R. Hartmann-Petersen

This study maps Parkin missense variants' abundance and degradation mechanisms, showing most low-abundance variants are degraded via the ubiquitin-proteasome system and stabilized at lower temperatures.

The paper characterizes mechanisms of human glucokinase variants by analyzing their abundance and stability, identifying residues that affect metabolic stability and conformational dynamics.

The paper shows two rare COMT missense variants are structurally unstable, leading to proteasomal degradation and reduced enzyme levels, with degradation independent of COMT isoform.

The paper identifies lysine deserts in UPS proteins and shows that introducing lysines increases ubiquitylation, with functional consequences for protein stability and function.

This study compares the functional and structural differences between glutamate and aspartate in intrinsically disordered proteins using experimental and computational methods.

This paper introduces a machine learning method to predict functional sites in proteins by integrating sequence conservation and biophysical stability models, validated through experimental data on missense variants.

The paper identifies conserved degron features in yeast, viruses, and humans that govern quality control proteolysis, showing transmembrane domain-like sequences are key determinants of protein half-life.

The paper shows that Hsp70-binding motifs can function as PQC degrons, targeting misfolded proteins for degradation in yeast and human cells.

This paper demonstrates that the cationic amphipathic peptide ChIP effectively kills colistin-resistant Gram-negative pathogens in vivo.

The paper identifies two PQC degrons in DHFR that become exposed in disease-linked missense variants, leading to proteasomal degradation.

The paper analyzes variant effects on protein activity and abundance in NUDT15 and PTEN, finding that a third of variants cause loss of function and half of these also reduce abundance.

This study investigates the degradation pathway of a disease-linked ASPA variant, finding it is degraded via the proteasome and dependent on Hsp70 and Hsp110.

The paper identifies structural destabilization and degradation of MLH1 variants in Lynch syndrome, linking reduced cellular levels to loss-of-function and suggesting stability predictions for diagnostic use.

The paper classifies PTEN missense variants as pathogenic or benign using experimental and computational methods, finding that ~60% of pathogenic variants destabilize the protein.