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Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.

The metabolite 2-hydroxybutyrate is an important aspect of exhaustion which leads to increased capacity in the branched chain amino acid degradation pathway.

Interdomain linker-mediated oligomerization of the endoplasmic reticulum chaperone protein BiP responds to the unfolded protein burden

The polymerase activity of PARP1 is converted to hydrolase activity upon binding of Histone Parylation Factor 1 (HPF1) with nucleosome activators.

DePARylation is essential for cell survival and thus poly(ADP-ribose) glycohydrolase (PARG) expression correlates with cytotoxicity induced by PARG inhibition, which will benefit the development of PARG inhibitors for cancer treatment.

Biochemical and structural analyses reveal direct ubiquitin modification of single-stranded nucleic acids, catalysed by the DTX3L ubiquitin ligase.

Non-synaptic extracellular vesicles may be involved in the release of endogenous cannabinoids in the central nervous system thereby representing a novel mechanism to mediate their effects on synaptic transmission.

ADP-ribosylation factor-like GTPase 15, an atypical small GTPase, binds to cystathionine-β-synthase-pair domain divalent metal cation transport mediator (CNNM) membrane proteins to inhibit divalent cation efflux by CNNM proteins and influx by transient receptor potential ion channel subfamily M member 7.

Identification of PARP1 trapping as the major contributor of PARP1 inhibitor-induced innate immune response.