Dirk Schwarzer

Summary

Country: Germany

Publications

  1. Schmohl L, Schwarzer D. Sortase-mediated ligations for the site-specific modification of proteins. Curr Opin Chem Biol. 2014;22:122-8 pubmed publisher
  2. Schmohl L, Wagner F, Schümann M, Krause E, Schwarzer D. Semisynthesis and initial characterization of sortase A mutants containing selenocysteine and homocysteine. Bioorg Med Chem. 2015;23:2883-9 pubmed publisher
    ..These observations provide information on sortase catalysis and the semisynthetic enzymes might represent useful tools for further biochemical investigations and engineering approaches of sortases A. ..
  3. Jost J, Hanswillemenke A, Schwarzer D. A miniaturized readout strategy for endogenous histone deacetylase activity. Mol Biosyst. 2015;11:1820-3 pubmed publisher
    ..We have developed a miniaturized assay for the multi-site readout of deacetylase activity and profiled the substrate selectivity of HDACs for acetylation sites on histone H4 and tumor suppressor protein p53. ..
  4. Fischle W, Mootz H, Schwarzer D. Synthetic histone code. Curr Opin Chem Biol. 2015;28:131-40 pubmed publisher
    ..We summarize pioneering experiments and recent developments in this exciting field of chemical biology. ..
  5. Dose A, Sindlinger J, Bierlmeier J, Bakirbas A, Schulze Osthoff K, Einsele Scholz S, et al. Interrogating Substrate Selectivity and Composition of Endogenous Histone Deacetylase Complexes with Chemical Probes. Angew Chem Int Ed Engl. 2016;55:1192-5 pubmed publisher
    ..These results underline the utility of the newly established probes for deciphering not only activity, but also substrate selectivity and composition of endogenous HDAC complexes, which can hardly be achieved otherwise. ..
  6. Seidel J, Klockenbusch C, Schwarzer D. Investigating Deformylase and Deacylase Activity of Mammalian and Bacterial Sirtuins. Chembiochem. 2016;17:398-402 pubmed publisher
    ..These investigations further showed that SrtN and human SIRT1 are efficient lysine-deformylases, thereby providing a first clue as to how this nonenzymatic modification might be removed from affected proteins. ..
  7. Schmohl L, Bierlmeier J, von Kügelgen N, Kurz L, Reis P, Barthels F, et al. Identification of sortase substrates by specificity profiling. Bioorg Med Chem. 2017;25:5002-5007 pubmed publisher
    ..Streptococci sortases prefer an LPKLG donor substrate sequence compared to the canonical sorting motif LPKTG. These findings might facilitate the use of Streptococci sortases as tools of protein chemistry. ..