Evidence map›Paper›PMID 20566626›Full record

ArticleThe Journal of biological chemistry2010

The PRiMA-linked cholinesterase tetramers are assembled from homodimers: hybrid molecules composed of acetylcholinesterase and butyrylcholinesterase dimers are up-regulated during development of chicken brain.

Vicky P Chen, Heidi Q Xie, Wallace K B Chan, K Wing Leung, Gallant K L Chan, Roy C Y Choi, Suzanne Bon, Jean Massoulié, Karl W K Tsim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  3. Butyrylcholinesterase gene transfer in obese mice prevents postdieting body weight rebound by suppressing ghrelin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  5. Review
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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

9 authors at 3 institutions in 2 countries.

Vicky P ChenDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
Heidi Q XieDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
Wallace K B ChanDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
K Wing LeungDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
Gallant K L ChanDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
Roy C Y ChoiDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China.
Suzanne BonCNRS-UMR 8197, Institut de Biologie de l'Ecole Normale Supérieure, 75005 Paris, France.
Jean MassouliéCNRS-UMR 8197, Institut de Biologie de l'Ecole Normale Supérieure, 75005 Paris, France.
Karl W K TsimDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China. Electronic address: botsim@ust.hk.
Hong Kong University of Science and Technology · HKCentre National de la Recherche Scientifique · FRChinese University of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylcholinesterase (AChE) is anchored onto cell membranes by the transmembrane protein PRiMA (proline-rich membrane anchor) as a tetrameric globular form that is prominently expressed in vertebrate brain. In parallel, the PRiMA-linked tetrameric butyrylcholinesterase (BChE) is also found in the brain. A single type of AChE-BChE hybrid tetramer was formed in cell cultures by co-transfection of cDNAs encoding AChE(T) and BChE(T) with proline-rich attachment domain-containing proteins, PRiMA I, PRiMA II, or a fragment of ColQ having a C-terminal GPI addition signal (Q(N-GPI)). Using AChE and BChE mutants, we showed that AChE-BChE hybrids linked with PRiMA or Q(N-GPI) always consist of AChE(T) and BChE(T) homodimers. The dimer formation of AChE(T) and BChE(T) depends on the catalytic domains, and the assembly of tetramers with a proline-rich attachment domain-containing protein requires the presence of C-terminal "t-peptides" in cholinesterase subunits. Our results indicate that PRiMA- or ColQ-linked cholinesterase tetramers are assembled from AChE(T) or BChE(T) homodimers. Moreover, the PRiMA-linked AChE-BChE hybrids occur naturally in chicken brain, and their expression increases during development, suggesting that they might play a role in cholinergic neurotransmission.

Indexed as

ChickensAcetylcholinesteraseAnimalsBrainButyrylcholinesteraseCells, CulturedChick EmbryoGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicMembrane ProteinsMultienzyme ComplexesMutationNerve Tissue ProteinsPeptidesProtein MultimerizationProtein Structure, QuaternaryAcetylcholinesteraseButyrylcholinesteraseMembrane ProteinsMultienzyme ComplexesNerve Tissue ProteinsPeptides

Identifiers

PMID20566626
PMCPMC2930726
OpenAlexW1996470833

What OpenQuestion holds

Textmetadata
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.