2023
Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?
Shillingford S, Bennett A. Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable? The Annual Review Of Pharmacology And Toxicology 2023, 63: 617-636. PMID: 36662585, PMCID: PMC10127142, DOI: 10.1146/annurev-pharmtox-051921-121923.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseSmall molecule inhibitionProtein kinaseCritical cellular functionsInhibition of PTPsProtein tyrosineCellular functionsProtein substratesPhosphorylated proteinsCell signalingTyrosine residuesAttractive therapeutic targetCellular effectsKinaseNumerous diseasesPTPDiscovery toolTherapeutic developmentTherapeutic targetMetabolic diseasesInhibitionDephosphorylationSignalingMKPProtein
2018
DUSPs, twists and turns in the Journey to Vascular Inflammation
Bennett AM. DUSPs, twists and turns in the Journey to Vascular Inflammation. The FEBS Journal 2018, 285: 1589-1592. PMID: 29682902, DOI: 10.1111/febs.14461.Peer-Reviewed Original Research
2017
Loss of MKP-5 promotes myofiber survival by activating STAT3/Bcl-2 signaling during regenerative myogenesis
Min K, Lawan A, Bennett AM. Loss of MKP-5 promotes myofiber survival by activating STAT3/Bcl-2 signaling during regenerative myogenesis. Skeletal Muscle 2017, 7: 21. PMID: 29047406, PMCID: PMC5648478, DOI: 10.1186/s13395-017-0137-7.Peer-Reviewed Original ResearchConceptsMAPK phosphatase-5Mitogen-activated protein kinaseRegenerative myogenesisApoptotic signalingMyofiber survivalMAPK/JNK signalingMuscle regenerationSkeletal muscleP38 mitogen-activated protein kinaseMitochondrial apoptotic pathwaySkeletal muscle regenerationSkeletal muscle survivalDegenerative muscle diseasePhosphatase 5Expression of catalaseProtein kinaseSTAT3/BclSignal transducerJNK signalingWild typeExpression exhibitTranscription 3Apoptotic pathwayMitochondrial functionSignaling
2013
Mitogen-Activated Protein Kinase Phosphatases in Metabolism
Lawan A, Bennett A. Mitogen-Activated Protein Kinase Phosphatases in Metabolism. 2013, 221-238. DOI: 10.1007/978-1-4614-7855-3_12.Peer-Reviewed Original ResearchMitogen-activated protein kinaseMetabolic homeostasisProtein kinaseTissue-specific mannerFamily of enzymesDirect dephosphorylationPathophysiological signalingMAPK activityMAPK inactivationMetabolic signalingImportant playersMKPHomeostasisKinaseCritical roleSignalingBody of evidenceMetabolismDephosphorylationComplex networksComparable levelsEnzymeMitogenPathwayRegulation
1994
Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.
Bennett A, Tang T, Sugimoto S, Walsh C, Neel B. Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7335-7339. PMID: 8041791, PMCID: PMC44394, DOI: 10.1073/pnas.91.15.7335.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBase SequenceBinding SitesCell LineDNAGenes, rasHumansIntracellular Signaling Peptides and ProteinsMiceMice, Inbred BALB CMolecular Sequence DataPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, Platelet-Derived Growth FactorSH2 Domain-Containing Protein Tyrosine PhosphatasesSignal TransductionConceptsPlatelet-derived growth factor receptor betaGrowth factor receptor betaPDGF stimulationPositive signalingReceptor tyrosine kinasesSH2 domainRas activationGrowth factor receptorReceptor betaTyrosine phosphorylationSHPTP2Gene productsTyrosine kinaseGrb2Vivo sitesFactor receptorPhosphorylationSignalingPositive signalsSOS1RAHomologuesKinaseSite displayBeta