Synthetic organic chemist for targeted protein degradation (m/f/x)
The Winter laboratory at CeMM, the Research Center for Molecular Medicine of the Austrian Academy of Sciences in Vienna, is recruiting a synthetic organic chemist to develop novel strategies for the treatment of cancer by chemically reprogramming the cellular degradation machinery.
The successful applicant will work as part of an ERC-funded team to mechanistically understand and chemically optimize novel strategies for the targeted degradation of cancer-relevant proteins. The position will be at the interface with ongoing efforts in phenotypic drug screening, chemical genetics, high-throughput CRISPR screens and proteomics. The Candidate will perform lead optimization, but also derivatization of screening hits to allow ensuing drug-target identification strategies.
The successful candidate holds a degree in Synthetic Organic Chemistry (Master or PhD degree), and has a proven track record in the application of synthetic pathways to systematically generate compound sets. Expertise in bioorthogonal chemistry, protein degradation, PROTAC development, or compound library design is considered a plus. The working language at CeMM is English, and excellent written and oral communication skills as well as high accuracy, reliability and excellent interpersonal and organizational skills are a requirement.
The Winter laboratory is working at the interface of chemical biology, cancer and gene-control with a particular focus on targeted protein degradation. The ERC-funded project “Glue2Degrade” aims to write the next chapter in the field of targeted protein degradation by systematically identifying and characterizing small “molecular glue”-type E3 ligase modulators. The ultimate goal of the Winter lab is to develop chemical strategies that allow the targeted degradation of oncogenic transcription factors. Dr. Winter’s seminal paper, showcasing the first in vivo compatible and generalizable strategy for targeted protein degradation (Winter et al., Science 2015), has sparked an immense research interest in the field. Since establishing his independent research lab at CeMM, the lab published, among others, molecules for the homolog-selective degradation of CDK6 (Brand et al., Cell Chemical Biology 2019), and a general survey for potential resistance mechanisms to small molecule degraders (Mayor-Ruiz et al., Molecular Cell 2019). The lab closely collaborates with the Platform Austria for Chemical Biology PLACEBO, a unique chemical screening infrastructure with a collection of 90,000 small molecule compounds. In addition, we apply proteomics, chemistry, mass spectrometry, bioinformatics, and next generation sequencing to address our research questions. In this position you will have the opportunity to work in an innovative research environment and collaborate closely with other groups at CeMM.
CeMM is a biomedical flagship institute in the heart of Europe, Vienna. We are committed to highest scientific standards and provide an international environment representing approximately 45 nationalities. The working language is English. CeMM has been ranked by The Scientist as one of the Best Places to Work Academia worldwide (link: http://goo.gl/51VMO). In the past 3 years CeMM groups published numerous ground-breaking studies in prestigious journals such as Science, Cell, Nature, New England Journal of Medicine, Nature Immunology, Immunity etc. CeMM is located within the medical campus of Vienna and operates several technology platforms (chemical biological screening, proteomics, metabolomics, next-generation sequencing) as well as extensive bioinformatics infrastructure. For more information please visit: www.cemm.at
CeMM aims to promote equality of opportunity for all with the right mix of talent, competences and potential. We welcome applications from candidates with diverse backgrounds. Please apply online with your application documents (cover letter, CV and names and contact details of 2 referees):
Applications will be reviewed on a rolling basis until the position is filled.