Evidence map›Paper›PMID 20885971›Full record

ReviewArchaea (Vancouver, B.C.)2010

Protein acetylation in archaea, bacteria, and eukaryotes.

Jörg Soppa

Open access · hybridAbstract readReview
In one paragraph

Review in Archaea (Vancouver, B.C.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

66 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Studying the long-term adaptation ofFrontiers in microbiology · 2025
    Article
  8. Article
  9. The role ofFrontiers in cellular and infection microbiology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review
  17. Review
  18. A Retrospective on eIF2A-and Not the Alpha Subunit of eIF2.International journal of molecular sciences · 2020
    Review
  19. Article
  20. Article

6 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

1 author at 1 institution in 1 country.

Jörg SoppaInstitute for Molecular Biosciences, Goethe University, Max-von-Laue-Strasse 9, 60438 Frankfurt, Germany. soppa@bio.uni-frankfurt.de
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins can be acetylated at the alpha-amino group of the N-terminal amino acid (methionine or the penultimate amino acid after methionine removal) or at the epsilon-amino group of internal lysines. In eukaryotes the majority of proteins are N-terminally acetylated, while this is extremely rare in bacteria. A variety of studies about N-terminal acetylation in archaea have been reported recently, and it was revealed that a considerable fraction of proteins is N-terminally acetylated in haloarchaea and Sulfolobus, while this does not seem to apply for methanogenic archaea. Many eukaryotic proteins are modified by differential internal acetylation, which is important for a variety of processes. Until very recently, only two bacterial proteins were known to be acetylation targets, but now 125 acetylation sites are known for E. coli. Knowledge about internal acetylation in archaea is extremely limited; only two target proteins are known, only one of which--Alba--was used to study differential acetylation. However, indications accumulate that the degree of internal acetylation of archaeal proteins might be underestimated, and differential acetylation has been shown to be essential for the viability of haloarchaea. Focused proteomic approaches are needed to get an overview of the extent of internal protein acetylation in archaea.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesArchaeaArchaeal ProteinsEscherichia coliEukaryotaAcetyltransferasesArchaeal Proteins

Identifiers

PMID20885971
PMCPMC2946573
OpenAlexW2051870213

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.