2004
IRS‐2 mediates the antiapoptotic effect of insulin in neonatal hepatocytes
Valverde A, Fabregat I, Burks D, White M, Benito M. IRS‐2 mediates the antiapoptotic effect of insulin in neonatal hepatocytes. Hepatology 2004, 40: 1285-1294. PMID: 15565601, DOI: 10.1002/hep.20485.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornApoptosisApoptosis Regulatory ProteinsBcl-2-Like Protein 11Bcl-X ProteinBlood ProteinsCarrier ProteinsEpidermal Growth FactorFemaleForkhead Box Protein O1Forkhead Transcription FactorsGene ExpressionHepatocytesHypoglycemic AgentsInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMaleMembrane ProteinsMiceMice, Mutant StrainsPhosphatidylinositol 3-KinasesPhosphoproteinsPregnancyProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-bcl-2Signal TransductionTranscription FactorsConceptsCaspase-3 activityIRS-2Caspase-3 activationGene expressionWild-type hepatocytesDominant negative FoxO1Wild-type cellsSerum withdrawal-induced apoptosisInsulin receptor substrateWithdrawal-induced apoptosisAnti-apoptotic gene expressionImmortalized hepatocyte cell linesIRS-2 signalingPIP3 generationProapoptotic gene expressionAntiapoptotic gene expressionProlonged insulin treatmentEpidermal growth factorActive FoxO1Receptor substrateNeonatal hepatocytesProapoptotic genesAntiapoptotic genesCaspase-8Serum withdrawal
1998
IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*
Burks D, Wang J, Towery H, Ishibashi O, Lowe D, Riedel H, White M. IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*. Journal Of Biological Chemistry 1998, 273: 31061-31067. PMID: 9813005, DOI: 10.1074/jbc.273.47.31061.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acids, DicarboxylicATP-Dependent ProteasesBinding SitesBlood ProteinsHeat-Shock ProteinsInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsLigandsMolecular Sequence DataOligopeptidesPeptide FragmentsPhosphoproteinsProtein BindingRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidSerine EndopeptidasesConceptsPH domainAcidic motifIRS-2IRS-1IRS proteinsLon proteaseInsulin-stimulated tyrosine phosphorylationTwo-hybrid systemBinding of nucleolinPleckstrin homologyPhospholipase CgammaMembrane proteinsTyrosine phosphorylationNucleolinPeptide motifsMembrane receptorsInsulin receptorSpecific functionsProteinMotifInsulin actionProteaseSynthetic peptidesBindingDomain
1996
The Pleckstrin Homology Domain Is the Principle Link between the Insulin Receptor and IRS-1*
Yenush L, Makati K, Smith-Hall J, Ishibashi O, Myers M, White M. The Pleckstrin Homology Domain Is the Principle Link between the Insulin Receptor and IRS-1*. Journal Of Biological Chemistry 1996, 271: 24300-24306. PMID: 8798677, DOI: 10.1074/jbc.271.39.24300.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesBlood ProteinsCell LineInsulin Receptor Substrate ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein BindingProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 Kinases