Oliver H. Weiergräber

This paper develops N-methylated and stapled peptide ligands for GABARAP with low nanomolar affinity and subfamily selectivity.

This paper introduces RFpeptides, a deep learning framework for designing high-affinity macrocyclic peptides, achieving sub-nanomolar binding affinities and accurate structural predictions.

The paper introduces the IWQ model to explain temperature-dependent protein function and links body temperatures to water quantum transitions at protein interfaces.

The paper investigates the binding affinity of GW5074 to LC3B and GABARAP using an AlphaScreen assay, finding micromolar inhibitory potencies and suggesting potential for targeted protein degradation.

The paper identifies a GABARAP binding site on EGFR and shows its role in EGFR degradation through biophysical and structural analysis.