Evidence map›Paper›PMID 15526038›Full record

ArticleThe EMBO journal2004

The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.

Hay Dvir, Michal Harel, Suzanne Bon, Wang-Qing Liu, Michel Vidal, Christiane Garbay, Joel L Sussman, Jean Massoulié, Israel Silman

Abstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
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  7. Neuroactive venom compounds obtained fromThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  8. Article
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  10. 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
  11. Article
  12. Characterization of butyrylcholinesterase from porcine milk.Archives of biochemistry and biophysics · 2018
    Article
  13. Review
  14. Review
  15. Article
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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.

Hay DvirDapartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Michal Harel
Suzanne Bon
Wang-Qing Liu
Michel Vidal
Christiane Garbay
Joel L Sussman
Jean Massoulié
Israel Silman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. The crystal structure of the WAT/PRAD complex reveals a novel supercoil structure in which four parallel WAT chains form a left-handed superhelix around an antiparallel left-handed PRAD helix resembling polyproline II. The WAT coiled coils possess a WWW motif making repetitive hydrophobic stacking and hydrogen-bond interactions with the PRAD. The WAT chains are related by an approximately 4-fold screw axis around the PRAD. Each WAT makes similar but unique interactions, consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ. The P59Q mutation in ColQ, which causes congenital endplate AChE deficiency, and is located within the PRAD, disrupts crucial WAT-WAT and WAT-PRAD interactions. A model is proposed for the synaptic AChE(T) tetramer.

Indexed as

Protein ConformationAcetylcholinesteraseAlternative SplicingAmino Acid MotifsAmino Acid SequenceAnimalsCollagenCrystallography, X-RayDisulfidesModels, ChemicalModels, MolecularMolecular Sequence DataMuscle ProteinsPeptidesPoint MutationProtein Structure, TertiaryAcetylcholinesteraseCollagenCOLQ protein, humanDisulfidesMuscle ProteinsPeptidespolyprolineTryptophan

Identifiers

PMID15526038
PMCPMC526459

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.