2020
Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells
De La Cena K, Ho R, Amraei R, Woolf N, Tashjian J, Zhao Q, Richards S, Walker J, Huang J, Chitalia V, Rahimi N. Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells. American Journal Of Pathology 2020, 191: 157-167. PMID: 33129760, PMCID: PMC7788663, DOI: 10.1016/j.ajpath.2020.09.015.Peer-Reviewed Original ResearchConceptsCell cycleColorectal cancerCell cycle checkpoint arrestCell cycle inhibitor proteinsNovel tumor suppressor geneFull molecular mechanismsPutative tumor suppressorColon cancer cellsTumor suppressor geneG2/M phaseSporadic human colorectal cancerNormal intestinal epithelial cellsEpigenetic mechanismsCheckpoint arrestTMIGD1Inhibitor proteinNovel potential therapeutic targetIntestinal epithelial cellsMolecular mechanismsTumor suppressorPoor overall survivalSuppressor geneDevelopment of adenomasImmunoglobulin domainHuman colorectal cancer
2014
Regulation of Rac1 translocation and activation by membrane domains and their boundaries
Moissoglu K, Kiessling V, Wan C, Hoffman BD, Norambuena A, Tamm LK, Schwartz MA. Regulation of Rac1 translocation and activation by membrane domains and their boundaries. Journal Of Cell Science 2014, 127: 2565-2576. PMID: 24695858, PMCID: PMC4038948, DOI: 10.1242/jcs.149088.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneFluorescence Resonance Energy TransferGTPase-Activating ProteinsHEK293 CellsHumansMembrane MicrodomainsMiceNIH 3T3 CellsProtein BindingProtein Transportrac1 GTP-Binding Proteinrho-Specific Guanine Nucleotide Dissociation InhibitorsSignal TransductionUnilamellar LiposomesConceptsFluorescence resonance energy transferMembrane domainsRac1 translocationGDP dissociation inhibitor proteinLiquid-ordered membrane domainsGTPase-activating proteinsNon-raft regionsNon-raft domainsBinding of Rac1Activation of Rac1Single-molecule analysisGTP loadingRho GTPasesLipid raftsRac1 localizationRho GTPaseInhibitor proteinResult of inactivationRac1Resonance energy transferFunctional studiesNovel mechanismLipid bilayersTranslocationRafts
2003
Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum
Del Valle A, Jones BF, Harrison LM, Chadderdon RC, Cappello M. Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum. Molecular And Biochemical Parasitology 2003, 129: 167-177. PMID: 12850261, DOI: 10.1016/s0166-6851(03)00121-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAncylostomaAnimalsAntibodies, HelminthChromatography, High Pressure LiquidCloning, MolecularCollagenDNA, ComplementaryFibrinogenHelminth ProteinsImmunoglobulin GImmunohistochemistryIntegrin alpha2beta1Molecular Sequence DataPlatelet Aggregation InhibitorsPlatelet Glycoprotein GPIIb-IIIa ComplexRecombinant ProteinsSpectrometry, Mass, Electrospray IonizationConceptsIron deficiency anemiaCell surface integrin receptorsIdentical N-terminalAmino acid sequence homologyAmino acid sequenceSingle gene productSurface integrin receptorsDeficiency anemiaMammalian hemostasisCorresponding native proteinsCDNA correspondingSignificant homologyMolecular cloningSimilar molecular massSecreted proteinsGene productsSequence homologyAcid sequenceInhibitor proteinHPI proteinVaccine-based strategiesNative proteinN-terminalAdult Ancylostoma caninumAdult stage
2002
The IκB-NF-κB Signaling Module: Temporal Control and Selective Gene Activation
Hoffmann A, Levchenko A, Scott M, Baltimore D. The IκB-NF-κB Signaling Module: Temporal Control and Selective Gene Activation. Science 2002, 298: 1241-1245. PMID: 12424381, DOI: 10.1126/science.1071914.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell NucleusChemokine CCL5Chemokine CXCL10Chemokines, CXCComputer SimulationCytoplasmDNA-Binding ProteinsElectrophoretic Mobility Shift AssayFeedback, PhysiologicalGene Expression RegulationHumansI-kappa B ProteinsMiceMice, KnockoutModels, BiologicalNF-kappa BNF-KappaB Inhibitor alphaProto-Oncogene ProteinsSignal TransductionTranscriptional ActivationTumor Cells, CulturedTumor Necrosis Factor-alphaConceptsTranscriptional activator NF-kappaBSelective gene activationKnockout cell linesTemporal controlNF-kappaB inhibitor proteinNF-kappaB responseSignaling modulesCoordinated degradationGene activationMammalian cellsNuclear localizationInhibitor proteinGene expressionIkappaB proteinsSignal-processing characteristicsEpsilon functionNF-kappaB activationCell linesNF-kappaB
2001
Protein phosphatase 1 regulation by inhibitors and targeting subunits
Watanabe T, Huang H, Horiuchi A, da Cruze Silva E, Hsieh-Wilson L, Allen P, Shenolikar S, Greengard P, Nairn A. Protein phosphatase 1 regulation by inhibitors and targeting subunits. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3080-3085. PMID: 11248035, PMCID: PMC30610, DOI: 10.1073/pnas.051003898.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsGene ExpressionHistone ChaperonesMicrofilament ProteinsMolecular Sequence DataMyelin Basic ProteinNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1ProteinsRabbitsRecombinant Fusion ProteinsSpodopteraSubstrate SpecificityTranscription FactorsConceptsProtein phosphatase 1Native protein phosphatase-1PP1 nuclear targeting subunitPhosphotyrosine-containing substratesInhibitor 2Protein phosphatase 1 regulationRecombinant protein phosphatase 1Sf9 insect cellsC-terminal sequencesLoss of interactionTargeting subunitPP1/Phosphatase 1Insect cellsResidues 274Inhibitor proteinRecombinant proteinsProtein inhibitorSubunitsEscherichia coliY272Corresponding regionPhosphorylase a.MutationsRegulation
1997
Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
Kwon Y, Huang H, Desdouits F, Girault J, Greengard P, Nairn A. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3536-3541. PMID: 9108011, PMCID: PMC20474, DOI: 10.1073/pnas.94.8.3536.Peer-Reviewed Original ResearchConceptsPP-1cPP-1C.PP-1DARPP-32Inhibitor 2Protein phosphatase 1Amino acid sequence analysisAmino acid residuesNH2-terminal regionAcid sequence analysisPhosphoinhibitor-1Threonine residuesPhosphatase 1Inhibitor-1Catalytic subunitCalyculin AOkadaic acidInhibitor proteinActive siteAcid residuesSequence analysisProteinEnzyme activityMotifResidues
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