2023
Amino-terminal proteolytic fragment of the axon growth inhibitor Nogo-A (Rtn4A) is upregulated by injury and promotes axon regeneration
Sekine Y, Wang X, Kikkawa K, Honda S, Strittmatter S. Amino-terminal proteolytic fragment of the axon growth inhibitor Nogo-A (Rtn4A) is upregulated by injury and promotes axon regeneration. Journal Of Biological Chemistry 2023, 299: 105232. PMID: 37690690, PMCID: PMC10622843, DOI: 10.1016/j.jbc.2023.105232.Peer-Reviewed Original ResearchConceptsAxon regenerationCentral nervous system injuryPersistent neurological deficitsCerebral cortical neuronsNervous system injuryNeurological deficitsSystem injuryCNS injuryCortical neuronsAmino-terminal fragmentInjuryExtracellular actionPhysiological productionNogoInhibitory proteinMiceNeuronsInhibitory domainOverexpression increasesVaried resultsProteolytic fragmentsAxotomyExpressionNogoAGene targeting
2021
NogoA-expressing astrocytes limit peripheral macrophage infiltration after ischemic brain injury in primates
Boghdadi AG, Spurrier J, Teo L, Li M, Skarica M, Cao B, Kwan WC, Merson TD, Nilsson SK, Sestan N, Strittmatter SM, Bourne JA. NogoA-expressing astrocytes limit peripheral macrophage infiltration after ischemic brain injury in primates. Nature Communications 2021, 12: 6906. PMID: 34824275, PMCID: PMC8617297, DOI: 10.1038/s41467-021-27245-0.Peer-Reviewed Original ResearchConceptsBrain injuryPeripheral macrophage infiltrationIschemic brain injuryAnti-inflammatory responseMajority of astrocytesNeurite outgrowth inhibitory proteinIschemic strokePeripheral macrophagesReactive astrocytesMacrophage infiltrationStroke recoveryAstrocyte clustersMarmoset monkeysVisual cortexAstrocytesNogoASingle-nucleus transcriptomicsInhibitory proteinInjuryStrokeHuman brainInfiltrationCritical rolePrecise functionOligodendrocytes(E)-N-(2-(3, 5-Dimethoxystyryl) phenyl) furan-2-carboxamide (BK3C231) induces cytoprotection in CCD18-Co human colon fibroblast cells through Nrf2/ARE pathway activation
Tan H, Thomas N, Inayat-Hussain S, Chan K. (E)-N-(2-(3, 5-Dimethoxystyryl) phenyl) furan-2-carboxamide (BK3C231) induces cytoprotection in CCD18-Co human colon fibroblast cells through Nrf2/ARE pathway activation. Scientific Reports 2021, 11: 4773. PMID: 33637843, PMCID: PMC7910600, DOI: 10.1038/s41598-021-83163-7.Peer-Reviewed Original ResearchConceptsGlutamate-cysteine ligase catalytic subunitGlutathione S-transferaseNrf2/ARE pathway activationDissociation of Nrf2New mechanistic insightsCatalytic subunitNrf2/ARE pathwayN-furanPromoter activityMolecular mechanismsResponse elementCytoprotective proteinsInhibitory proteinS-transferaseQuinone oxidoreductase 1Mitochondrial damageCytoprotective enzymesMechanistic insightsARE pathwayProtein expressionFactor 2Pathway activationNuclear factorNormal cellsFibroblast cells
2020
Control of Murine Primordial Follicle Growth Activation by IκB/NFκB Signaling
Wright CJ, Cari EL, Sandoval J, Bales E, Sam PK, Zarate MA, Polotsky AJ, Kallen AN, Johnson J. Control of Murine Primordial Follicle Growth Activation by IκB/NFκB Signaling. Reproductive Sciences 2020, 27: 2063-2074. PMID: 32542534, PMCID: PMC7529825, DOI: 10.1007/s43032-020-00225-3.Peer-Reviewed Original ResearchConceptsPrimordial follicle growth activationLargest human genome-wide association studyGrowth activationHuman genome-wide association studiesGenome-wide association studiesLigand/receptor interactionsTranscription factor NFκBInhibitory protein IκBαAssociation studiesIκB proteinsWild-type controlsInhibitory proteinProtein IκBαPrimordial stageNFκB signalingMechanistic insightsReceptor interactionProteinMurine ovariesNFκB pathwayKey membersNFκBSubunit p65NFκB activationIκBβ
2010
A novel role for PTEN in the inhibition of neurite outgrowth by myelin-associated glycoprotein in cortical neurons
Perdigoto AL, Chaudhry N, Barnes GN, Filbin MT, Carter BD. A novel role for PTEN in the inhibition of neurite outgrowth by myelin-associated glycoprotein in cortical neurons. Molecular And Cellular Neuroscience 2010, 46: 235-244. PMID: 20869442, PMCID: PMC3018674, DOI: 10.1016/j.mcn.2010.09.006.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCerebral CortexCHO CellsCoculture TechniquesCricetinaeCricetulusHEK293 CellsHumansMiceMice, Inbred C57BLMice, KnockoutMyelin-Associated GlycoproteinNeuritesNeuronsProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseReceptor, Nerve Growth Factorrho GTP-Binding Proteinsrho-Associated KinasesConceptsCortical neuronsInhibitory effectNeurite outgrowthEffect of MAGP75 neurotrophin receptorPI3K/AKT axisCentral nervous systemPTEN/PI3K/AKT axisAxonal regenerationCorticospinal tractPermanent disabilityNeurotrophin receptorNervous systemAKT axisPhospho-AktNeuronsStriking reductionProcess outgrowthDownstream effector kinasesMyelinInhibitory proteinNovel rolePTENReceptorsNovel pathway
2009
Inhibition of Neutrophil Function by Two Tick Salivary Proteins
Guo X, Booth CJ, Paley MA, Wang X, DePonte K, Fikrig E, Narasimhan S, Montgomery RR. Inhibition of Neutrophil Function by Two Tick Salivary Proteins. Infection And Immunity 2009, 77: 2320-2329. PMID: 19332533, PMCID: PMC2687334, DOI: 10.1128/iai.01507-08.Peer-Reviewed Original ResearchConceptsPolymorphonuclear leukocytesPMN functionNumber of PMNPMN integrinsPMN adherenceNeutrophil functionSpirochete burdenTick salivary proteinsTick salivaLyme diseaseTick attachmentSalivary glandsBorrelia burgdorferiTick feedingCausative agentReduced levelsInhibitory proteinSalivaBlood mealAntihemostatic activityInfectionInhibitionSalivary proteinsHematophagous arthropodsTick Ixodes scapularis
2004
Nogo-66 Receptor Prevents Raphespinal and Rubrospinal Axon Regeneration and Limits Functional Recovery from Spinal Cord Injury
Kim JE, Liu BP, Park JH, Strittmatter SM. Nogo-66 Receptor Prevents Raphespinal and Rubrospinal Axon Regeneration and Limits Functional Recovery from Spinal Cord Injury. Neuron 2004, 44: 439-451. PMID: 15504325, DOI: 10.1016/j.neuron.2004.10.015.Peer-Reviewed Original ResearchMeSH Keywords5,7-DihydroxytryptamineAnimalsAxonsBehavior, AnimalBlotting, NorthernBlotting, SouthernBrainCell CountCells, CulturedCloning, MolecularCornified Envelope Proline-Rich ProteinsDesipramineDisease Models, AnimalEvoked Potentials, MotorFemaleGanglia, SpinalGlial Fibrillary Acidic ProteinGlucoseGPI-Linked ProteinsGrowth ConesImmunohistochemistryMiceMice, Inbred C57BLMice, KnockoutMotor ActivityMyelin ProteinsMyelin SheathMyelin-Associated GlycoproteinNerve RegenerationNeuronsNogo ProteinsNogo Receptor 1Phospholipid EthersProteinsPyramidal TractsReceptors, Cell SurfaceRecovery of FunctionSerotoninSerotonin AgentsSpinal CordSpinal Cord InjuriesTime FactorsConceptsAdult CNSNogo-66Spinal cord injuryAdult mammalian CNSNogo-66 receptorDorsal hemisectionDRG neuronsFunctional recoveryRubrospinal fibersCord injuryMyelin inhibitorsComplete transectionCorticospinal fibersMotor functionSpinal cordMotor impairmentAxon regenerationMammalian CNSAxonal growthAxonal outgrowthCNS myelinMiceInhibitory proteinInjuryGrowth cones
2002
Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact
Wang X, Chun SJ, Treloar H, Vartanian T, Greer CA, Strittmatter SM. Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact. Journal Of Neuroscience 2002, 22: 5505-5515. PMID: 12097502, PMCID: PMC6758202, DOI: 10.1523/jneurosci.22-13-05505.2002.Peer-Reviewed Original ResearchConceptsAdult CNSLimited axonal regenerationSpinal cord injuryNogo-66 receptorInteraction of NogoAxonal plasticityCord injurySynaptic contactsAxonal regenerationNgR proteinMyelinated fibersPostnatal neuronsLocalization of NogoMyelinated axonsAxonal growthOligodendrocyte surfacePhysiologic roleAxonsNogoProtein expressionNeuronsReceptorsInhibitory proteinInjuryCNS
2000
Xenotransplantation of transgenic pig olfactory ensheathing cells promotes axonal regeneration in rat spinal cord
Imaizumi T, Lankford K, Burton W, Fodor W, Kocsis J. Xenotransplantation of transgenic pig olfactory ensheathing cells promotes axonal regeneration in rat spinal cord. Nature Biotechnology 2000, 18: 949-953. PMID: 10973214, PMCID: PMC2605371, DOI: 10.1038/79432.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedAxonsCD59 AntigensCell SeparationElectrophysiologyFlow CytometryFluorescent Antibody Technique, IndirectHumansImmunosuppression TherapyModels, BiologicalOlfactory NerveRatsRats, WistarRegenerationSchwann CellsSciatic NerveSpinal CordSwineTransgenesTransplantation, HeterologousConceptsAxonal regenerationSpinal cordSchwann cellsImpulse conductionLesion-control ratsDorsal column lesionTransplantation of olfactoryRat spinal cordConduction velocity measurementsComplement inhibitory proteinsHyperacute responseRegenerated axonsImmunosuppressed ratsTransection siteLesion sitePeripheral patternHost tractCordNormal axonsDonor cellsAxonsInhibitory proteinRatsDonor cell typeTransgenic pigs
1999
Expression of p-27 (kip1) in Nevi and Melanomas
Morgan M, Cowper S. Expression of p-27 (kip1) in Nevi and Melanomas. American Journal Of Dermatopathology 1999, 21: 121-124. PMID: 10218670, DOI: 10.1097/00000372-199904000-00002.Peer-Reviewed Original ResearchConceptsExpression of p27Melanocytic lesionsSpitz neviDistribution of immunoreactivityP27 labeling indexMinority of casesCell cycle inhibitory proteinsChart reviewMalignant melanocytic lesionsClinical historyDiagnostic challengeBiologic behaviorHistopathologic criteriaLabeling indexCompound neviLogistic regressionHuman neoplasmsNeviNuclear stainingLesionsMelanomaP27Inhibitory proteinAccurate distinctionSkin
1997
Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
Huang H, Horiuchi A, Goldberg J, Greengard P, Nairn A. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3530-3535. PMID: 9108010, PMCID: PMC20473, DOI: 10.1073/pnas.94.8.3530.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Site-directed mutagenesisActive site residuesOkadaic acidPhosphatase 1Calyculin AMammalian protein phosphatase 1PP-1Site residuesEnzyme activityMutation of residuesAmino acid residuesMechanism of catalysisActive siteInhibitor bindingAcid residuesInhibitory proteinMutationsResiduesMutagenesisDivalent cationsToxinY272Large lossesR221
1994
A granulocyte inhibitory protein overexpressed in chronic renal disease regulates expression of interleukin 6 and interleukin 8.
Ziesche R, Roth M, Papakonstantinou E, Nauck M, Hörl W, Kashgarian M, Block L. A granulocyte inhibitory protein overexpressed in chronic renal disease regulates expression of interleukin 6 and interleukin 8. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 301-305. PMID: 8278382, PMCID: PMC42935, DOI: 10.1073/pnas.91.1.301.Peer-Reviewed Original ResearchConceptsGranulocyte inhibitory proteinsInterleukin-6Chronic renal diseaseChronic renal failureProgression of glomerulosclerosisHuman mesangial cellsInhibitory proteinPluripotential effectsRenal failureRenal diseaseCytokine expressionIL-6IL-8Interleukin-8Inflammatory reactionGIP resultsGlomerular responseMesangial cellsC-jun mRNAC-fos geneC-JunDe novo synthesisNovo synthesisExpressionOverall effect
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