| University scholarship | 5 | University scholarship reserved to foreign applicants | 0 | Department scholarship | 0 |
| Scholarship funded by private research institution | 0 | Scholarship funded by private non-research institution | 0 | Scholarship funded by public research institution | 1 |
| Scholarship funded by public non-research institution | 0 | PhD position under national research programs | 0 | PhD position under EU research programs | 0 |
| Foreign independent candidates | 0 | Employee of private research institution/organisation under a cooperation agreement | 0 | Employee of private non-research institution/organisation under a cooperation agreement | 0 |
| Employee of public research institution/organisation under a cooperation agreement | 0 | Employee of public non-research institution/organisation under a cooperation agreement | 4 | PhD under higher education and research apprenticeship contract at a private research institution/organisation | 0 |
| PhD under higher education and research apprenticeship contract at a private non-research institution/organisation | 0 | PhD under higher education and research apprenticeship contract at a public research institution/organisation | 0 | PhD under higher education and research apprenticeship contract at a public non-research institution/organisation | 0 |
| No scholarship | 3 | | | | |
Founded by: Istituto Superiore di Sanità
Research topic: Advanced Quantitative and Functional Proteomics of Cellular Perturbations for Biomedical Insights
Description: Results from an ISS-funded research project demonstrated that inhibition of phosphatidylcholine-specific phospholipase C activity by the investigative tricyclodecan-9-yl xanthogenate (D609) thiol drug reduces viability and proliferation in triple-negative breast cancer cells and affects proteome composition. However, the D609 mechanism of action and its protein target(s) are still unknown.
This PhD project aims to fill this knowledge gap by conducting a multi-layered mass spectrometry analysis to identify protein targets, characterize proteome remodeling, signaling pathway modulation, and drug mechanism of action. The target will be identified through a drug-induced protein thermal stabilization strategy via label-free, intensity-based quantitative mass spectrometry. The mechanism of action will be investigated by state-of-the-art mass spectrometry strategies combined with machine learning-based algorithms. These approaches will measure quantitative proteome modulation, phosphorylation dynamics, and cysteine reactivity.
This project is expected to characterize drug-driven cellular responses including pathway alteration, post-translational modifications and redox state, presumptively modified by a thiol-containing compound. It will thus elucidate the mechanisms leading to cell proliferation arrest.
Scholarship type: BORSISTA ENTE ESTERNO PUBBLICO DI RICERCA
Lenght: 36
|