Evidence map›Paper›PMID 20493179›Full record

ArticleChemico-biological interactions2010

From Split to Sibenik: the tortuous pathway in the cholinesterase field.

Palmer Taylor

Abstract readAddress
In one paragraph

Article in Chemico-biological interactions, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 34% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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 at 1 institution in 1 country.

Palmer TaylorDepartment of Pharmacology 0636, Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0650, USA. pwtaylor@ucsd.edu
University of Montana · US

Funding

Yeast Genetics and Stress Response Genes-BiomedicalP42ES010337 · NIEHS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TUKEY, ROBERT H · 2000 to 2022
$69.8M
KINETICS OF DRUG MACROMOLECULE COMPLEX FORMATIONR37GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1999 to 2008
$5.7M
KINETICS OF DRUG-MACROMOLECULE COMPLEX FORMATIONR01GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1985 to 2013
$2.8M
NIEHS NIH HHS P42 ES010337NIEHS NIH HHS P42ES10337NIGMS NIH HHS R01 GM018360NIGMS NIH HHS R37GM 18360
6 · The paper itself

Abstract

The interim between the first and tenth International Cholinesterase Meetings has seen remarkable advances associated with the applications of structural biology and recombinant DNA methodology to our field. The cloning of the cholinesterase genes led to the identification of a new super family of proteins, termed the alpha,beta-hydrolase fold; members of this family possess a four helix bundle capable of linking structural subunits to the functioning globular protein. Sequence comparisons and three-dimensional structural studies revealed unexpected cousins possessing this fold that, in turn, revealed three distinct functions for the alpha,beta-hydrolase proteins. These encompass: (1) a capacity for hydrolytic cleavage of a great variety of substrates, (2) a heterophilic adhesion function that results in trans-synaptic associations in linked neurons, (3) a chaperone function leading to stabilization of nascent protein and its trafficking to an extracellular or secretory storage location. The analysis and modification of structure may go beyond understanding mechanism, since it may be possible to convert the cholinesterases to efficient detoxifying agents of organophosphatases assisted by added oximes. Also, the study of the relationship between the alpha,beta-hydrolase fold proteins and their biosynthesis may yield means by which aberrant trafficking may be corrected, enhancing expression of mutant proteins. Those engaged in cholinesterase research should take great pride in our accomplishments punctuated by the series of ten meetings. The momentum established and initial studies with related proteins all hold great promise for the future.

Indexed as

CholinesterasesAcetylcholinesteraseAnimalsAntidotesCholinesterase InhibitorsGene Expression Regulation, EnzymologicHumansAcetylcholinesteraseAntidotesCholinesterase InhibitorsCholinesterases

Identifiers

PMID20493179
PMCPMC3000743
OpenAlexW2051135921

What OpenQuestion holds

Textmetadata
LicenceTDM
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.