https://elifesciences.org/articles/38752
Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible...
Tuning of BiP activity by Fic-mediated AMPylation is required for Drosophila photoreceptor plasticity and attenuation of the unfolded protein response.
https://elifesciences.org/articles/12621/peer-reviews
Peer review in AMPylation matches BiP activity to client protein load in the endoplasmic reticulum...
Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.
https://elifesciences.org/articles/12621v1
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum | eLife
https://elifesciences.org/articles/12621
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum | eLife
Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.
https://www.frontiersin.org/journals/chemistry/articles/10.3389/fchem.2023.1077188/full
Frontiers | Catalytic deAMPylation in AMPylation-inhibitory/assistant forms of FICD protein
DeAMPylation, as a reversible reaction of AMPylation and mediated by the endoplasmic reticulum-localized enzyme FICD (filamentation induced by cAMP domain pr...
frontierscatalyticampylation