Evidence map›Paper›PMID 21655302›Full record

ArticlePLoS biology2011

N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.

Gabriella M A Forte, Martin R Pool, Colin J Stirling

Abstract read
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
–field-weighted citation impact
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

103 citing papers in PubMed.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. InPathogens (Basel, Switzerland) · 2025
    Article
  6. Review
  7. Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

43 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

3 authors.

Gabriella M A ForteFaculty of Life Sciences, University of Manchester, Manchester, United Kingdom.
Martin R Pool
Colin J Stirling

Funding

Biotechnology and Biological Sciences Research Council BB/H007202Biotechnology and Biological Sciences Research Council BB/H007202/1Wellcome Trust 74149
6 · The paper itself

Abstract

Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway. While cytosolic proteins were profoundly biased in favour of processing, we found an equal and opposite bias against such modification for secretory proteins. Mutations in secretory signal sequences that led to their acetylation resulted in mis-sorting to the cytosol in a manner that was dependent upon the N-terminal processing machinery. Hence N-terminal acetylation represents an early determining step in the cellular sorting of nascent polypeptides that appears to be conserved across a wide range of species.

Indexed as

Protein TransportAcetylationComputational BiologyCytosolEndoplasmic ReticulumProtein Processing, Post-TranslationalProtein Sorting SignalsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein Sorting SignalsSaccharomyces cerevisiae Proteins

Identifiers

PMID21655302
PMCPMC3104963

What OpenQuestion holds

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LicenceCC BY
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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.