2018
Analysis of Cellular Tyrosine Phosphorylation via Chemical Rescue of Conditionally Active Abl Kinase
Wang Z, Kim MS, Martinez-Ferrando I, Koleske A, Pandey A, Cole P. Analysis of Cellular Tyrosine Phosphorylation via Chemical Rescue of Conditionally Active Abl Kinase. Biochemistry 2018, 57: 1390-1398. PMID: 29341593, PMCID: PMC5906802, DOI: 10.1021/acs.biochem.7b01158.Peer-Reviewed Original ResearchConceptsProtein kinaseNonreceptor tyrosine kinases AblMass spectrometry-based quantitative proteomicsNovel putative substratesTyrosine kinase AblCellular tyrosine phosphorylationExtracellular growth factorsChemical rescue approachIntracellular signal transductionQuantitative phosphoproteomicsUnanticipated functionCellular physiologyGrowth factorPhosphorylation sitesPutative substratesDirect substrateDownstream substratesSignal transductionReceptor kinaseQuantitative proteomicsTyrosine phosphorylationActive Abl kinasesAbl kinaseChemical rescueKinase
2001
The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
Wang Y, Miller A, Mooseker M, Koleske A. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14865-14870. PMID: 11752434, PMCID: PMC64950, DOI: 10.1073/pnas.251249298.Peer-Reviewed Original ResearchConceptsF-actin-binding domainActin-rich structuresAbl family kinasesNonreceptor tyrosine kinaseF-actinActin cytoskeletonFamily kinasesFluorescent protein fusion proteinTyrosine kinaseActin-bundling activityProtein fusion proteinActin cytoskeletal structuresCellular morphogenesisSwiss 3T3 fibroblastsBundling activityDeletion mutantsCytoskeletal structuresC-terminusFusion proteinFunctional interactionKinaseActin moleculesCytoskeletonPositive cooperativityArgThe ARG Tyrosine Kinase Interacts with Siva-1 in the Apoptotic Response to Oxidative Stress*
Cao C, Ren X, Kharbanda S, Koleske A, Prasad K, Kufe D. The ARG Tyrosine Kinase Interacts with Siva-1 in the Apoptotic Response to Oxidative Stress*. Journal Of Biological Chemistry 2001, 276: 11465-11468. PMID: 11278261, DOI: 10.1074/jbc.c100050200.Peer-Reviewed Original Research
1995
A kinase–cyclin pair in the RNA polymerase II holoenzyme
Liao S, Zhang J, Jeffery D, Koleske A, Thompson C, Chao D, Viljoen M, van Vuuren H, Young R. A kinase–cyclin pair in the RNA polymerase II holoenzyme. Nature 1995, 374: 193-196. PMID: 7877695, DOI: 10.1038/374193a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCyclin-Dependent Kinase 8Cyclin-Dependent KinasesCyclinsFungal ProteinsMolecular Sequence DataMutationProtein Serine-Threonine KinasesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticConceptsRNA polymerase II holoenzymeSRB proteinsKinase functionRNA polymerase II carboxy-terminal domainCyclin-like proteinGeneral transcription factorsRNA polymerase IISuppressors of mutationsNormal transcriptional responseCarboxy-terminal domainPolymerase IITranscriptional regulatorsTranscriptional responseGalactose inductionTranscription factorsRegulatory proteinsTranscription systemHoloenzymeRegulatory roleKinaseProteinBiochemical evidenceGenesVivoSrb11