2013
Direct Autocrine Action of Insulin on β-Cells: Does It Make Physiological Sense?
Rhodes C, White M, Leahy J, Kahn S. Direct Autocrine Action of Insulin on β-Cells: Does It Make Physiological Sense? Diabetes 2013, 62: 2157-2163. PMID: 23801714, PMCID: PMC3712043, DOI: 10.2337/db13-0246.Peer-Reviewed Original ResearchConceptsΒ-cellsDirect autocrine effectsTransgenic mouse studiesSignal transductionPancreatic β-cellsDownstream elementsAutocrine actionRelevant ligandsΒ-cell functionAutocrine effectsMouse studiesCircumstantial evidencePhysiological senseTransductionAvailable experimental evidencePathwayInsightsExperimental evidenceInsulin
1998
The IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Molecular And Cellular Biochemistry 1998, 182: 3-11. PMID: 9609109, DOI: 10.1023/a:1006806722619.Peer-Reviewed Original ResearchConceptsIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetesThe IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Developments In Molecular And Cellular Biochemistry 1998, 3-11. DOI: 10.1007/978-1-4615-5647-3_1.Peer-Reviewed Original ResearchIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetes
1991
The Juxtamembrane Regions of the Epidermal Growth Factor Receptor and gpl85 erbB-2 Determine the Specificity of Signal Transduction
Segatto O, Lonardo F, Wexler D, Fazioli F, Pierce J, Bottaro D, White M, Di Fiore P. The Juxtamembrane Regions of the Epidermal Growth Factor Receptor and gpl85 erbB-2 Determine the Specificity of Signal Transduction. Molecular And Cellular Biology 1991, 11: 3191-3202. DOI: 10.1128/mcb.11.6.3191-3202.1991.Peer-Reviewed Original ResearchEpidermal growth factor receptorSignal transductionSpecificity of substrate recognitionErbB-2Specificity of signal transductionAmino-terminal halfDeletion of residuesMitogenic signaling pathwaysMitogenic signal transductionEGFR kinaseGrowth factor receptorSubstrate recognitionTyrosine kinase domainJuxtamembrane regionKinase domainStructural homologyKinase propertiesFactor receptorMutation analysisSignaling pathwayTyrosine kinaseChimeric moleculesKinaseTyrosineTransduction