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Selected Publication:
SHR Neuro Cancer Cardio Lipid Metab Microb
Zhang, F; Kerbl-Knapp, J; Rodriguez Colman, MJ; Meinitzer, A; Macher, T; Vujic, N; Fasching, S; Jany-Luig, E; Korbelius, M; Kuentzel, KB; Mack, M; Akhmetshina, A; Pirchheim, A; Paar, M; Rinner, B; Hörl, G; Steyrer, E; Stelzl, U; Burgering, B; Eisenberg, T; Pertschy, B; Kratky, D; Madl, T. .
Global analysis of protein arginine methylation.
Cell reports methods. 2021; 1(2):
Doi: 10.1016/j.crmeth.2021.100016
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- Leading authors Med Uni Graz
- Madl Tobias
- Zhang Fangrong
- Co-authors Med Uni Graz
- Akhmetshina Alena
- Eisenberg Tobias
- Hörl Gerd
- Kerbl-Knapp Jakob
- Korbelius Melanie
- Kratky Dagmar
- Küntzel Katharina Barbara
- Macher Therese
- Mack Maximilian
- Meinitzer Andreas
- Paar Margret
- Pirchheim Anita
- Rinner Beate
- Steyrer Ernst
- Vujic Nemanja
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- Abstract:
- Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.