Professor Matthias Feige studied biochemistry at the Swiss Federal Institute of Technology (ETH Zurich) and TUM. In 2009, he obtained his PhD in biochemistry under the supervision of Johannes Buchner at TUM. As a postdoctoral fellow in the laboratory of Linda Hendershot at the St. Jude Children’s Research Hospital, Memphis, TN, USA, he expanded his research toward cell biology and now heads the laboratory for cellular protein biochemistry at TUM.
2012 Rainer Rudolph Foundation, Rainer Rudolph Award
2011-2014 Fellow of the German Academy of Sciences Leopoldina
2011 Management Engineers Presidential Award, Management Engineers and TUM
2010-2011 Paul Barrett Fellowship, St. Jude Children’s Research Hospital
2010 Hans Fischer Award, Hans Fischer Society
2010 PhD Award, TUM Graduate School
2005 Jürgen Manchot Award, Jürgen Manchot Foundation
2003-2009 Fellow of the German National Academic Foundation
Matthias Feige’s laboratory aims at understanding how cells control and maintain the integrity of their proteome. He is particularly interested in proteins of the secretory pathway – proteins that are ultimately secreted or localized on the cell surface and allow cells to interact with their environment. Using an interdisciplinary approach from protein biochemistry to cell biology, he analyzes the machinery and mechanisms that monitor cellular protein biogenesis. By focusing on proteins of immunological and biomedical relevance, he seeks a molecular understanding of fundamental biological processes that at the same time may help in developing new approaches for protein engineering and human therapy.
- Feige, Matthias J.; Buchner, Johannes: Principles and engineering of antibody folding and assembly. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1844 (11), 2014, 2024-2031.
- The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins. Proceedings of the National Academy of Sciences 111 (22), 2014, 8155-8160.
- Quality Control of Integral Membrane Proteins by Assembly-Dependent Membrane Integration. Molecular Cell 51 (3), 2013, 297-309.
- An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies. Molecular Cell 34 (5), 2009, 569-579.
- The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity. Proceedings of the National Academy of Sciences 105 (36), 2008, 13373-13378.
- Genetically encoded biotin analogs: Incorporation and application in bacterial and mammalian cells. ChemBioChem, 2019 mehr… BibTeX Volltext ( DOI )
- The molecular basis of chaperone-mediated interleukin 23 assembly control. Nature Communications 10 (1), 2019 mehr… BibTeX Volltext ( DOI )
- An Interspecies Analysis Reveals Molecular Construction Principles of Interleukin 27. Journal of Molecular Biology 431 (12), 2019, 2383-2393 mehr… BibTeX Volltext ( DOI )
- A folding switch regulates interleukin 27 biogenesis and secretion of its α-subunit as a cytokine. Proceedings of the National Academy of Sciences 116 (5), 2019, 1585-1590 mehr… BibTeX Volltext ( DOI )
- Dissipative Self-Assembly of Photoluminescent Silicon Nanocrystals. Angewandte Chemie International Edition 57 (44), 2018, 14608-14612 mehr… BibTeX Volltext ( DOI )
- Oxidative Folding of Proteins. Royal Society of Chemistry, 2018 mehr… BibTeX Volltext ( DOI )
- hIAPP forms toxic oligomers in plasma. Chemical Communications 54 (43), 2018, 5426-5429 mehr… BibTeX Volltext ( DOI )
- BiP and Its Nucleotide Exchange Factors Grp170 and Sil1: Mechanisms of Action and Biological Functions. Journal of Molecular Biology 427 (7), 2015, 1589-1608 mehr… BibTeX Volltext ( DOI )
- Dimerization-dependent Folding Underlies Assembly Control of the Clonotypic αβT Cell Receptor Chains. Journal of Biological Chemistry 290 (44), 2015, 26821-26831 mehr… BibTeX Volltext ( DOI )