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We have used mass spectrometry for over 5 years as a viable method to investigate protein protein interactions and post-translational modifications in cellular proteins as well as a method to investigate the role of extra-cellular proteins.
Research areas that use these methods include the investigation of various protein modifications in cellular processes, modifying proteins for efficient recombinant expression, and the stabilization of mRNAs to allow for increased protein expression.
Recent advances in redox proteomics have provided significant insight into the role of oxidative modifications in cellular signalling and metabolism.
Despite their Herculean efforts, these projects have comprehensively analyzed only a small fraction the modifications in cellular contexts of interest to the scientific community.
To explore the regulatory potential for tRNA modifications in cellular stress responses, we developed a systems-oriented LC MS platform to measure changes in the relative quantities of all tRNA modifications in an organism.
The reason for the down-regulation of structural cytoskeleton proteins (actin, alpha- and beta-tubulin) in the fat body is not known, and could be related to modifications in cellular trafficking, mitosis, or apoptosis (preparation to pupation).
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In parallel with the decrease in cell proliferation, we observed that the presence of SI 34 determined a modification in cellular morphology.
Indeed the most important problem in cell modelization is the continuous modification in cellular protein content and in molecular interactions due to the dynamical regulation of genes expression and protein transcription.
Modifications in vital cellular molecules can provoke alterations in the cellular structure causing malfunctions that may finally result in apoptosis or necrosis.
Fitness costs associated with resistance may arise from modifications in the cellular targets of antibiotics, which prevent binding of the drug but also compromise their cellular role.
We recently found that exposure to high glucose also induced significant abundance changes of O-linked N-acetylglucosamine (O-GlcNAc) modification of mesothelial cell proteins, a posttranslational protein modification relevant in cellular survival [ 8].
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