Ubiquitination, an important type of protein posttranslational modification (PTM), plays a
crucial role in controlling substrate degradation and subsequently mediates the “quantity” …

The post-translational modification of proteins with ubiquitin plays a central role in nearly all
aspects of eukaryotic biology. Historically, studies have focused on the conjugation of …

The protein complex crystallographic beamline BL19U1 at the Shanghai Synchrotron
Radiation Facility is one of the five beamlines dedicated to protein sciences operated by …

Enzymes with a protein kinase fold transfer phosphate from adenosine 5′-triphosphate
(ATP) to substrates in a process known as phosphorylation. Here, we show that the …

Grazing of amoebae on microorganisms represents one of the oldest predator-prey dynamic
relationships in nature. It represents a genetic “melting pot” for an ancient and continuous …

Legionella pneumophila grows intracellularly within the membrane-bound Legionella-
containing vacuole (LCV) established by proteins translocated via the bacterial type IV …

The family of bacterial SidE enzymes catalyzes non-canonical phosphoribosyl-linked (PR)
serine ubiquitination and promotes infectivity of Legionella pneumophila. Here, we describe …

Regulation through post‐translational ubiquitin signaling underlies a large portion of
eukaryotic biology. This has not gone unnoticed by invading pathogens, many of which have …

Pseudokinases are considered to be the inactive counterparts of conventional protein
kinases and comprise approximately 10% of the human and mouse kinomes. Here, we …

Posttranslational protein modification by ubiquitin (Ub) is a central eukaryotic mechanism
that regulates a plethora of physiological processes. Recent studies unveiled an …