Evidence map›Paper›PMID 23085121›Full record

ArticleChemico-biological interactions2013

Cholinesterase confabs and cousins: approaching forty years.

Palmer Taylor, Antonella De Jaco, Davide Comoletti, Meghan Miller, Shelley Camp

Abstract readHistorical Article
In one paragraph

Article in Chemico-biological interactions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
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

5 authors.

Palmer TaylorSkaggs School of Pharmacy & Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Drive, Mail Code 0657, La Jolla, CA 92093, United States. pwtaylor@ucsd.edu
Antonella De Jaco
Davide Comoletti
Meghan Miller
Shelley Camp

Funding

Oxime-Assisted Catalysis of Organophosphates and Reactivation of AChEU01NS058046 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 2006 to 2011
$4.0M
KINETICS OF DRUG-MACROMOLECULE COMPLEX FORMATIONR01GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1985 to 2013
$2.8M
NIGMS NIH HHS R01 GM018360NINDS NIH HHS U01 NS058046
6 · The paper itself

Abstract

In the past four decades of cholinesterase (ChE) research, we have seen substantive evolution of the field from one centered around substrate and inhibitor kinetic profiles and compound characterizations to the analysis of ChE structure, first through the gene families and then by X-ray crystallographic determinations of the free enzymes and their complexes and conjugates. Indeed, these endeavors have been facilitated by recombinant DNA technologies, structure determinations and parallel studies in related proteins in the α/β-hydrolase fold family. This approach has not only contributed to a fundamental understanding of structure and function of a large family of hydrolase-like proteins possessing functions other than catalysis, but also has been used to develop new practical strategies for scavenging and antidotal activity in cases of organophosphate insecticide or nerve agent exposure.

Indexed as

AnimalsCholinesterasesHistory, 20th CenturyHistory, 21st CenturyHumansModels, MolecularNerve Tissue ProteinsProtein FoldingProtein Structure, TertiaryCholinesterasesNerve Tissue Proteins

Identifiers

PMID23085121
PMCPMC3618580

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.