Sort by
Refine Your Search
-
Listed
-
Category
-
Program
-
Employer
- ETH Zurich
- University of Basel
- ETH Zürich
- Empa
- Nature Careers
- University of Zurich
- EPFL
- Paul Scherrer Institut Villigen
- University of Geneva
- Zürcher Hochschule für Angewandte Wissenschaft ZHAW
- Ecole Polytechnique Federale de Lausanne
- Ecole Polytechnique Federale de Lausanne - EPFL
- Fluxim AG
- Prof. Dr. Ricarda Toerner
- Swiss Federal Institute for Forest, Snow and Landscape Research WSL
- University of Bern
- Universität Basel
- École Polytechnique Fédérale de Lausanne (EPFL)
- 8 more »
- « less
-
Field
-
. This position is primarily linked to the EU Horizon Europe project titled ‘Renovation with automation and optimization of processes and products’ (RENOMIZE) (https://cordis.europa.eu/project/id/101192326 and
-
. The aim of the project is to extend cycle life by the controlled release of active lithium. Your tasks Develop lithiation agents to recover lost active lithium during operation of the battery Develop
-
enrolled at ETH Zürich, with Prof. Salvador Pané i Vidal as academic supervisor (Department of Mechanical and Process Engineering, D-MAVT). You will be employed at Empa in St. Gallen full-time for three
-
. All data is acquired and processed using SeisComP. Project background We are seeking an outstanding scientist with strong interest in network seismology and software development to enhance our
-
conduct their research at the Biozentrum at the moment. Our selection procedure Our selection procedure is based on in-person interactions on site. Shortlisted candidates will be invited to the Biozentrum
-
process monitoring for manufacturing. Project background We are seeking a motivated engineer to join our team for a funded innovation project in collaboration with a leading Swiss industrial partner
-
100%, starting January 2026 (negotiable) Proteins must fold correctly to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a
-
to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a molecular chaperone essential for the folding and maturation of at least 20% of
-
transfer. We use complementary approaches including cryo-EM, biophysical methods and in vivo functional assays to study the protein machineries involved in this process. Join our young, ambitious, and
-
transfer. We use complementary approaches including cryo-EM, biophysical methods and in vivo functional assays to study the protein machineries involved in this process. Join our young, ambitious, and