2023
HOXC6 drives a therapeutically targetable pancreatic cancer growth and metastasis pathway by regulating MSK1 and PPP2R2B
Malvi P, Chava S, Cai G, Hu K, Zhu L, Edwards Y, Green M, Gupta R, Wajapeyee N. HOXC6 drives a therapeutically targetable pancreatic cancer growth and metastasis pathway by regulating MSK1 and PPP2R2B. Cell Reports Medicine 2023, 4: 101285. PMID: 37951219, PMCID: PMC10694669, DOI: 10.1016/j.xcrm.2023.101285.Peer-Reviewed Original ResearchConceptsPancreatic ductal adenocarcinomaHomeobox C6PDAC growthInsulin-like growth factor 1 receptorGrowth factor 1 receptorKinase MSK1Factor 1 receptorTranscription factorsPancreatic cancer growthMSK1Tumor growthPDAC tumor growthMost pancreatic ductal adenocarcinomasMammalian targetIGF1R inhibitorsTherapeutic vulnerabilitiesRapamycin (mTOR) pathway activationMEK inhibitor trametinibMetastasis pathwaysPDAC mouse modelPDAC cellsMTOR inhibitionPharmacological inhibitionPathway activationInhibition blocksPaclitaxel With or Without Cixutumumab as Second-Line Treatment of Metastatic Esophageal or Gastroesophageal Junction Cancer: A Randomized Phase II ECOG-ACRIN Trial
Stockton S, Catalano P, Cohen S, Burtness B, Mitchell E, Dotan E, Lubner S, Kumar P, Mulcahy M, Fisher G, Crandall T, Benson A. Paclitaxel With or Without Cixutumumab as Second-Line Treatment of Metastatic Esophageal or Gastroesophageal Junction Cancer: A Randomized Phase II ECOG-ACRIN Trial. The Oncologist 2023, 28: 827-e822. PMID: 37104870, PMCID: PMC10485278, DOI: 10.1093/oncolo/oyad096.Peer-Reviewed Original ResearchConceptsProgression-free survivalSecond-line therapyGastroesophageal junction cancerArm AMetastatic esophagealJunction cancerArm BMedian progression-free survivalRandomized phase II trialMedian overall survivalObjective response rateSecond-line treatmentAdvanced esophageal cancerInsulin-like growth factor 1 receptorPhase II trialStandard of careGrowth factor 1 receptorFactor 1 receptorStable diseaseII trialMetastatic settingPrimary endpointOverall survivalPreclinical evidenceClinical outcomes18F-Labeled o‑aminopyridyl alkynyl radioligands targeting colony-stimulating factor 1 receptor for neuroinflammation imaging
An X, Wang J, Tong L, Zhang X, Fu H, Zhang J, Xie H, Huang Y, Jia H. 18F-Labeled o‑aminopyridyl alkynyl radioligands targeting colony-stimulating factor 1 receptor for neuroinflammation imaging. Bioorganic & Medicinal Chemistry 2023, 83: 117233. PMID: 36933438, DOI: 10.1016/j.bmc.2023.117233.Peer-Reviewed Original ResearchConceptsBrain of lipopolysaccharideMale ICR miceModerate brain uptakeFactor 1 receptorColony-stimulating factor 1 receptorBrain uptakeICR miceGBq/Metabolic stability studiesID/Neuroinflammation imagingMouse brainBiodistribution studiesNanomolar inhibitory potencyReceptor ligandsMiceInhibitory potencySpecific bindingBrainCSF-1RRadiochemical purityMolar activity
2022
Hyperinsulinemia induces early and dyssynchronous puberty in lean female mice.
Saleh FL, Joshi AA, Tal A, Xu P, Hens J, Wong SL, Flannery C. Hyperinsulinemia induces early and dyssynchronous puberty in lean female mice. Journal Of Endocrinology 2022, 254: 121-135. PMID: 35904489, PMCID: PMC9837806, DOI: 10.1530/joe-21-0447.Peer-Reviewed Original ResearchConceptsVaginal openingInsulin resistanceDay of VOIGF-1 levelsInsulin-like growth factor 1 receptorGreater insulin resistanceHigher insulin levelsEffect of hyperinsulinemiaGrowth factor 1 receptorGonadotropin-releasing hormoneLower body weightFactor 1 receptorReceptor isoform expressionMammary gland developmentLH levelsInsulin levelsInsulin receptor isoform expressionKisspeptin expressionChildhood obesityFemale miceHormone levelsEarly initiationHyperinsulinemiaBody weightOvarian follicles
2019
Selective inhibition of N-linked glycosylation impairs receptor tyrosine kinase processing
Klaver E, Zhao P, May M, Flanagan-Steet H, Freeze HH, Gilmore R, Wells L, Contessa J, Steet R. Selective inhibition of N-linked glycosylation impairs receptor tyrosine kinase processing. Disease Models & Mechanisms 2019, 12: dmm039602. PMID: 31101650, PMCID: PMC6602306, DOI: 10.1242/dmm.039602.Peer-Reviewed Original ResearchConceptsNull cellsReceptor processingEndoplasmic reticulum localizationGlycan site occupancyInsulin-like growth factor 1 receptorReceptor tyrosine kinasesGrowth factor 1 receptorFactor 1 receptorCell surface glycoproteinMutant cellsNGI-1Catalytic subunitReceptor kinaseGlycosylation statusReduced abundanceTyrosine kinaseGlycan occupancyTyrosine receptor kinaseSurface localizationInsulin receptorAbnormal glycosylationProteolytic processingFunctional consequencesCell surfaceGlycosylationModeling cell line-specific recruitment of signaling proteins to the insulin-like growth factor 1 receptor
Erickson KE, Rukhlenko OS, Shahinuzzaman M, Slavkova KP, Lin YT, Suderman R, Stites EC, Anghel M, Posner RG, Barua D, Kholodenko BN, Hlavacek WS. Modeling cell line-specific recruitment of signaling proteins to the insulin-like growth factor 1 receptor. PLOS Computational Biology 2019, 15: e1006706. PMID: 30653502, PMCID: PMC6353226, DOI: 10.1371/journal.pcbi.1006706.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesSrc homology 2Autophosphorylation sitesInsulin-like growth factor 1 receptorGrowth factor 1 receptorFactor 1 receptorPTB domain-containing proteinsCopy numberDomain-containing proteinsPhosphotyrosine-binding (PTB) domainProtein copy numbersMultiple autophosphorylation sitesProtein abundance profilesMultiple signaling proteinsShort linear motifsOutcome of competitionCell line-specific modelsHomology 2Cytoplasmic domainSignaling proteinsLinear motifsTyrosine kinaseEffects of competitionRule-based modeling approachRelative abundance
2018
Ablation of insulin receptor substrates 1 and 2 suppresses Kras-driven lung tumorigenesis
Xu H, Lee M, Tsai P, Adler A, Curry N, Challa S, Freinkman E, Hitchcock D, Copps K, White M, Bronson R, Marcotrigiano M, Wu Y, Clish C, Kalaany N. Ablation of insulin receptor substrates 1 and 2 suppresses Kras-driven lung tumorigenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 4228-4233. PMID: 29610318, PMCID: PMC5910837, DOI: 10.1073/pnas.1718414115.Peer-Reviewed Original ResearchMeSH KeywordsA549 CellsAmino AcidsAnimalsAutophagyCarcinogenesisCarcinoma, Non-Small-Cell LungCodon, TerminatorGenes, rasHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor ILung NeoplasmsMiceNeoplasm ProteinsProteolysisProto-Oncogene Proteins c-aktProto-Oncogene Proteins p21(ras)Signal TransductionConceptsIR/IGF1RLung cancerLung tumorigenesisInsulin receptorTumor cellsInsulin-like growth factor 1 receptorCell lung cancerGrowth factor 1 receptorHuman NSCLC cellsEffective therapeutic strategyLung cancer initiationIntracellular levelsKirsten rat sarcomaFactor 1 receptorTumor burdenCancer deathLeading causeMutant NSCLCNSCLC cellsIGF1R inhibitionMouse modelTherapeutic strategiesInsulin/IGF1Acute lossRat sarcoma
2014
Insulin Receptor Substrates Are Essential for the Bioenergetic and Hypertrophic Response of the Heart to Exercise Training
Riehle C, Wende A, Zhu Y, Oliveira K, Pereira R, Jaishy B, Bevins J, Valdez S, Noh J, Kim B, Moreira A, Weatherford E, Manivel R, Rawlings T, Rech M, White M, Abel E. Insulin Receptor Substrates Are Essential for the Bioenergetic and Hypertrophic Response of the Heart to Exercise Training. Molecular And Cellular Biology 2014, 34: 3450-3460. PMID: 25002528, PMCID: PMC4135616, DOI: 10.1128/mcb.00426-14.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEnergy MetabolismGene Expression RegulationGlycogenHeartInsulin Receptor Substrate ProteinsMiceMice, Inbred C57BLMice, KnockoutMitochondriaPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPhosphatidylinositol 3-KinasesProtein IsoformsSignal TransductionSwimmingTranscription FactorsConceptsInsulin receptor substrate-1IRS isoformsProtein phosphatase 2AReceptor substrate-1Insulin receptor substrateInsulin-like growth factor 1 receptorGrowth factor 1 receptorSynthase kinase-3βPeroxisome proliferator-activated receptor gamma coactivatorPhosphatase 2AProliferator-activated receptor gamma coactivatorFactor 1 receptorPGC-1α protein contentCardiomyocyte-specific deletionDevelopmental regulationProtein contentHypertrophic responseReceptor substrateReceptor gamma coactivatorFatty acid oxidationSubstrate-1Kinase-3βDivergent rolesMetabolic adaptationNonredundant rolePrognostic Biomarkers in Phase II Trial of Cetuximab-Containing Induction and Chemoradiation in Resectable HNSCC: Eastern Cooperative Oncology Group E2303
Psyrri A, Lee JW, Pectasides E, Vassilakopoulou M, Kosmidis EK, Burtness BA, Rimm DL, Wanebo HJ, Forastiere AA. Prognostic Biomarkers in Phase II Trial of Cetuximab-Containing Induction and Chemoradiation in Resectable HNSCC: Eastern Cooperative Oncology Group E2303. Clinical Cancer Research 2014, 20: 3023-3032. PMID: 24700741, PMCID: PMC4049169, DOI: 10.1158/1078-0432.ccr-14-0113.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAntibodies, Monoclonal, HumanizedAntineoplastic Combined Chemotherapy ProtocolsBiomarkers, TumorCarboplatinCarcinoma, Squamous CellCetuximabChemoradiotherapyDisease-Free SurvivalDrug Resistance, NeoplasmFemaleFluorescent Antibody TechniqueHead and Neck NeoplasmsHumansInduction ChemotherapyKaplan-Meier EstimateMaleMiddle AgedMitogen-Activated Protein Kinase KinasesPaclitaxelPhosphatidylinositol 3-KinasesPrognosisProportional Hazards ModelsProto-Oncogene Proteins c-aktras ProteinsSignal TransductionSquamous Cell Carcinoma of Head and NeckTissue Array AnalysisConceptsProgression-free survivalEvent-free survivalPhase II trialOverall survivalII trialTissue microarrayStage III/IV headMultivariable Cox proportional hazards modelsMultivariable Cox regression analysisNeck squamous cell cancerRAS/MAPK/ERKCox proportional hazards modelInsulin-like growth factor 1 receptorLarge prospective studiesCox regression analysisInferior overall survivalKaplan-Meier methodSquamous cell cancerLog-rank testGrowth factor 1 receptorProportional hazards modelPI3K/Akt pathwayFactor 1 receptorPI3K/AktEGF receptor
2013
Esophageal carcinoma
Boland PM, Burtness B. Esophageal carcinoma. Current Opinion In Oncology 2013, 25: 417-424. PMID: 23680713, DOI: 10.1097/cco.0b013e328362105e.Peer-Reviewed Original ResearchConceptsEsophageal cancerT-lymphocyte antigen-4Platinum-based regimensSubgroup of patientsVascular endothelial growth factorGrowth factor 1 receptorImproved patient selectionEndothelial growth factorEpidermal growth factor receptorMinimal additional benefitFactor 1 receptorProminent molecular targetsGrowth factor receptorStandard cytotoxicChemotherapeutic regimenSurvival benefitPatient selectionEsophagogastric junctionTherapeutic regimensAntigen-4Esophageal carcinomaClinical investigationEncouraging dataMulticenter effortsEarly benefits
2012
Activity of insulin growth factor-receptor (IGF-1R) antibody cixutumumab combined with the mTOR inhibitor temsirolimus in patients with metastatic refractory adrenocortical carcinoma.
Naing A, LoRusso P, Fu S, Hong D, Chen H, Doyle L, Phan A, Habra M, Kurzrock R. Activity of insulin growth factor-receptor (IGF-1R) antibody cixutumumab combined with the mTOR inhibitor temsirolimus in patients with metastatic refractory adrenocortical carcinoma. Journal Of Clinical Oncology 2012, 30: 4639-4639. DOI: 10.1200/jco.2012.30.15_suppl.4639.Peer-Reviewed Original ResearchIGF-1R inhibitorsAdrenocortical carcinomaStable diseaseHuman IgG1 monoclonal antibodyProlonged stable diseaseGrowth factor receptor antibodyEffective systemic chemotherapyGrowth factor 1 receptorInsulin growth factor-1 receptorMTOR inhibitor temsirolimusFactor 1 receptorIgG1 monoclonal antibodyPrior therapyFrequent toxicitiesSystemic chemotherapyMedian agePreclinical dataMedian numberTemsirolimusPatientsCixutumumabMTOR pathwayGrade 1Monoclonal antibodiesCarcinoma
2009
Mammalian target of rapamycin regulates vascular endothelial growth factor–dependent liver cyst growth in polycystin‐2–defective mice
Spirli C, Okolicsanyi S, Fiorotto R, Fabris L, Cadamuro M, Lecchi S, Tian X, Somlo S, Strazzabosco M. Mammalian target of rapamycin regulates vascular endothelial growth factor–dependent liver cyst growth in polycystin‐2–defective mice. Hepatology 2009, 51: 1778-1788. PMID: 20131403, PMCID: PMC2930014, DOI: 10.1002/hep.23511.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCystsDisease Models, AnimalExtracellular Signal-Regulated MAP KinasesHypoxia-Inducible Factor 1, alpha SubunitInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsLiver DiseasesMicePolycystic Kidney, Autosomal DominantProtein Serine-Threonine KinasesSirolimusTOR Serine-Threonine KinasesTRPP Cation ChannelsVascular Endothelial Growth Factor AConceptsMammalian targetInsulin-like growth factor-1Extracellular signal-regulated kinase 1/2Extracellular signal-regulated kinaseSignal-regulated kinase 1/2Autosomal dominant polycystic kidney diseaseLiver cyst growthVascular endothelial growth factorProtein kinase AInsulin-like growth factor 1 receptorSignal-regulated kinaseGrowth factor 1 receptorVEGF secretionCyst growthMTOR inhibitor rapamycinFactor 1 receptorHIF1alpha accumulationFactor 1 alphaDependent phosphorylationKinase AKinase 1/2P-P70S6KInhibitor rapamycinHypoxia-inducible factor-1 alphaExpression of CC3
2005
Insulin Receptor Substrate 2 Is Essential for Maturation and Survival of Photoreceptor Cells
Yi X, Schubert M, Peachey N, Suzuma K, Burks D, Kushner J, Suzuma I, Cahill C, Flint C, Dow M, Leshan R, King G, White M. Insulin Receptor Substrate 2 Is Essential for Maturation and Survival of Photoreceptor Cells. Journal Of Neuroscience 2005, 25: 1240-1248. PMID: 15689562, PMCID: PMC6725974, DOI: 10.1523/jneurosci.3664-04.2005.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsAnimals, NewbornApoptosisCell SurvivalDiabetic RetinopathyEye ProteinsGene DeletionHomeodomain ProteinsHyperglycemiaHyperinsulinismInsulin Receptor Substrate ProteinsInsulin ResistanceInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutPhosphoproteinsPhosphorylationPhotic StimulationPhotoreceptor CellsProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRetinal Ganglion CellsSignal TransductionTrans-ActivatorsConceptsIrs2-/- micePhotoreceptor cellsPlexiform layerInsulin receptor substrate 2Insulin receptor substrateInsulin-like growth factor 1 receptorGrowth factor 1 receptorMost photoreceptor cellsInner plexiform layerOuter plexiform layerFactor 1 receptorFinal common pathwaySurvival of photoreceptorsNormal electrical functionMonths of ageWeeks of ageReceptor substrateCellular growthSubstrate 2Akt phosphorylationGanglion cellsIRS2 expressionPharmacological strategiesControl littermatesPhotoreceptor degeneration
2004
Macrophage Colony-Stimulating Factor-1 Receptor Expression Is Associated with Poor Outcome in Breast Cancer by Large Cohort Tissue Microarray Analysis
Kluger HM, Dolled-Filhart M, Rodov S, Kacinski BM, Camp RL, Rimm DL. Macrophage Colony-Stimulating Factor-1 Receptor Expression Is Associated with Poor Outcome in Breast Cancer by Large Cohort Tissue Microarray Analysis. Clinical Cancer Research 2004, 10: 173-177. PMID: 14734466, DOI: 10.1158/1078-0432.ccr-0699-3.Peer-Reviewed Original ResearchConceptsNode-positive patientsNode-negative patientsNode-positive casesCSF-1R expressionBreast cancerNodal statusOverall survivalPoor outcomeIpsilateral breast cancer recurrenceInvasive breast cancerNonmetastatic breast cancerPredictors of survivalNode-negative casesLarger tumor sizeSmall cohort studiesBreast cancer recurrenceCSF-1RTissue microarray analysisMacrophage colony-stimulating factor 1 receptorFactor 1 receptorTransmembrane tyrosine kinase receptorTyrosine kinase receptorsCohort studyColony-stimulating factor 1 receptorNodal involvement
2003
The tyrphostin AG1024 accelerates the degradation of phosphorylated forms of retinoblastoma protein (pRb) and restores pRb tumor suppressive function in melanoma cells.
von Willebrand M, Zacksenhaus E, Cheng E, Glazer P, Halaban R. The tyrphostin AG1024 accelerates the degradation of phosphorylated forms of retinoblastoma protein (pRb) and restores pRb tumor suppressive function in melanoma cells. Cancer Research 2003, 63: 1420-9. PMID: 12649208.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell DivisionCyclin-Dependent KinasesDNA-Binding ProteinsE2F Transcription FactorsE2F1 Transcription FactorE2F3 Transcription FactorHumansMAP Kinase Signaling SystemMelanocytesMelanomaMiceMitogen-Activated Protein Kinase 1PhosphorylationRetinoblastoma ProteinTranscription FactorsTyrphostinsUbiquitinConceptsTumor suppressive functionPhosphorylated formCell surface receptor kinaseMitogen-activated protein kinase/extracellular signal-regulated kinase pathwayProtein kinase/extracellular signal-regulated kinase pathwayExtracellular signal-regulated kinase (ERK) pathwaySignal-regulated kinase pathwayMelanoma cellsPhosphorylation/inactivationCyclin-dependent kinase 2Insulin-like growth factor 1 receptorActivation of pRbReceptor kinase activitySpecific chemical inhibitorsGrowth factor 1 receptorFactor 1 receptorPocket proteinsRetinoblastoma familyMelanoma cell proliferationReceptor kinaseProtein degradationKinase pathwayRetinoblastoma proteinKinase activityMelanoma cell growth
1997
Interaction of wild type and dominant-negative p55PIK regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins.
Mothe I, Delahaye L, Filloux C, Pons S, White M, Van Obberghen E. Interaction of wild type and dominant-negative p55PIK regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins. Endocrinology 1997, 11: 1911-23. PMID: 9415396, DOI: 10.1210/mend.11.13.0029.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportFungal ProteinsGenes, ReporterGlucoseInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IMutagenesis, Site-DirectedPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPrecipitin TestsReceptor, IGF Type 1Recombinant Fusion ProteinsSaccharomyces cerevisiaeSignal TransductionConceptsTwo-hybrid systemInsulin receptor substrate-1Receptor substrate-1Regulatory subunitSubstrate-1Src homology 2 domainInter-SH2 domainProtein-protein interactionsInhibitor of PIAmino acids 203Dominant negative mutantInsulin-stimulated glucose transportIGF-IRInsulin-like growth factor 1 receptorNH2 terminus regionDominant negative actionGrowth factor 1 receptorP110alpha catalytic subunitIGF-I stimulationSH2 domainFactor 1 receptorCatalytic subunitTyrosine phosphorylationWild typeP55PIK
1996
Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product.
Uddin S, Yetter A, Katzav S, Hofmann C, White M, Platanias L. Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product. Experimental Hematology 1996, 24: 622-7. PMID: 8605967.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineHumansInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMicePhosphoproteinsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-vavSignal TransductionConceptsSrc homology 2 domainVav proto-oncogene productGuanine exchange factorAntiphosphotyrosine monoclonal antibodyProto-oncogene productInsulin-like growth factor 1 receptorIGF-1 stimulationGrowth factor 1 receptorHematopoietic cell proliferationFactor 1 receptorExchange factorSH3 domainTyrosine phosphorylationPhosphorylation statusLigand bindingMediate signalsHematopoietic cellsImmunoblotting experimentsHematopoietic originCell proliferationCell linesHuman myeloma cell linesMyeloma cell linesCellsPhosphorylation
1995
The HPV16 E5 Protein: Expression, Detection, and Stable Complex Formation with Transmembrane Proteins in COS Cells
Hwang E, Nottoli T, Dimaio D. The HPV16 E5 Protein: Expression, Detection, and Stable Complex Formation with Transmembrane Proteins in COS Cells. Virology 1995, 211: 227-233. PMID: 7645215, DOI: 10.1006/viro.1995.1395.Peer-Reviewed Original ResearchConceptsE5 proteinHPV16 E5 proteinStable complex formationTransmembrane proteinGrowth factor receptorE5 genePlatelet-derived growth factor beta receptorViral proteinsVesicular stomatitis virus glycoproteinComplex formationFactor receptorCOS monkey cellsGrowth factor beta receptorStable growth transformationCultured cell systemsEpidermal growth factor receptorFactor 1 receptorTransforming proteinCoimmunoprecipitation analysisCOS cellsExpression vectorMonkey cellsBiochemical propertiesProteinE5 expression
1992
A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase
Goldstein D, Kulke R, Dimaio D, Schlegel R. A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase. Journal Of Virology 1992, 66: 405-413. PMID: 1370089, PMCID: PMC238300, DOI: 10.1128/jvi.66.1.405-413.1992.Peer-Reviewed Original ResearchConceptsK proteinGrowth factor receptorE5 oncoproteinGlutamine residuesRandom hydrophobic sequencesSpecific amino acid residuesMembrane-associated domainMajor transforming proteinK protein componentCarboxyl-terminal domainEndoplasmic reticulum membraneFactor receptorBovine papillomavirus type 1Colony-stimulating factor 1 receptorTransformation-defective mutantsAmino acid residuesPotential binding sitesPlatelet-derived growth factor receptorAmino acid substitutionsPapillomavirus type 1Hydrophilic amino acidsE5 dimerE5 mutantsFactor 1 receptorProtein complexes
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