Dieter Willbold

UCS enables high-throughput single-cell proteomic analysis of blood samples, revealing disease-specific expression profiles and immune subpopulations in acute myeloid leukemia.

This study identifies single-stranded nucleic acids that enhance the catalytic activity of Chikungunya virus nsP2 protease through specific interactions.

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

This study evaluates pantinin-1, a scorpion venom peptide, as an inhibitor of CHIKV nsP2 protease, showing effective inhibition with low micromolar affinity and no toxicity.

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

This paper shows lecanemab binds to amyloid-β fibrils from Alzheimer's disease mouse models with flexible N-termini, including type-I, type-II, and Arctic folds, but not those with fixed N-termini like in tg-SwDI mice.

This paper expresses and characterizes native-like human prion protein with GPI-anchoring and glycosylation using Leishmania tarentolae, confirming its structural homogeneity and monomeric conformation.

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.

This paper develops all-D-peptide ligands that disassemble alpha-syn preformed fibrils into monomers, showing potential for treating Parkinson's disease.

This study introduces a split-tandem GABARAP construct to monitor its association with microtubules in living cells, revealing a robust interaction not observed with N-terminal fluorescent tags.

The paper presents cryo-EM structures of Aβ fibrils from Alzheimer's disease mouse models and compares them to human fibrils.

The paper demonstrates that SARS-CoV-2 spike protein binding to ACE2 involves a two-step process with a secondary rate transition that enhances complex stability, and this is also observed in the B.1.1.7 variant.

This study uses solid-state MAS NMR to investigate the structure of Aβ oligomers bound to huPrP, revealing conformational heterogeneity and β-strand content.