Publications @ the Gevaert Group
- Aksnes, H. et al. An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. Cell Rep 10, 1362–1374 (2015).
- Van Damme, P., Støve, S. I., Glomnes, N., Gevaert, K. & Arnesen, T. A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutant. Mol. Cell Proteomics 13, 2031–2041 (2014).
- Staes, A. et al. Selecting protein N-terminal peptides by combined fractional diagonal chromatography. Nat. Protoc 6, 1130–1141 (2011).
- Van Damme, P. et al. Complementary positional proteomics for screening substrates of endo- and exoproteases. Nat. Methods 7, 512–515 (2010).
- Colaert, N., Helsens, K., Martens, L., Vandekerckhove, J. & Gevaert, K. Improved visualization of protein consensus sequences by iceLogo. Nat. Methods 6, 786–787 (2009).
- Gevaert, K. et al. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21, 566–569 (2003).
- Organellar Omics-A Reviving Strategy to Untangle the Biomolecular Complexity of the Cell.
- Isolation of protein complexes from the model legume Medicago truncatula by tandem affinity purification in hairy root cultures.
- Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.
- Proteogenomics in Aid of Host-Pathogen Interaction Studies: A Bacterial Perspective.
- Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.
- The ROS Wheel: Refining ROS Transcriptional Footprints.
- Gold nanodome SERS platform for label-free detection of protease activity.
- Identification of a novel mechanism of blood-brain communication during peripheral inflammation via choroid plexus-derived extracellular vesicles.
- Ectopic application of the repressive histone modification H3K9me2 establishes post-zygotic reproductive isolation in Arabidopsis thaliana.
- Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.