- Trentini DB, Pecoraro M, Tiwary S, Cox J, Mann M, Hipp MS, and Hartl FU (2020) Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation. Proc Natl Acad Sci U S A., 117(8): 4099-4108.
Winner of the Junior Scientists' Publication Award 2020 of the Max Planck Institute of Biochemistry https://twitter.com/MPI_Biochem/status/1284128946192289795?s=20
See the comment about this paper at the Nature Research Microbiology Community: https://go.nature.com/3e1XggL. Many thanks to Marcin Suskiewicz for highlighting our story!
- Trentini DB*, Suskiewicz MJ*, Heuck A, Kurzbauer R, Deszcz L, Mechtler K, and Clausen T (2016) Arginine phosphorylation marks proteins for degradation by a Clp protease. Nature.539: 48.*equal contribution
This paper has been graded “exceptional” 4 times in the F1000Prime/Faculty Opinions platform! See opinions at: https://facultyopinions.com/prime/726854959
Discussed in Nature’s News and Views https://www.nature.com/articles/539038a and in Nature Reviews Microbiology https://www.nature.com/articles/nrmicro.2016.159
Read the “behind the paper” story at http://go.nature.com/2hUgM5y
- Trentini DB, Fuhrmann J, Mechtler K, and Clausen T (2014) Chasing phosphoarginine proteins: development of a selective enrichment method using a phosphatase trap. Mol Cell Proteomics. 13: 1953-1964.
- Schmidt A*, Trentini DB*, Spiess S, Fuhrmann J, Ammerer G, Mechtler K, and Clausen T (2014) Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response. Mol Cell Proteomics.13: 537-550. *equal contribution
One of the highlights of Mol Cell Proteomics Vol. 13, Issue 2
- Fuhrmann J, Mierzwa B, Trentini DB, Spiess S, Lehner A, Charpentier E, Clausen T (2013) Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria. Cell Rep. 3(6): 1832-9.
- Sant'Anna FH*, Trentini DB*, de Souto Weber S, Cecagno R, da Silva SC, Schrank IS. (2009) The PII superfamily revised: a novel group and evolutionary insights. J Mol Evol. 68(4): 322-36. *equal contribution