Evidence map›Paper›PMID 21795704›Full record

ArticleThe Journal of biological chemistry2011

The assembly of proline-rich membrane anchor (PRiMA)-linked acetylcholinesterase enzyme: glycosylation is required for enzymatic activity but not for oligomerization.

Vicky P Chen, Roy C Y Choi, Wallace K B Chan, K Wing Leung, Ava J Y Guo, Gallant K L Chan, Wilson K W Luk, Karl W K Tsim

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Acetylcholinesterase: Structure, dynamics, and interactions with organophosphorus compounds.Protein science : a publication of the Protein Society · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Presenilin 1 Modulates Acetylcholinesterase Trafficking and Maturation.International journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Interacting withActa pharmaceutica Sinica. B · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. LW-AFC Effects onAging and disease · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

8 authors.

Vicky P ChenDivision of Life Science and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong SAR, China.
Roy C Y Choi
Wallace K B Chan
K Wing Leung
Ava J Y Guo
Gallant K L Chan
Wilson K W Luk
Karl W K Tsim

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylcholinesterase (AChE) anchors onto cell membranes by a transmembrane protein PRiMA (proline-rich membrane anchor) as a tetrameric form in vertebrate brain. The assembly of AChE tetramer with PRiMA requires the C-terminal "t-peptide" in AChE catalytic subunit (AChE(T)). Although mature AChE is well known N-glycosylated, the role of glycosylation in forming the physiologically active PRiMA-linked AChE tetramer has not been studied. Here, several lines of evidence indicate that the N-linked glycosylation of AChE(T) plays a major role for acquisition of AChE full enzymatic activity but does not affect its oligomerization. The expression of the AChE(T) mutant, in which all N-glycosylation sites were deleted, together with PRiMA in HEK293T cells produced a glycan-depleted PRiMA-linked AChE tetramer but with a much higher K(m) value as compared with the wild type. This glycan-depleted enzyme was assembled in endoplasmic reticulum but was not transported to Golgi apparatus or plasma membrane.

Indexed as

AcetylcholinesteraseAnimalsBiocatalysisChickensEnzyme StabilityGlycosylationGPI-Linked ProteinsHEK293 CellsHumansMembrane ProteinsMiceNerve Tissue ProteinsPolysaccharidesProtein BindingProtein MultimerizationProtein Structure, QuaternaryAcetylcholinesteraseACHE protein, humanGPI-Linked ProteinsMembrane ProteinsNerve Tissue ProteinsPolysaccharidesprima1 protein, mouseRecombinant Proteins

Identifiers

PMID21795704
PMCPMC3190869

What OpenQuestion holds

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Registered trials

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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.