The article: Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry., Journal of Proteome Research, 2013 (DOI: 10.3410/f.717997979.793474359), has been selected for F1000Prime. It was recommended as being of special significance in its…
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The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases. Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins…
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SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma.
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Chemical probes are urgently needed to functionally annotate hitherto-untargeted kinases and stimulate new drug discovery efforts to address unmet medical needs. The size of the human kinome combined with the high cost associated with probe generation severely limits access to new probes. We propose…
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We are proud to announce that Karl Kramer, Group Leader Cell Biology of the institute, has been awarded the 2012 Life Science Teaching Award of the Faculty of Biosciences, Technische Universität München.
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Our research article 'Discovery of O-GlcNAc-6-phosphate Modified Proteins in Large-scale Phosphoproteomics Data' is featured as highlight in the October 2012 issue of Molecular and Cellular Proteomics. The article describes the discovery of 23 O-GlcNAc-6-phosphate modified peptides corresponding to…
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The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription and translation. It is further presumed that…
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