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Gruppiert nach: Dokumententyp | Veröffentlichungsdatum
Springe zu: 2021 | 2020 | 2019 | 2018 | 2017 | 2016
Anzahl der Publikationen: 12

2021

Schumacher, Dominik; Harms, Andrea; Bergeler, Silke; Frey, Erwin und Sogaard-Andersen, Lotte (2021): PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus. In: eLife, Bd. 10, e66160 [PDF, 6MB]

2020

Kasper, Marc-Andre; Gerlach, Marcus; Schneider, AnseIm F. L.; Groneberg, Christiane; Ochtrop, Philipp; Boldt, Stefanie; Schumacher, Dominik; Helma, Jonas; Leonhardel, Heinrich; Christmann, Mathias und Hackenberger, Christian P. R. (2020): N-Hydroxysuccinimide-Modified Ethynylphosphonamidates Enable the Synthesis of Configurationally Defined Protein Conjugates. In: Chembiochem, Bd. 21: S. 113-119

2019

Kasper, Marc-Andre; Glanz, Maria; Stengl, Andreas; Penkert, Martin; Klenk, Simon; Sauer, Tom; Schumacher, Dominik; Helma, Jonas; Krause, Eberhard; Cardoso, M. Cristina; Leonhardt, Heinrich und Hackenberger, Christian P. R. (2019): Cysteine-Selective Phosphonamidate Electrophiles for Modular Protein Bioconjugations. In: Angewandte Chemie-International Edition, Bd. 58, Nr. 34: S. 11625-11630

Kasper, Marc-Andre; Stengl, Andreas; Ochtrop, Philipp; Gerlach, Marcus; Stoschek, Tina; Schumacher, Dominik; Helma, Jonas; Penkert, Martin; Krause, Eberhard; Leonhardt, Heinrich und Hackenberger, Christian P. R. (2019): Ethynylphosphonamidates for the Rapid and Cysteine-Selective Generation of Efficacious Antibody-Drug Conjugates. In: Angewandte Chemie-International Edition, Bd. 58, Nr. 34: S. 11631-11636

Stengl, Andreas; Gerlach, Marcus; Kasper, Marc-Andre; Hackenberger, Christian P. R.; Leonhardt, Heinrich; Schumacher, Dominik und Helma, Jonas (2019): TuPPL: Tub-tag mediated C-terminal protein-protein-ligation using complementary click-chemistry handles. In: Organic & Biomolecular Chemistry, Bd. 17, Nr. 20: S. 4964-4969

Effenberger, Manuel; Stengl, Andreas; Schober, Kilian; Gerget, Maria; Kampick, Maximilian; Müller, Thomas R.; Schumacher, Dominik; Helma, Jonas; Leonhardt, Heinrich und Busch, Dirk H. (2019): FLEXamers: A Double Tag for Universal Generation of Versatile Peptide-MHC Multimers. In: Journal of Immunology, Bd. 202, Nr. 7: S. 2164-2171

2018

Schumacher, Dominik; Helma-Smets, Jonas; Hackenberger, Christian und Leonhardt, Heinrich (2018): Neue Generation von Antikörper‐Wirkstoff‐Konjugaten. Start‐Ups. In: Chemie in Unserer Zeit, Bd. 52, Nr. 2: S. 80-82

Schumacher, Dominik; Helma, Jonas; Schneider, Anselm F. L.; Leonhardt, Heinrich und Hackenberger, Christian P. R. (2018): Nanobodies: Chemical Functionalization Strategies and Intracellular Applications. In: Angewandte Chemie-International Edition, Bd. 57, Nr. 9: S. 2314-2333

2017

Schumacher, Dominik; Bergeler, Silke; Harms, Andrea; Vonck, Janet; Huneke-Vogt, Sabrina; Frey, Erwin und Sogaard-Andersen, Lotte (2017): The PomXYZ Proteins Self-Organize on the Bacterial Nucleoid to Stimulate Cell Division. In: Developmental Cell, Bd. 41, Nr. 3: S. 299-314

Herce, Henry D.; Schumacher, Dominik; Schneider, Anselm F. L.; Ludwig, Anne K.; Mann, Florian A.; Fillies, Marion; Kasper, Marc-Andre; Reinke, Stefan; Krause, Eberhard; Leonhardt, Heinrich; Cardoso, M. Cristina und Hackenberger, Christian P. R. (2017): Cell-permeable nanobodies for targeted immunolabelling and antigen manipulation in living cells. In: Nature Chemistry, Bd. 9, Nr. 8: S. 762-771

Schumacher, Dominik; Lemke, Oliver; Helma, Jonas; Gerszonowicz, Lena; Waller, Verena; Stoschek, Tina; Durkin, Patrick M.; Budisa, Nediljko; Leonhardt, Heinrich; Keller, Bettina G. und Hackenberger, Christian P. R. (2017): Broad substrate tolerance of tubulin tyrosine ligase enables one-step site-specific enzymatic protein labeling. In: Chemical Science, Bd. 8, Nr. 5: S. 3471-3478

2016

Schumacher, Dominik; Hackenberger, Christian P. R.; Leonhardt, Heinrich und Helma, Jonas (2016): Current Status: Site-Specific Antibody Drug Conjugates. In: Journal of Clinical Immunology, Bd. 36: S100-S107

Diese Liste wurde am Sat Mar 23 21:46:39 2024 CET erstellt.