2019
Chemical complementarity between immune receptor CDR3s and IDH1 mutants correlates with increased survival for lower grade glioma
Chobrutskiy BI, Yeagley M, Tipping P, Zaman S, Diviney A, Patel DN, Falasiri S, Uversky VN, Blanck G. Chemical complementarity between immune receptor CDR3s and IDH1 mutants correlates with increased survival for lower grade glioma. Oncogene 2019, 39: 1773-1783. PMID: 31740784, DOI: 10.1038/s41388-019-1101-2.Peer-Reviewed Original ResearchConceptsLow-grade gliomasComplementarity-determining region 3T cell receptor beta chainImmune responseGrade gliomasIDH1 mutantChronic inflammationReceptor beta chainCancer immunologyLGG prognosisNRAS mutantsSurvival rateCancer developmentCDR3 domainsGliomasImmune receptorsBeta chainAnticancer processesSurvivalPotential MMP2-mediated availability of HLA binding, mutant ECM peptides reflects better melanoma survival rates and greater T-cell infiltrates
Zaman S, Chobrutskiy BI, Patel JS, Callahan BM, Mihyu MM, Diviney A, Blanck G. Potential MMP2-mediated availability of HLA binding, mutant ECM peptides reflects better melanoma survival rates and greater T-cell infiltrates. Laboratory Investigation 2019, 99: 1287-1295. PMID: 31019293, DOI: 10.1038/s41374-019-0248-3.Peer-Reviewed Original ResearchConceptsMutant amino acidsAmino acidsStructural proteinsExtracellular matrix structural proteinsMatrix metalloproteinase-2Cancer progressionLate-stage cancer developmentMutant peptidesECM structural proteinsMatrix structural proteinsBioinformatics approachProtein mutantsProtease functionECM peptidesSuch proteasesMutantsPotential substratesCancer developmentProteaseMelanoma samplesProteinSpread of cancerTumor samplesMetalloproteinase-2Cancer microenvironment
2018
P081 ST14 protease resistant peptides, from glioblastoma multiforme mutant proteins, represent higher binding affinities as potential HLA class I epitopes
Zaman S, Chobrutskiy B, Patel J, Callahan B, Blanck G. P081 ST14 protease resistant peptides, from glioblastoma multiforme mutant proteins, represent higher binding affinities as potential HLA class I epitopes. Human Immunology 2018, 79: 121. DOI: 10.1016/j.humimm.2018.07.140.Peer-Reviewed Original ResearchJ recombinationT cell receptorAa substitutionsProtease sensitivityExtracellular matrix-related proteinsCancer developmentMatrix-related proteinsAmino acid substitutionsBinding affinitiesTransmembrane serine proteaseHigh binding affinityMutant proteinsBioinformatics approachAcid substitutionsProtease cleavageExtracellular matrixSerine proteasesMutant peptidesCytoskeletonProteasePeptide sequencesClass IBarcodesRecombinationProteinMutant cytoskeletal and ECM peptides sensitive to the ST14 protease are associated with a worse outcome for glioblastoma multiforme
Zaman S, Chobrutskiy BI, Patel JS, Callahan BM, Tong WL, Blanck G. Mutant cytoskeletal and ECM peptides sensitive to the ST14 protease are associated with a worse outcome for glioblastoma multiforme. Biochemical And Biophysical Research Communications 2018, 503: 2218-2225. PMID: 29953855, DOI: 10.1016/j.bbrc.2018.06.141.Peer-Reviewed Original ResearchConceptsT cell receptorAa substitutionsExtracellular matrix-related proteinsMatrix-related proteinsAmino acid substitutionsTransmembrane serine proteaseBioinformatics approachECM peptidesProtease sensitivityAcid substitutionsSerine proteasesCancer developmentProteasePeptide sequencesBarcodesHigh binding affinityBinding affinitiesCancer datasetsClass IRecombinationExome filesCytoskeletalCytoskeletonSubstitutionGlioblastoma multiforme