Evidence map›Paper›PMID 20004171›Full record

ReviewArchives of biochemistry and biophysics2010

Butyrylcholinesterase for protection from organophosphorus poisons: catalytic complexities and hysteretic behavior.

Patrick Masson, Oksana Lockridge

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
21.1field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 222 citations in OpenAlex.

  1. Article
  2. Xenobiotic Hazards in Aircraft Cabin Air.Journal of xenobiotics · 2026
    Article
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  13. Emerging significance of butyrylcholinesterase.World journal of experimental medicine · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

16 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Patrick MassonEppley Institute, University of Nebraska Medical Center, Omaha, NE 68198-5950, USA. pmasson@unmc.edu
Oksana Lockridge
Nebraska Medical Center · USUniversity of Nebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Mass Spectrometry in Clinical Diagnosis of Nerve Agent ExposureU01NS058056 · NINDS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LOCKRIDGE, OKSANA · 2006 to 2008
$1.4M
NCI NIH HHS CA036727NCI NIH HHS P30 CA036727NINDS NIH HHS U01 NS058056
6 · The paper itself

Abstract

Butyrylcholinesterase is a promiscuous enzyme that displays complex kinetic behavior. It is toxicologically important because it detoxifies organophosphorus poisons (OP) by making a covalent bond with the OP. The OP and the butyrylcholinesterase are both inactivated in the process. Inactivation of butyrylcholinesterase has no adverse effects. However, inactivation of acetylcholinesterase in nerve synapses can be lethal. OP-inhibited butyrylcholinesterase and acetylcholinesterase can be reactivated with oximes provided the OP has not aged. Strategies for preventing the toxicity of OP include (a) treatment with an OP scavenger, (b) reaction of non-aged enzyme with oximes, (c) reactivation of aged enzyme, (d) slowing down aging with peripheral site ligands, and (e) design of mutants that rapidly hydrolyze OP. Option (a) has progressed through phase I clinical trials with human butyrylcholinesterase. Option (b) is in routine clinical use. The others are at the basic research level. Butyrylcholinesterase displays complex kinetic behavior including activation by positively charged esters, ability to hydrolyze amides, and a lag time (hysteresis) preceding hydrolysis of benzoylcholine and N-methylindoxyl acetate. Mass spectrometry has identified new OP binding motifs on tyrosine and lysine in proteins that have no active site serine. It is proposed, but not yet proven, that low dose exposure involves OP modification of proteins that have no active site serine.

Indexed as

BiocatalysisAmino Acid SequenceAnimalsButyrylcholinesteraseCholinesterase InhibitorsHumansMolecular Sequence DataOrganophosphate PoisoningOrganophosphorus CompoundsProtein MultimerizationProtein Structure, QuaternaryButyrylcholinesteraseCholinesterase InhibitorsOrganophosphorus Compounds

Identifiers

PMID20004171
PMCPMC2819560
OpenAlexW2035067870

What OpenQuestion holds

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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.