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