2025
Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions
Torres Robles J, Stiegler A, Boggon T, Turk B. Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. Journal Of Biological Chemistry 2025, 301: 108348. PMID: 40015635, DOI: 10.1016/j.jbc.2025.108348.Peer-Reviewed Original ResearchShort linear motifsCancer hotspot mutationsLinear motifsERK substratesYeast two-hybrid libraryHotspot mutationsTwo-hybrid libraryCancer-associated mutantsDocking interactionsWild-type ERK2Cancer-associated mutationsDocking motifBinding sequenceKinase ERK2Co-crystal structureMutant formsERK2 mutantsDisordered regionsERK2MotifStructural rationalePeptide bindingMutationsWT kinasePeptide fragments
2012
Phosphoglycerate Mutase 1 Promotes Leukemia Metabolism by Coordinating Glycolysis and Biosynthesis, and Represnts a Therapuetic Target in Leukemia Treatment
Hitosugi T, Zhou L, Fan J, Arellano M, Khoury H, Lee B, Boggon T, Kang S, He C, Chen J. Phosphoglycerate Mutase 1 Promotes Leukemia Metabolism by Coordinating Glycolysis and Biosynthesis, and Represnts a Therapuetic Target in Leukemia Treatment. Blood 2012, 120: 860. DOI: 10.1182/blood.v120.21.860.860.Peer-Reviewed Original ResearchPhosphoglycerate mutase 1Pentose phosphate pathwayHuman leukemia cell linesCell proliferationAnabolic biosynthesisCell metabolismLeukemia cell linesOxidative pentose phosphate pathwayPrimary leukemia cellsLeukemia cellsCancer cellsCell linesGlycolytic enzyme phosphoglycerate mutase 1PGAM1 inhibitorsSmall molecule inhibitorsCo-crystal structureXenograft nude miceInhibits cell proliferationLeukemia cell metabolismBiosynthesis pathwayEnzyme activity levelsHuman leukemia cellsShRNA resultsLoss of TP53Phosphate pathway
2005
Jak3 Kinase Domain Crystal Structures and Implications for Jak-Specific Drug Design.
Boggon T. Jak3 Kinase Domain Crystal Structures and Implications for Jak-Specific Drug Design. Blood 2005, 106: 69. DOI: 10.1182/blood.v106.11.69.69.Peer-Reviewed Original ResearchJAK3 kinase domainKinase domainDomain crystal structureResolution co-crystal structureJAK kinase family membersTyrosine kinaseLatent transcription factorsNon-receptor tyrosine kinaseActivation of transcriptionReceptor cytoplasmic tailKinase family membersRapid tyrosine phosphorylationThree-dimensional structural dataJAK-specific inhibitorDrug designTyrosine kinase activityFurther crystal structuresAutoinhibited conformationCo-crystal structureJAK activityConformational plasticityCytoplasmic tailTranscription factorsTranscription (STAT) proteinsGrowth factor receptor
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