Evidence map›Paper›PMID 12675141›Full record

ArticleNeurochemical research2003

Trimerization domain of the collagen tail of acetylcholinesterase.

Suzanne Bon, Annick Ayon, Jacqueline Leroy, Jean Massoulié

Abstract read
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In one paragraph

Article in Neurochemical research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Cholinesterases in Tripartite Neuromuscular Synapse.Frontiers in molecular neuroscience · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Acetylcholinesterase: from 3D structure to function.Chemico-biological interactions · 2010
    Article
  10. Article
  11. Article
  12. Article
  13. 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

4 authors.

Suzanne BonLaboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS UMR 8544, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France.
Annick Ayon
Jacqueline Leroy
Jean Massoulié

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the collagen-tailed forms of cholinesterases, each subunit of a specific triple helical collagen, ColQ, may be attached through a proline-rich domain (PRAD) situated in its N-terminal noncollagenous region, to tetramers of acetylcholinesterase (AChE) or butyrylcholinesterase (BChE). This heteromeric assembly ensures the functional anchoring of AChE in extracellulare matrices, for example, at the neuromuscular junction. In this study, we analyzed the influence of deletions in the noncollagenous C-terminal region of ColQ on its capacity to form a triple helix. We show that an 80-residue segment located downstream of the collagenous regions contains the trimerization domain, that it can form trimers without the collagenous regions, and that a pair of cysteines located at the N-boundary of this domain facilitates oligomerization, although it is not absolutely required. We further show that AChE subunits can associate with nonhelical collagen ColQ monomers, forming ColQ-associated tetramers (G4-Q), which are secreted or are anchored at the cell surface when the C-terminal domain of ColQ is replaced by a GPI-addition signal.

Indexed as

Muscle ProteinsAcetylcholinesteraseAmino Acid SequenceAnimalsCollagenCOS CellsMolecular Sequence DataMutationProtein Structure, TertiaryTorpedoTransfectionAcetylcholinesteraseCollagenCOLQ protein, humanMuscle Proteins

Identifiers

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.