O. Burlet-Schiltz

Extra-cellular matrix remodeling as a unique mechanism of expansion of periprostatic adipose tissue: a potential driver of prostate cancer aggressiveness

The paper defines abundant periprostatic adipose tissue using a statistical approach and shows it is associated with prostate cancer aggressiveness through extracellular matrix remodeling.

LptM promotes oxidative maturation of the lipopolysaccharide translocon by substrate binding mimicry.

This study identifies LptM as a conserved lipoprotein that facilitates oxidative maturation of the LPS translocon by mimicking LPS binding, enabling efficient disulfide bond formation in LptD.

In depth exploration of the alternative proteome of Drosophila melanogaster

This study identifies 401 alternative proteins in Drosophila melanogaster through peptidomics, showing some are more abundant than canonical proteins and exhibit developmentally regulated or stress-induced expression.

Human Cytomegalovirus modifies placental small extracellular vesicle secretion and composition towards a proviral phenotype to enhance infection of fetal recipient cells

This study shows hCMV infection alters placental sEVs to promote viral spread to fetal cells.

SDR enzymes oxidize specific lipidic alkynylcarbinols into cytotoxic protein-reactive species

The paper identifies SDR enzymes as bioactivators of lipidic alkynylcarbinols, converting them into cytotoxic electrophiles that modify proteins and induce cell death.

Phosphoproteomics identifies PI3K inhibitor-selective adaptive responses in pancreatic cancer cell therapy and resistance

This study identifies adaptive phosphoprotein responses to isoform-selective PI3K inhibitors in pancreatic cancer, showing that combination therapy can overcome resistance.

Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependant inter-ring crosstalks

The paper uses HDX-MS to show conformational differences between human 20S proteasomes and their PA28 activators, revealing allosteric changes upon binding.

PIP30/FAM192A is a novel regulator of the nuclear proteasome activator PA28gamma

This paper identifies PIP30/FAM192A as a novel cofactor of PA28gamma, showing it binds to PA28gamma and modulates its interactions with the 20S proteasome and coilin.