Measurement of Aberrant Protein Folds in Malignant Cells with Proteomics and Mass Spectrometry
Measurement of Aberrant Protein Folds in Malignant Cells with Proteomics and Mass Spectrometry
批准号:
9233438
负责人:
John R Yates III
金额:
$43.56万
依托单位国家:
美国
项目类别:
财政年份:
2017
资助国家:
美国
项目状态:
已结题
起止时间:
2017-03-10 至 2020-02-29
关键词:
1-Phosphatidylinositol 3-KinaseAminationAminesArchitectureBiochemicalBioinformaticsBiopsyBreast Epithelial CellsCell LineCellsChargeChemicalsCloningComputer SimulationCoupledCrystallizationDNADNA BindingDNA Binding DomainDNA Sequence AlterationDetectionDevelopmentDigestionEnvironmentEvolutionGenotypeGunsIndividualIsotopesK-ras OncogeneLabelLysineMCF10A cellsMalignant - descriptorMalignant NeoplasmsMass Spectrum AnalysisMeasurementMeasuresMembrane ProteinsMethodsMethylationModificationMolecularMusMutateMutationNon-MalignantPIK3CA genePatientsPeptidesPoint MutationProtein p53ProteinsProteomeProteomicsProto-OncogenesRNAReactionReagentReproducibilityResearchSamplingScreening for cancerSolventsSomatic CellSomatic MutationStructureSurfaceTechniquesTechnologyTemperatureTestingTherapeutic InterventionTimeValidationamino groupbasebiological adaptation to stresscancer cellcell transformationchemical reactionexperimental studyin vivoinsightmisfolded proteinmouse modelnew technologynovelnovel strategiesoverexpressionprotein foldingprotein misfoldingprotein structureresponsestable isotopetargeted cancer therapytargeted treatmenttooltumor
中文摘要
项目总结
英文摘要
Project Summary
Malignant transformation of cells drives the development of tumors. Cancer cells can be
routinely genotyped today revealing a large number of somatic mutations. However, it remains
unclear which mutations contribute to malignant transformation and provide a survival
advantage to cancer cells and which are simply passenger mutations. Rather than dissecting
each mutation individually by biochemical techniques such as cloning and overexpression, we
propose to systematically profile the proteome of cancer cells for altered protein surface
accessibility, which can help to better understand the impact of somatic mutations on proteome
function and activity. Neomorphic perturbations in protein surface accessibility is revealed with
a new, quantitative, in vivo chemical labeling approach coupled to shot gun proteomics. The
novel approach can be used as a platform technology to screen patient-derived cancer cells and
holds promise to pinpoint critical, cancer cell specific perturbations in the proteome.
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海外基金