H. Schuler

Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15

This study shows that PARP15's ADP-ribosyltransferase activity is regulated by dimerization, with dimers required for catalytic function and monomers inactive.

Modelling single-stress omics integration with HIVE enables the identification of responding signatures to multifactorial stress combinations in plants

HIVE integrates single-stress transcriptomics data to identify gene signatures responding to multifactorial stress combinations in plants.

PARP14 is a writer, reader and eraser of mono-ADP-ribosylation

This study identifies PARP14 and PARP9 macrodomain-1 as ADP-ribosyl glycohydrolases, expanding the known human ADP-ribosyl glycohydrolase family to eight members.

The bacterial community of the European spruce bark beetle in space and time

This study analyzes the bacterial communities of the European spruce bark beetle across different populations and seasons, finding variation in community structure but no difference between epidemic and endemic populations.

Division of labour within psyllids: Metagenomics reveals an ancient dual endosymbiosis with metabolic complementarity in the genus Cacopsylla

The paper identifies a dual endosymbiosis in psyllids, revealing a new bacterial symbiont that complements the metabolic functions of the primary endosymbiont.

The genomics of trait combinations and their influence on adaptive divergence

The paper investigates how genetic correlations between traits influence adaptive divergence in apple maggot flies, showing that antagonistic pleiotropy shapes genomic footprints of rapid adaptation.

System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA)

SIESTA identifies and prioritizes enzyme substrates by detecting thermal stability changes caused by post-translational modifications, demonstrating effectiveness across multiple enzyme systems.

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface

This study identifies a novel hydrophobic interface between 14-3-3 proteins and Pseudomonas exotoxins-S and -T, showing 14-3-3 activates these toxins by preventing aggregation, independent of their C-terminal phosphopeptide binding motifs.