2023
Senataxin helicase, the causal gene defect in ALS4, is a significant modifier of C9orf72 ALS G4C2 and arginine-containing dipeptide repeat toxicity
Bennett C, Dastidar S, Arnold F, McKinstry S, Stockford C, Freibaum B, Sopher B, Wu M, Seidner G, Joiner W, Taylor J, West R, La Spada A. Senataxin helicase, the causal gene defect in ALS4, is a significant modifier of C9orf72 ALS G4C2 and arginine-containing dipeptide repeat toxicity. Acta Neuropathologica Communications 2023, 11: 164. PMID: 37845749, PMCID: PMC10580588, DOI: 10.1186/s40478-023-01665-z.Peer-Reviewed Original ResearchConceptsDipeptide repeatsFamilial amyotrophic lateral sclerosisAmyotrophic lateral sclerosisRNA-protein interactionsC9orf72 amyotrophic lateral sclerosisMobility of proteinsNuclear helicaseRNA-dependentDrosophila modelFly linesSenataxin functionFly modelCellular processesC9orf72 geneMembraneless organellesGenetic modifiersSenataxinMovement assayGenetic causeCo-expressionPrimary neuronsDisease phenotypeSporadic amyotrophic lateral sclerosisAge-related motor deficitsHEK293 cells
2021
Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells
Zhang Y, Li K, Li Y, Zhao W, Wang L, Chen Z, Ma X, Yao T, Wang J, Dong W, Li X, Tian X, Fu R. Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells. Pharmacological Research 2021, 169: 105630. PMID: 33932609, DOI: 10.1016/j.phrs.2021.105630.Peer-Reviewed Original ResearchMeSH KeywordsAdamantaneAnimalsBlotting, WesternCase-Control StudiesCell LineDipeptidasesDipeptidesDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEpithelial-Mesenchymal TransitionFibrosisFluorescent Antibody TechniqueHumansKidney Tubules, ProximalMaleMiceMice, Inbred C57BLReal-Time Polymerase Chain ReactionRenal Insufficiency, ChronicConceptsTubulointerstitial fibrosisTubule epithelial cellsCKD patientsUUO miceHK-2 cell modelChronic kidney disease patientsTGF-β1/Smad signalingUnilateral ureteral obstruction animal modelEpithelial cellsKidney disease patientsHealthy control subjectsKidney biopsy specimensProximal tubule epithelial cellsRenal tubule epithelial cellsRenal proximal tubule epithelial cellsHK-2 cellsPotential therapeutic targetRenal inflammationTubulointerstitial injuryRenal functionUUO groupKidney functionProfibrotic mechanismsControl subjectsDisease patients
2020
Caspase 8 loss radiosensitizes head and neck squamous cell carcinoma to SMAC mimetic induced necroptosis
Uzunparmak B, Gao M, Lindemann A, Erikson K, Wang L, Lin E, Frank SJ, Gleber-Netto FO, Zhao M, Skinner HD, Newton JM, Sikora AG, Myers JN, Pickering CR. Caspase 8 loss radiosensitizes head and neck squamous cell carcinoma to SMAC mimetic induced necroptosis. JCI Insight 2020, 5: e139837. PMID: 33108350, PMCID: PMC7714407, DOI: 10.1172/jci.insight.139837.Peer-Reviewed Original ResearchConceptsReceptor-interacting serine/threonine-protein kinase 3Caspase-8Serine/threonine-protein kinase 3Regulated cell death mechanismsPan-caspase inhibitor z-VADSecond mitochondria-derived activatorProtein kinase 3Cell death mechanismsRIP3 functionSmac mimeticsZ-VADKinase 3Death mechanismsMolecular underpinningsNecroptosis pathwayHNSCC cell linesNecroptosisRIP3 expressionCancer cellsCell linesBirinapantNeck squamous cell carcinomaCASP8 mutationsSquamous cell carcinomaSyngeneic mouse model
2019
Dilysine-Methylene Diphenyl Diisocyanate (MDI), a Urine Biomarker of MDI Exposure?
Wisnewski AV, Nassar AF, Liu J, Bello D. Dilysine-Methylene Diphenyl Diisocyanate (MDI), a Urine Biomarker of MDI Exposure? Chemical Research In Toxicology 2019, 32: 557-565. PMID: 30724074, PMCID: PMC6465083, DOI: 10.1021/acs.chemrestox.8b00262.Peer-Reviewed Original ResearchConceptsRespiratory tract exposureMDI exposureUrine biomarkersSkin exposureUrine of miceFuture translational investigationsWestern blot studiesUrinary biomarkersRespiratory tractExposure surveillanceTranslational investigationsDisease preventionMDI conjugatesMiceUrineBiomarkersCollision-induced dissociation (CID) fragmentation patternsExposureUnderstanding pathwaysMDIIndustrial hygieneAlbuminMS/MSTractPrevention
2016
SMAC Mimetic Birinapant plus Radiation Eradicates Human Head and Neck Cancers with Genomic Amplifications of Cell Death Genes FADD and BIRC2
Eytan D, Snow G, Carlson S, Derakhshan A, Saleh A, Schiltz S, Cheng H, Mohan S, Cornelius S, Coupar J, Sowers A, Hernandez L, Mitchell J, Annunziata C, Chen Z, Van Waes C. SMAC Mimetic Birinapant plus Radiation Eradicates Human Head and Neck Cancers with Genomic Amplifications of Cell Death Genes FADD and BIRC2. Cancer Research 2016, 76: 5442-5454. PMID: 27469115, PMCID: PMC5026594, DOI: 10.1158/0008-5472.can-15-3317.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic AgentsBlotting, WesternCarcinoma, Squamous CellCell Line, TumorChemoradiotherapyDipeptidesFas-Associated Death Domain ProteinFemaleGene AmplificationGene Knockdown TechniquesHead and Neck NeoplasmsHumansImmunohistochemistryIndolesInhibitor of Apoptosis ProteinsMiceMice, Inbred BALB CMice, SCIDReal-Time Polymerase Chain ReactionSquamous Cell Carcinoma of Head and NeckTNF-Related Apoptosis-Inducing LigandTumor Necrosis Factor-alphaUbiquitin-Protein LigasesXenograft Model Antitumor AssaysConceptsSmac mimeticsCell deathNovel Smac mimeticsCaspase-dependent apoptosisExpression of FADDFrequent genomic amplificationCell cycle arrestBaculovirus inhibitorG2-M cell cycle arrestApoptosis repeatCancer Genome AtlasDeath domainIAP inhibitorsFunctional importanceSiRNA knockdownDNA fragmentationHNSCC cell linesFADDBirinapantGenomic amplificationGene transferGenome AtlasProtein markersComparison of tumorGenomic alterationsRisk for Hospitalized Heart Failure Among New Users of Saxagliptin, Sitagliptin, and Other Antihyperglycemic Drugs: A Retrospective Cohort Study.
Toh S, Hampp C, Reichman ME, Graham DJ, Balakrishnan S, Pucino F, Hamilton J, Lendle S, Iyer A, Rucker M, Pimentel M, Nathwani N, Griffin MR, Brown NJ, Fireman BH. Risk for Hospitalized Heart Failure Among New Users of Saxagliptin, Sitagliptin, and Other Antihyperglycemic Drugs: A Retrospective Cohort Study. Annals Of Internal Medicine 2016, 164: 705-14. PMID: 27110660, PMCID: PMC5178978, DOI: 10.7326/m15-2568.Peer-Reviewed Original ResearchConceptsHospitalized heart failureMini-Sentinel programCohort studyHeart failureAntihyperglycemic agentsPropensity score-matched analysisDipeptidyl peptidase-4 inhibitorsNew-user cohort studyU.S. FoodPrior cardiovascular diseaseRetrospective cohort studyPeptidase-4 inhibitorsSubgroup of patientsPrincipal discharge diagnosisDPP-4 inhibitorsSecond-generation sulfonylureasType 2 diabetesLarge cohort studyDisease risk scoreSitagliptin usersStudy drugHazard ratioDischarge diagnosisNinth RevisionResidual confoundingUnderstanding the physical basis for the side‐chain conformational preferences of methionine
Virrueta A, O'Hern CS, Regan L. Understanding the physical basis for the side‐chain conformational preferences of methionine. Proteins Structure Function And Bioinformatics 2016, 84: 900-911. PMID: 26917446, DOI: 10.1002/prot.25026.Peer-Reviewed Original ResearchConceptsSide-chain dihedral angle distributionsAmino acidsHigh-resolution protein crystal structuresProtein-protein interfacesMet side chainsStructure of MetProtein crystal structuresVersatile amino acidDihedral angle distributionsProtein structureProtein coreIleSide chainsLeuValPheAcidThrObserved distributionCrystal structureMetSMethionineSerTyrSelenomethionine
2015
CA‐074Me compound inhibits osteoclastogenesis via suppression of the NFATc1 and c‐FOS signaling pathways
Patel N, Nizami S, Song L, Mikami M, Hsu A, Hickernell T, Chandhanayingyong C, Rho S, Compton JT, Caldwell J, Kaiser PB, Bai H, Lee HG, Fischer CR, Lee FY. CA‐074Me compound inhibits osteoclastogenesis via suppression of the NFATc1 and c‐FOS signaling pathways. Journal Of Orthopaedic Research® 2015, 33: 1474-1486. PMID: 25428830, DOI: 10.1002/jor.22795.Peer-Reviewed Original ResearchConceptsOsteolytic disordersOsteoclast biologyBone resorptionCA-074MeC-fosMechanisms of cathepsinsCathepsin B knockout miceB knockout miceCathepsin B inhibitor CA-074Dose-dependent mannerOsteoclast resorption pitsCathepsin B inhibitionInhibits osteoclastogenesisNFATc1 pathwayNew therapiesOsteoclastogenic effectsCA-074Knockout miceLysosomal proteasesMature osteoclastsResorption pitsCathepsin KNew targetsOsteoclastsCompound inhibitsTranscriptional Profiling of Ectoderm Specification to Keratinocyte Fate in Human Embryonic Stem Cells
Tadeu AM, Lin S, Hou L, Chung L, Zhong M, Zhao H, Horsley V. Transcriptional Profiling of Ectoderm Specification to Keratinocyte Fate in Human Embryonic Stem Cells. PLOS ONE 2015, 10: e0122493. PMID: 25849374, PMCID: PMC4388500, DOI: 10.1371/journal.pone.0122493.Peer-Reviewed Original ResearchConceptsHuman embryonic stem cellsEmbryonic stem cellsEctoderm specificationStem cellsHuman embryonic stem cell differentiationEmbryonic stem cell differentiationStem cell differentiationKeratinocyte fateEctoderm lineageEpidermal specificationTranscriptional regulationCandidate regulatorsTranscriptional profilingEpidermal developmentGrowth factor activityProtein aP2Keratinocyte developmentCell differentiationΓ-secretase inhibitor DAPTGenesFactor activityHomeostatic conditionsEpithelial tissuesInhibitor DAPTCell signature
2014
Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models
Zhou AQ, O'Hern CS, Regan L. Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models. Proteins Structure Function And Bioinformatics 2014, 82: 2574-2584. PMID: 24912976, DOI: 10.1002/prot.24621.Peer-Reviewed Original ResearchIntrinsic α‐helical and β‐sheet conformational preferences: A computational case study of alanine
Caballero D, Määttä J, Zhou AQ, Sammalkorpi M, O'Hern CS, Regan L. Intrinsic α‐helical and β‐sheet conformational preferences: A computational case study of alanine. Protein Science 2014, 23: 970-980. PMID: 24753338, PMCID: PMC4088981, DOI: 10.1002/pro.2481.Peer-Reviewed Original Research
2012
The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val
Zhou AQ, O'Hern CS, Regan L. The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val. Biophysical Journal 2012, 102: 2345-2352. PMID: 22677388, PMCID: PMC3353012, DOI: 10.1016/j.bpj.2012.01.061.Peer-Reviewed Original ResearchALK1 Signaling Inhibits Angiogenesis by Cooperating with the Notch Pathway
Larrivée B, Prahst C, Gordon E, del Toro R, Mathivet T, Duarte A, Simons M, Eichmann A. ALK1 Signaling Inhibits Angiogenesis by Cooperating with the Notch Pathway. Developmental Cell 2012, 22: 489-500. PMID: 22421041, PMCID: PMC4047762, DOI: 10.1016/j.devcel.2012.02.005.Peer-Reviewed Original ResearchMeSH KeywordsActivin Receptors, Type IActivin Receptors, Type IIAnimalsArteriovenous MalformationsBasic Helix-Loop-Helix Transcription FactorsCell Cycle ProteinsDipeptidesDisease Models, AnimalGrowth Differentiation Factor 2Growth Differentiation FactorsHumansMiceMice, Inbred C57BLNeovascularization, PhysiologicReceptors, NotchRepressor ProteinsRetinaSignal TransductionSmad ProteinsTelangiectasia, Hereditary HemorrhagicVascular Endothelial Growth FactorsConceptsActivin receptor-like kinase 1Hereditary hemorrhagic telangiectasiaArteriovenous malformationsActivation of ALK1Receptor-like kinase 1Notch pathwayVascular lesionsHemorrhagic telangiectasiaPostnatal developmentInhibits angiogenesisNotch inhibitionTip cell formationReceptor familyAngiogenesisHypervascularizationALK1Kinase 1Cell formationEndothelial sproutingPatients
2011
Intravenous Ethanol Infusion Decreases Human Cortical γ-Aminobutyric Acid and N-Acetylaspartate as Measured with Proton Magnetic Resonance Spectroscopy at 4 Tesla
Gomez R, Behar KL, Watzl J, Weinzimer SA, Gulanski B, Sanacora G, Koretski J, Guidone E, Jiang L, Petrakis IL, Pittman B, Krystal JH, Mason GF. Intravenous Ethanol Infusion Decreases Human Cortical γ-Aminobutyric Acid and N-Acetylaspartate as Measured with Proton Magnetic Resonance Spectroscopy at 4 Tesla. Biological Psychiatry 2011, 71: 239-246. PMID: 21855054, PMCID: PMC3227760, DOI: 10.1016/j.biopsych.2011.06.026.Peer-Reviewed Original ResearchConceptsIntravenous ethanol infusionProton magnetic resonance spectroscopyEthanol infusionNAA levelsN-acetylaspartateCortical γ-aminobutyric acidAcute pharmacologic effectsLevels of GABAHealthy social drinkersBreath alcohol levelsN-acetylaspartyl-glutamateCortical GABAEthanol modulatesFirst infusionΓ-aminobutyric acidGABA levelsPharmacologic effectsBrain ethanolOccipital GABAInfusionAlcohol levelsMagnetic resonance spectroscopyReceptor functionBreath ethanolHuman cortexA bright approach to the immunoproteasome: Development of LMP2/β1i-specific imaging probes
Carmony K, Lee D, Wu Y, Lee N, Wehenkel M, Lee J, Lei B, Zhan C, Kim K. A bright approach to the immunoproteasome: Development of LMP2/β1i-specific imaging probes. Bioorganic & Medicinal Chemistry 2011, 20: 607-613. PMID: 21741845, PMCID: PMC3193892, DOI: 10.1016/j.bmc.2011.06.039.Peer-Reviewed Original Research
2009
Analysis of gene expression in PTHrP−/− mammary buds supports a role for BMP signaling and MMP2 in the initiation of ductal morphogenesis
Hens J, Dann P, Hiremath M, Pan T, Chodosh L, Wysolmerski J. Analysis of gene expression in PTHrP−/− mammary buds supports a role for BMP signaling and MMP2 in the initiation of ductal morphogenesis. Developmental Dynamics 2009, 238: 2713-2724. PMID: 19795511, PMCID: PMC2862621, DOI: 10.1002/dvdy.22097.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBone Morphogenetic Protein 4Cells, CulturedDipeptidesDown-RegulationGene Expression Regulation, DevelopmentalHydroxamic AcidsIntercellular Signaling Peptides and ProteinsKeratinsMammary Glands, AnimalMatrix Metalloproteinase 2Matrix Metalloproteinase InhibitorsMesodermMiceMice, KnockoutMorphogenesisOligonucleotide Array Sequence AnalysisParathyroid Hormone-Related ProteinProtease InhibitorsSignal TransductionTranscription FactorsUp-RegulationConceptsGene expressionMammary budMammary mesenchymeDuctal outgrowthMesenchymal cellsEmbryonic mammary developmentMMP2 gene expressionEmbryonic mammary budFunctional roleGenesDuctal morphogenesisBud culturesMammary developmentBudsPTHrP effectsBMPMesenchymeExpressionMMP2 activityMMP2OutgrowthVentral skinCellsMorphogenesisBMP4
2008
Therapeutic efficacy of SJA6017, a calpain inhibitor, in rat spinal cord injury
Akdemir O, Uçankale M, Karaoğlan A, Barut Ş, Sağmanligil A, Bilguvar K, Çirakoğlu B, Şahan E, Çolak A. Therapeutic efficacy of SJA6017, a calpain inhibitor, in rat spinal cord injury. Journal Of Clinical Neuroscience 2008, 15: 1130-1136. PMID: 18656362, DOI: 10.1016/j.jocn.2007.08.011.Peer-Reviewed Original ResearchConceptsSpinal cord injuryGroup 3 ratsCord injuryRat spinal cord injury modelGrading scaleRat spinal cord injurySpinal cord injury modelApoptotic cell deathSpinal cord traumaGroup 2 ratsFeasible therapeutic strategySpinal cord tissueWistar albino ratsNecrosis 24 hCell deathTarlov scoreModerate traumaCord traumaNeuroprotective effectsFunctional recoveryFunctional outcomeLimb functionNeurological performanceWidespread edemaInjury modelCathepsin B Is Involved in the Trafficking of TNF-α-Containing Vesicles to the Plasma Membrane in Macrophages
Ha S, Martins A, Khazaie K, Han J, Chan B, Kim S. Cathepsin B Is Involved in the Trafficking of TNF-α-Containing Vesicles to the Plasma Membrane in Macrophages. The Journal Of Immunology 2008, 181: 690-697. PMID: 18566436, DOI: 10.4049/jimmunol.181.1.690.Peer-Reviewed Original ResearchConceptsPlasma membraneIntracellular cathepsin B activityCathepsin BCathepsin B activityMouse bone marrow-derived macrophagesGene identification methodsBone marrow-derived macrophagesMarrow-derived macrophagesB activityEctopic expressionLysosomal cysteine proteinasesInnate immune responsePosttranslational processingCysteine proteinasesTNF-alphaVesiclesKey mediatorMembranePotent proinflammatory cytokineLess TNF-alphaChronic inflammatory diseaseMacrophagesMutagenesisGFPMicrobes
2007
Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*
Sánchez-Sánchez F, Martínez-Redondo F, Aroca-Aguilar JD, Coca-Prados M, Escribano J. Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*. Journal Of Biological Chemistry 2007, 282: 27810-27824. PMID: 17650508, DOI: 10.1074/jbc.m609608200.Peer-Reviewed Original ResearchConceptsExtracellular calciumCalpain IICalcium-activated proteaseIntraocular pressureT cellsIntracellular proteolytic cleavageCalpain inhibitorsCalcium uptakeProteolytic cleavageCalpain inhibitor IVOlfactomedin-like domainCalpain IInhibitor IVMyocilinEndoplasmic reticulumIntracellular processingLumenRNA interference knockdownCalciumProteolytic processingCellsCulture mediumGlaucomaSubcellular fractionationEndoproteolytic processing
2005
Glutamate Cysteine Ligase Catalysis DEPENDENCE ON ATP AND MODIFIER SUBUNIT FOR REGULATION OF TISSUE GLUTATHIONE LEVELS*
Chen Y, Shertzer HG, Schneider SN, Nebert DW, Dalton TP. Glutamate Cysteine Ligase Catalysis DEPENDENCE ON ATP AND MODIFIER SUBUNIT FOR REGULATION OF TISSUE GLUTATHIONE LEVELS*. Journal Of Biological Chemistry 2005, 280: 33766-33774. PMID: 16081425, DOI: 10.1074/jbc.m504604200.Peer-Reviewed Original Research
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