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1. Discovery of a novel class of highly potent inhibitors of the p53–MDM2 interaction by structure-based design starting from a conformational argument. Issue 19 (1st October 2016)

2. Front Cover: Structural States of Hdm2 and HdmX: X‐ray Elucidation of Adaptations and Binding Interactions for Different Chemical Compound Classes (ChemMedChem 14/2019). (17th July 2019)

3. In vitro and in vivo characterization of a novel, highly potent p53-MDM2 inhibitor. Issue 20 (1st November 2018)

4. N-aryl-piperidine-4-carboxamides as a novel class of potent inhibitors of MALT1 proteolytic activity. Issue 12 (1st July 2018)

5. Requirement of Mucosa‐Associated Lymphoid Tissue Lymphoma Translocation Protein 1 Protease Activity for Fcγ Receptor–Induced Arthritis, but Not Fcγ Receptor–Mediated Platelet Elimination, in Mice. Issue 6 (26th April 2020)

6. Stabilizing Inactive Conformations of MALT1 as an Effective Approach to Inhibit Its Protease Activity. Issue 9 (17th June 2020)

7. Structural States of Hdm2 and HdmX: X‐ray Elucidation of Adaptations and Binding Interactions for Different Chemical Compound Classes. (27th May 2019)

8. The T‐cell fingerprint of MALT1 paracaspase revealed by selective inhibition. Issue 1 (21st December 2017)