1152/ajpgi.1996.270.1.g171.Peer-Reviewed Original ResearchConceptsPancreatic acinar cellsEffects of ethanolAbility of ethanolAcinar cellsHigh dosesLow dose cholecystokininCholecystokinin receptor antagonistDose of ethanolReceptor antagonistCholecystokininSmall intestineCholecystokinin receptorsEthanol treatmentActive formCarbamylcholineZymogen conversionIntracellular conversionDosesPancreatic zymogensCellsAntagonistDoseIntestine
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