PhD Positions - Molecular and Cellular Life Sciences
The International Max Planck Research School for Molecular and Cellular Life Sciences (IMPRS-LS), jointly conducted by Munich based Max Planck Institutes and Universities, is an internationally recognized center of scientific and educational excellence.
More than 60 distinguished group leaders actively participate in the PhD program and offer challenging and cutting-edge PhD projects in the following areas:
- Biochemistry
- Neurobiology
- Cell Biology
- Molecular Medicine
- Structural Biology
The program provides comprehensive scientific training in a superb and vibrant research environment with state-of-the-art facilities. Doctoral students are fully integrated in international teams of scientists providing ample access to expertise and support in an interdisciplinary setting.
Laboratory work is supplemented by seminars, summer schools, elective courses, career development training and participation in national or international conferences.
Munich, as one of the leading German research areas in life sciences, offers a unique mixture of academic and urban lifestyle spiced with Bavarian tradition.
Highly qualified candidates with a deep commitment to basic research are invited to apply. Applicants should hold a MSc (or an equivalent degree) with a strong background in biological sciences, biochemistry, biophysics, biotechnology or a related discipline.
Successful candidates will be supported with a generous PhD fellowship covering living expenses and tuition.
Application Start: October 15, 2013
Closing Date: January 10, 2014
For more information and online application please visit our website:
www.imprs-ls.de
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We offer you:
- Excellent career opportunities
- Structured PhD program organized by Munich-based Max Planck Institutes and Universities
- State-of-the-art facilities and cutting-edge research projects
- Individualized supervision and mentoring
- International setting – Language of instruction is English, German language skills are not required
- Full funding provided for international and German students
We are looking for:
- Talented, creative and enthusiastic doctoral students from all over the world with a strong passion for science & research
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Selected publications 2013:
Maisak, M.S., Haag, J., Ammer, G., Serbe, E., Meier, M., Leonhardt, A., Schilling, T., Bahl, A., Rubin, G.M., Nern, A., Dickson, B.J., Reiff, D.F., Hopp, E., and Borst, A. (2013). A directional tuning map of Drosophila elementary motion detectors.
Nature, 500:212-216.
Helmstaedter, M., Briggman, K.L., Turaga, S.C., Jain, V., Seung, H.S., and Denk, W. (2013). Connectomic reconstruction of the inner plexiform layer in the mouse retina.
Nature, 500:168-174.
Park, S.H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M.S., Hayer-Hartl, M., and Hartl, F.U. (2013). PolyQ Proteins Interfere with Nuclear Degradation of Cytosolic Proteins by Sequestering the Sis1p Chaperone.
Cell, 154(1):134-45.
Tosi A, Haas C, Herzog F, Gilmozzi A, Berninghausen O, Ungewickell C, Gerhold CB, Lakomek K, Aebersold R, Beckmann R, Hopfner KP. (2013). Structure and Subunit Topology of the INO80 Chromatin Remodeler and Its Nucleosome Complex.
Cell, 154(6):1207-19.
Halbach, F., Reichelt, P., Rode, M., and Conti, E. (2013). The yeast ski complex: crystal structure and RNA channeling to the exosome complex.
Cell, 154:814-826.
Bhogaraju, S., Cajanek, L., Fort, C., Blisnick, T., Weber, K., Taschner, M., Mizuno, N., Lamla, S., Bastin, P., Nigg, E.A., andLorentzen, E. (2013). Molecular basis of tubulin transport within the cilium by IFT74 and IFT81.
Science, 341:1009-1012.
Civril, F., Deimling, T., de Oliveira Mann, C.C., Ablasser, A., Moldt, M., Witte, G., Hornung, V., and Hopfner, K.P. (2013). Structural mechanism of cytosolic DNA sensing by cGAS.
Nature, 498(7454):332-7
Hondele, M., Stuwe, T., Hassler, M., Halbach, F., Bowman, A., Zhang, E.T., Nijmeijer, B., Kotthoff, C., Rybin, V., Amlacher, S., Hurt, E., and Ladurner, A.G. (2013). Structural basis of histone H2A-H2B recognition by the essential chaperone FACT.
Nature, 499(7456):111-4
Mues, M., Bartholomaus, I., Thestrup, T., Griesbeck, O., Wekerle, H., Kawakami, N., and Krishnamoorthy, G. (2013). Real-time in vivo analysis of T cell activation in the central nervous system using a genetically encoded calcium indicator.
Nat Med., 19(6):778-83
Anger, A.M., Armache, J.P., Berninghausen, O., Habeck, M., Subklewe, M., Wilson, D.N., and Beckmann, R. (2013). Structures of the human and Drosophila 80S ribosome.
Nature, 497:80-85
Stahl, R., Walcher, T., De Juan Romero, C., Pilz, G.A., Cappello, S., Irmler, M., Sanz-Aquela, J.M., Beckers, J., Blum, R., Borrell, V., and Gotz, M. (2013). Trnp1 regulates expansion and folding of the Mammalian cerebral cortex by control of radial glial fate.
Cell, 153:535-549.
Meissner, F., Scheltema, R.A., Mollenkopf, H.J., and Mann, M. (2013). Direct proteomic quantification of the secretome of activated immune cells.
Science, 340:475-478.
Mori, K., Weng, S.M., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H.A., Cruts, M., Van Broeckhoven, C., Haass, C., and Edbauer, D. (2013). The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS.
Science, 339(6125):1335-8
Pengelly, A.R., Copur, O., Jackle, H., Herzig, A., and Muller, J. (2013). A histone mutant reproduces the phenotype caused by loss of histone-modifying factor Polycomb.
Science, 339:698-699.
Dept. of Bioscience and Informatics - Keio Univ - Japan
Dept. of Computer Science and Electronics - Gadjah Mada Univ - Indonesia
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