2021
Chemical complementarity between immune receptors and cancer mutants, independent of antigen presentation protein binding, is associated with increased survival rates
Hsiang M, Chobrutskiy BI, Diaz M, Huda TI, Creadore S, Zaman S, Cios KJ, Gozlan EC, Blanck G. Chemical complementarity between immune receptors and cancer mutants, independent of antigen presentation protein binding, is associated with increased survival rates. Translational Oncology 2021, 14: 101069. PMID: 33780706, PMCID: PMC8039726, DOI: 10.1016/j.tranon.2021.101069.Peer-Reviewed Original ResearchT cell receptor alpha geneAmino acidsT cell receptorChemical complementarityV-J recombinationMutant amino acidsThe Cancer Genome Atlas (TCGA) databaseCancer Genome Atlas (TCGA) databaseCancer mutantsBioinformatics approachAlpha geneReceptor alpha geneImmune receptorsComplement genesAtlas databaseMutantsPeptide sequencesSpecific interactionsGenesII bindingLRP2Region 3 sequencesUterine cancerProtein bindingBinding
2019
Potential 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