Monday, October 19 15:15-16:00 UTC ![]() |
Accelerating COVID Proteomics Research Using Tandem Mass Tags
Chair: Aaron Gajadhar, Strategic Marketing Specialist, Thermo Fisher Scientific Speakers:
For more information, click HERE. |
Monday, October 19 15:15-16:00 UTC ![]() |
Explore the Proteome Using CETSA MS
Chair: Stina Lundgren, Pelago Bioscience Speaker: Tomas Friman, Senior Research Scientist, Pelago Bioscience CETSA® MS allows for proteome-wide measurement of cellular target engagement using mass spectrometry by generating thermal profiles for 6000−7000 proteins in a single experiment. In contrast to conventional proteomics applications, CETSA MS measures the direct consequences of a drug on both its intended and off targets, as well as the immediate signaling cascade perturbed by the addition of a compound. This assay is free of labels and can be carried out in the live unmodified cells, thereby enabling the discovery of protein targets and pathways that would otherwise not be identified using traditional methods. Further, machine learning algorithms allows for exploration of global patterns and differences as well as extraction of differential proteins or groups of proteins to explore and compare the molecular mode of action of the profiled compounds. Welcome to learn about the CETSA methodology and how the mass spectrometric readout can be used for drug profiling, target deconvolution, biomarker discovery and toxicology safety assessment studies. |
Tuesday, October 20 15:15-16:00 UTC ![]() |
Advance in 4D-Proteomics™: Bioinformatics and prm-PASEF®
Chair: Gary Kruppa, Bruker Daltonics Speakers:
For more information and to pre-register, click HERE (note, you will still need to register for HUPO Connect 2020). |
Wednesday, October 21 15:15-16:00 UTC ![]() |
Exploring Multiplexed Proteomics in Complex Applications with SpectroMine
Chair: Lukas Reiter, PhD, Biognosys Speakers:
For more information, click HERE. |
Wednesday, October 21 15:15-16:00 UTC ![]() |
Multi-omic Analysis of Two Common p53 Mutations: Proteins Regulated by Mutated p53 as Potential Targets for Immunotherapy
Chair: Arianna Jones, Global Marketing Manager, Life Science Research, SCIEX Speakers:
The p53 protein is mutated in about 50% of human cancers. The mutant p53 proteins not only lose their normal function but often acquire novel oncogenic functions, a phenomenon termed mutant p53 gain-of-function (GOF). Mutant p53 has been shown to affect the transcription of various genes, as well as by protein–protein interactions with transcription factors and other effectors, however no one has investigated which of these proteins has the potential for being targeted by immunotherapeutic interventions. We therefore investigated the changes occurring after the p53 Null SaOS-2 cells were transfected by conformational p53-mutants R-273 and R-175, examined phenotypic and functional differences using macroscopic observations, proliferation, overall mRNA and proteomic changes alongside immunopeptidome profiling of peptide antigens bound to molecules encoded by the major histocompatibility complex (MHC) and presented on the cell surface. Expression profiling using gene expression microarray, qRT-PCR, and quantitative proteomic mass spectrometry, were employed to identify proteins whose peptide repertoire may be targeted by future immunotherapy/vaccine. The phenotype of SaOS-2-273 and SaOS-175 cells were assessed using colony formation, and proliferation assays. Using OneOmics™ Suite in SCIEX cloud, we identified several candidate markers in both p53 mutant cell lines with differential gene and protein expression from the p53 null control. Cross-comparison with the MHC bound peptides further identified potential targets. |
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