Evidence map›Paper›PMID 24743167›Full record

ArticleCell cycle (Georgetown, Tex.)2014

Transamidase subunit GAA1/GPAA1 is a M28 family metallo-peptide-synthetase that catalyzes the peptide bond formation between the substrate protein's omega-site and the GPI lipid anchor's phosphoethanolamine.

Birgit Eisenhaber, Stephan Eisenhaber, Toh Yew Kwang, Gerhard Grüber, Frank Eisenhaber

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-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

27 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Molecular Insights into Fungal Glycosylphosphatidylinositol Transamidase Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Review
  4. Review
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  6. Review
  7. [Glycosylphosphatidylinositol biosynthesis deficiency 15 caused byZhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. International journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. The Temperature-Dependent Retention of Introns inInternational journal of molecular sciences · 2019
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Birgit EisenhaberBioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore.
Stephan EisenhaberDepartment of Physical Chemistry; University of Vienna; Wien/Vienna, Republic of Austria.
Toh Yew KwangBioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore.
Gerhard GrüberBioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore; Nanyang Technological University; School of Biological Sciences; Singapore, Republic of Singapore.
Frank EisenhaberBioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore; Department of Biological Sciences (DBS); National University of Singapore (NUS); Singapore, Republic of Singapore; School of Computer Engineering (SCE); Nanyang Technological University (NTU); Singapore, Republic of Singapore.
A*STAR Graduate Academy · SGBioinformatics Institute · SGNational University of Singapore · SGUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transamidase subunit GAA1/GPAA1 is predicted to be the enzyme that catalyzes the attachment of the glycosylphosphatidyl (GPI) lipid anchor to the carbonyl intermediate of the substrate protein at the ω-site. Its ~300-amino acid residue lumenal domain is a M28 family metallo-peptide-synthetase with an α/β hydrolase fold, including a central 8-strand β-sheet and a single metal (most likely zinc) ion coordinated by 3 conserved polar residues. Phosphoethanolamine is used as an adaptor to make the non-peptide GPI lipid anchor look chemically similar to the N terminus of a peptide.

Indexed as

AminoacyltransferasesEthanolaminesGlycosylphosphatidylinositolsHumansMembrane GlycoproteinsPeptidesPeptide SynthasesProtein CarbonylationProtein SubunitsAminoacyltransferasesEthanolaminesGlycosylphosphatidylinositolsGPAA1 protein, humanMembrane GlycoproteinsPeptidesPeptide SynthasesphosphorylethanolamineProtein SubunitstransamidasesGAA1GPAA1GPI lipid anchorGPI transamidaseM28 peptidasemetallo-peptide-synthetaseprotein sequencesequence analysis

Identifiers

PMID24743167
PMCPMC4111754
OpenAlexW1991883956

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.