Ulrich Stelzl

This study identifies acid phospholipase A1's role in lysosomal glycerophospholipid catabolism and shows its interaction with bis(monoacylglycero)phosphate and inhibition by cationic amphiphilic drugs.

The paper identifies Sni445 as a novel factor that recruits snR4 and snR45 snoRNPs to 90S pre-ribosomes, enabling Kre33-mediated acetylation of 18S rRNA.

The paper describes a non-canonical phospholipid synthesis pathway catalyzed by CLN8, leading to BMP synthesis and revealing its role in lysosomal lipid homeostasis and Batten disease.

The paper identifies PRMT5-CDK4 complex formation as a non-enzymatic regulator of cell cycle signaling, showing it modulates CDK4 interactions and mimics CDK4 inhibition.

The paper studies the evolution of protein interactions in the Drosophila piRNA pathway, revealing conserved and co-evolved interactions that support evolutionary adaptation.

The paper identifies switch mutations in ATGL that selectively disrupt interactions with specific regulatory proteins, linking these mutations to altered lipolysis activity and disease relevance.

This study identifies 51 direct interactions between SARS-CoV-2 proteins and human kinases, revealing altered kinase activity patterns and highlighting FER kinase inhibition by ORF6.

The paper identifies missense variants in NF2 that affect its conformation and tumor suppressor function through systematic mutational interaction perturbation analysis.

The paper uses phospho-proteomics in yeast to identify distinct phosphorylation motifs for BCR-ABL kinase isoforms compared to wild-type ABL1, showing altered substrate specificity.

The paper develops a human kinase yeast array to assess kinase activities and identify kinases modulating phosphorylation-dependent protein-protein interactions.

The paper develops an NMR-based method to quantify global protein arginine methylation levels across various biological samples and demonstrates its prevalence and modulation in health and disease.

Proximity-dependent biotinylation (BioID) of 28 SARS-CoV-2 proteins in human cells maps 5,415 proximal interactions with 2,128 host targets across basal and poly(I:C) conditions.