Evidence map›Paper›PMID 29760078›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Chaperone AMPylation modulates aggregation and toxicity of neurodegenerative disease-associated polypeptides.

Matthias C Truttmann, David Pincus, Hidde L Ploegh

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Review
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  9. Article
  10. Review
  11. Article
  12. Review
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  14. Article
  15. Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022
    Article
  16. Oxidative medicine and cellular longevity · 2022
    Article
  17. The AMPylase FIC-1 modulates TGF-β signaling inFrontiers in molecular neuroscience · 2022
    Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Matthias C TruttmannProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA; 02115; hidde.ploegh@childrens.harvard.edu matthias.truttmann@childrens.harvard.edu.
David PincusWhitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142.
Hidde L PloeghProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA; 02115; hidde.ploegh@childrens.harvard.edu matthias.truttmann@childrens.harvard.edu.ORCID 0000-0002-1090-6071
Boston Children's Hospital · USWhitehead Institute for Biomedical Research · US

Funding

Quantitative approaches to reveal the homeostatic control mechanisms of stress reDP5OD017941 · OD · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PINCUS, DAVID · 2013 to 2017
$2.4M
NIH HHS DP5 OD017941
6 · The paper itself

Abstract

Proteostasis is critical to maintain organismal viability, a process counteracted by aging-dependent protein aggregation. Chaperones of the heat shock protein (HSP) family help control proteostasis by reducing the burden of unfolded proteins. They also oversee the formation of protein aggregates. Here, we explore how AMPylation, a posttranslational protein modification that has emerged as a powerful modulator of HSP70 activity, influences the dynamics of protein aggregation. We find that adjustments of cellular AMPylation levels in

Indexed as

Adenosine Monophosphatealpha-SynucleinAmyloidAmyloid beta-PeptidesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesNeurodegenerative DiseasesNucleotidyltransferasesPeptidesProtein Aggregation, PathologicalProtein Processing, Post-TranslationalProteostasisAdenosine Monophosphatealpha-SynucleinAmyloidAmyloid beta-PeptidesCaenorhabditis elegans ProteinsFIC-1 protein, C elegansHSP70 Heat-Shock ProteinsMolecular ChaperonesNucleotidyltransferasesPeptidesAMPylationchaperonesHsp70protein aggregationproteostasis

Identifiers

PMID29760078
PMCPMC5984528
OpenAlexW2753879466

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.