Evidence map›Paper›PMID 27918543›Full record

ArticleNature structural & molecular biology2017

FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.

Steffen Preissler, Claudia Rato, Luke Perera, Vladimir Saudek, David Ron

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
6.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed, 110 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
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  5. Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  8. Article
  9. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
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  19. FicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Steffen Preissler *Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Claudia Rato *Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Luke PereraCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Vladimir SaudekInstitute of Metabolic Science, University of Cambridge, Cambridge, United Kingdom.
David RonCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
University of Cambridge · GB

Funding

Medical Research CouncilWellcome Trust 100140Wellcome Trust 200848
6 · The paper itself

Abstract

Protein folding homeostasis in the endoplasmic reticulum (ER) is defended by an unfolded protein response that matches ER chaperone capacity to the burden of unfolded proteins. As levels of unfolded proteins decline, a metazoan-specific FIC-domain-containing ER-localized enzyme (FICD) rapidly inactivates the major ER chaperone BiP by AMPylating T518. Here we show that the single catalytic domain of FICD can also release the attached AMP, restoring functionality to BiP. Consistent with a role for endogenous FICD in de-AMPylating BiP, FICD

Indexed as

Protein Processing, Post-TranslationalAdenosine MonophosphateAnimalsBiocatalysisCarrier ProteinsCatalytic DomainCHO CellsCricetinaeCricetulusEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHEK293 CellsHumansKineticsMembrane ProteinsNucleotidyltransferasesAdenosine MonophosphateCarrier ProteinsEndoplasmic Reticulum Chaperone BiPFICD protein, humanHeat-Shock ProteinsMembrane ProteinsNucleotidyltransferases

Identifiers

PMID27918543
PMCPMC5221731
OpenAlexW2560463443

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.