Evidence map›Paper›PMID 10585848›Full record

ReviewThe Biochemical journal1999

Neuropathy target esterase.

P Glynn

Abstract readReview
In one paragraph

Review in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Lipid-metabolizing serine hydrolases in the mammalian central nervous system: endocannabinoids and beyond.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Neuropathy target esterase catalyzes osmoprotective renal synthesis of glycerophosphocholine in response to high NaCl.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  18. Brain-specific deletion of neuropathy target esterase/swisscheese results in neurodegeneration.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  19. Insecticides.Current treatment options in neurology · 2004
    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

1 author.

P GlynnMRC Toxicology Unit, University of Leicester, Leicester LE1 9HN, U.K. pg8@le.ac.uk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuropathy target esterase (NTE) is an integral membrane protein present in all neurons and in some non-neural-cell types of vertebrates. Recent data indicate that NTE is involved in a cell-signalling pathway controlling interactions between neurons and accessory glial cells in the developing nervous system. NTE has serine esterase activity and efficiently catalyses the hydrolysis of phenyl valerate (PV) in vitro, but its physiological substrate is unknown. By sequence analysis NTE has been found to be related neither to the major serine esterase family, which includes acetylcholinesterase, nor to any other known serine hydrolases. NTE comprises at least two functional domains: an N-terminal putative regulatory domain and a C-terminal effector domain which contains the esterase activity and is, in part, conserved in proteins found in bacteria, yeast, nematodes and insects. NTE's effector domain contains three predicted transmembrane segments, and the active-site serine residue lies at the centre of one of these segments. The isolated recombinant domain shows PV hydrolase activity only when incorporated into phospholipid liposomes. NTE's esterase activity appears to be largely redundant in adult vertebrates, but organophosphates which react with NTE in vivo initiate unknown events which lead, after a delay of 1-3 weeks, to a neuropathy with degeneration of long axons. These neuropathic organophosphates leave a negatively charged group covalently attached to the active-site serine residue, and it is suggested that this may cause a toxic gain of function in NTE.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCarboxylic Ester HydrolasesCloning, MolecularHumansMembrane ProteinsMolecular Sequence DataNervous System DiseasesNeuronsSpecies SpecificityTritolyl PhosphatesValeratesCarboxylic Ester HydrolasesMembrane Proteinsneurotoxic esterasephenyl valeratetri-o-cresyl phosphateTritolyl PhosphatesValerates

Identifiers

PMID10585848
PMCPMC1220683

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.