Methods to direct the degradation of protein targets with proximity-inducing molecules that
coopt the cellular degradation machinery are advancing in leaps and bounds, and diverse …

Specificity of eukaryotic protein degradation is determined by E3 ubiquitin ligases and their
selective binding to protein motifs, termed" degrons," in substrates for ubiquitin-mediated …

In 2008, we published the first set of guidelines for standardizing research in autophagy.
Since then, this topic has received increasing attention, and many scientists have entered …

Protein modifications provide cells with exquisite temporal and spatial control of protein
function. Ubiquitin is among the most important modifiers, serving both to target hundreds of …

INTRODUCTION Cells synthesize glucose if deprived of it, and destroy gluconeogenic
enzymes upon return to glucose-replete conditions. Gluconeogenesis (de novo synthesis of …

Saccharomyces cerevisiae preferentially uses glucose as a carbon source, but following its
depletion, it can utilize a wide variety of other carbons including nonfermentable compounds …

Targeted protein degradation (TPD) strategies exploit bivalent small molecules to bridge
substrate proteins to an E3 ubiquitin ligase to induce substrate degradation. Few E3s have …

Ubiquitylation is catalyzed by coordinated actions of E3 and E2 enzymes. Molecular
principles governing many important E3-E2 partnerships remain unknown, including those …

How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by
studying the yeast GID complex (mutation of which causes deficiency in glucose-induced …

A diverse antibody repertoire is essential for humoral immunity. Antibody diversification
requires the introduction of deoxyuridine (dU) mutations within immunoglobulin genes to …