Associated Papers
The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP.
Runge S et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
Discovery and validation of a novel inhibitor of HYPE-mediated AMPylation.
Camara A et al.
Cell Stress & Chaperones, 2024
Infancy-onset diabetes caused by de-regulated AMPylation of the human endoplasmic reticulum chaperone BiP.
Perera LA et al.
Embo Molecular Medicine, 2023
36704923 (PubMed )
Supplement: EMMM-15-e16491-s002.pdf
A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP).
Li H et al.
Protein Science : a Publication of the Protein Society, 2022
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.
Perera LA et al.
Nature Communications, 2021
Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.
Fauser J et al.
Nature Communications, 2021
33893288 (PubMed )
Supplement: 41467_2021_22596_MOESM1_ESM.pdf
An oligomeric state-dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP.
Perera LA et al.
The Embo Journal, 2019
The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.
Pobre KFR et al.
The Journal of Biological Chemistry, 2019
MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP.
Yan Y et al.
Nature Communications, 2019
Fic-mediated deAMPylation is not dependent on homodimerization and rescues toxic AMPylation in flies.
Casey AK et al.
The Journal of Biological Chemistry, 2017
A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response.
Amin-Wetzel N et al.
Cell, 2017
AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.
Preissler S et al.
Elife, 2017
FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.
Preissler S et al.
Nature Structural & Molecular Biology, 2017
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum.
Preissler S et al.
Elife, 2015
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Yang J et al.
Structure (london, England : 1993), 2015
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