Location: | Oxford |
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Salary: | £30,502 to £36,386 Grade 6 per annum |
Hours: | Full Time |
Contract Type: | Fixed-Term/Contract |
Placed On: | 4th January 2023 |
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Closes: | 6th February 2023 |
Job Ref: | 162660 |
About the role
We have an exciting opportunity to join the D’Angiolella laboratory in the Department of Oncology.
We are looking for a research assistant who will play a key part in driving the translational goals of an industrially funded project within the D’Angiolella laboratory. The post holder is to assist a postdoctoral researcher in delivering the aims of a project focused on the targeted protein degradation space, utilising highly complementary expertise of four academic research groups at the University of Oxford. The post holder will have the opportunity to learn more deeply about ubiquitin biology, drug design, protein degradation, mass spectrometry-based proteomics and translational research.
About you
You will become an integral part of the project team, using biochemistry, molecular biology, and cell biology to help create the foundations of an exciting new area of targeted protein degradation. You will help to screen a Cullin-RING E3 ubiquitin ligase for novel molecular glues and/or PROTACs – small molecules that recruit neosubstrates to E3 ligases for ubiquitination and proteasomal degradation. This will involve a variety of cell culture and cellular assays, as well as immunoprecipitations to generate samples for mass spectrometry-based proteomics.
You should be highly motivated, meticulous and interested in ubiquitin biology.
Application Process
If you would like to discuss this role, please contact Dr Vincenzo D’Angiolella on vincenzo.dangiolella@oncology.ox.ac.uk
You will be required to upload a supporting statement (one page, setting out how you meet the selection criteria), a curriculum vitae and the names and contact details of two referees as part of your online application.
Only applications received before 12pm GMT on the 6th of February 2023 can be considered.
Committed to equality and valuing diversity
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