Evidence map›Paper›PMID 28433487›Full record

ReviewTrends in cell biology2017

rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.

Matthias C Truttmann, Hidde L Ploegh

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. The AMPylase FIC-1 modulates TGF-β signaling inFrontiers in molecular neuroscience · 2022
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Chaperone AMPylation modulates aggregation and toxicity of neurodegenerative disease-associated polypeptides.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Bio-protocol · 2017
    Article
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

2 authors at 1 institution in 1 country.

Matthias C TruttmannBoston Children's Hospital, Boston, MA, USA. Electronic address: matthias.truttmann@childrens.harvard.edu.
Hidde L PloeghBoston Children's Hospital, Boston, MA, USA; Massachusetts Institute of Technology, Cambridge, MA, USA. Electronic address: hidde.ploegh@childrens.harvard.edu.
Boston Children's Hospital · US

Funding

A new strategy to disrupt protein-protein interactions in eukaryotic cells.DP1GM106409 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2012 to 2016
$4.8M
Sortase-mediated protein engineering for the study of host-pathogen interactionsR01AI087879 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2010 to 2019
$4.5M
NIAID NIH HHS R01 AI087879NIGMS NIH HHS DP1 GM106409
6 · The paper itself

Abstract

Protein AMPylation - the covalent attachment of an AMP residue to amino acid side chains using ATP as the donor - is a post-translational modification (PTM) increasingly appreciated as relevant for both normal and pathological cell signaling. In metazoans single copies of filamentation induced by cAMP (fic)-domain-containing AMPylases - the enzymes responsible for AMPylation - preferentially modify a set of dedicated targets and contribute to the perception of cellular stress and its regulation. Pathogenic bacteria can exploit AMPylation of eukaryotic target proteins to rewire host cell signaling machinery in support of their propagation and survival. We review endogenous as well as parasitic protein AMPylation in metazoans and summarize current views of how fic-domain-containing AMPylases contribute to cellular proteostasis.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionStress, PhysiologicalAdenosine MonophosphateAnimalsBacterial ProteinsCarrier ProteinsEndoplasmic Reticulum Chaperone BiPHumansMembrane ProteinsNucleotidyltransferasesAdenosine MonophosphateBacterial ProteinsCarrier ProteinsEndoplasmic Reticulum Chaperone BiPFICD protein, humanHSPA5 protein, humanMembrane ProteinsNucleotidyltransferasesadenylylationendoplasmic reticulumGrp78/BiPheat shock proteinprotein aggregation

Identifiers

PMID28433487
PMCPMC5524611
OpenAlexW2605419678

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.