605 machine-learning "https:" "https:" "https:" "https:" "UCL" "UCL" PhD research jobs
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the Ph.D. candidate is enrolled as a Ph.D. student at Aarhus University Graduate School of Health ( http://phd.health.au.dk/ ) in a separate procedure before starting as a Ph.D. student. The successful
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Description Applications are invited for a full-time postdoctoral position in the laboratory of Dr. Catherine Searle, Department of Biological Sciences, Purdue University: https://www.bio.purdue.edu/lab/searle
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nanotechnology. ISSP UL is an active participant in Horizon Europe, ERDF, and international R&I programmes, and maintains strong industrial partnerships across Europe. More information: https://www.cfi.lu.lv https
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. Adapt, develop and learn new tools, software, and methodologies independently. Present and publish research in both academic and non-academic audiences. Attend and participate in academic and non-academic
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literature review, hypothesis development, and experimental design. Adapt, develop and learn new tools, software, and methodologies independently. Present and publish research in both academic and non-academic
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31.12.2025. Please apply exclusively via our job portal (https://jobs.uni-siegen.de ). Unfortunately, we cannot consider applications in writing or by e-mail. Your contact person: Prof. Dr. Roman Obermaisser
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of charge, at universities or research institutions, both Italian and foreign, other than the University of Pisa Where to apply Website https://pica.cineca.it/unipi/ Requirements Additional Information Work
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. The presentation of such Recognition is mandatory for contract signature. More information can be obtained in: https://www.dges.gov.pt/en/pagina/degree-and-diploma-recognition . II. Preferential Requirements R&D
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recruited will be based at the Musée de l'Homme in Paris within the Eco-Anthropologie UMR 7206 unit (https://ecoanthropologie.fr/fr ) and will interact regularly with the UMR5300 Centre de Recherche pour la
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date. Recent relevant publications include: Ramage DE. Timms RT (2025) LRRC58 defines an E3 ubiquitin ligase complex sensitive to cysteine abundance. bioRxiv https://doi.org/10.1101/2025.09.23.678073