Evidence map›Paper›PMID 26892220›Full record

ReviewChemico-biological interactions2016

Carboxylesterases: General detoxifying enzymes.

M Jason Hatfield, Robyn A Umans, Janice L Hyatt, Carol C Edwards, Monika Wierdl, Lyudmila Tsurkan, Michael R Taylor, Philip M Potter

Abstract readReview
In one paragraph

Review in Chemico-biological interactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
10.1field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Hepatocyte-SpecificAntioxidants (Basel, Switzerland) · 2026
    Article
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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

8 authors at 1 institution in 1 country.

M Jason HatfieldDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Robyn A UmansDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Janice L HyattDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Carol C EdwardsDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Monika WierdlDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Lyudmila TsurkanDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Michael R TaylorDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Philip M PotterDepartment of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States. Electronic address: phil.potter@stjude.org.
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Neural Stem Cell Mediated CE-CPT11 Therapy for NeuroblastomaU01NS082328 · NINDS · BECKMAN RESEARCH INSTITUTE/CITY OF HOPE · PI ABOODY, KAREN S · 2013 to 2017
$4.7M
Improving CPT-11 Efficacy Using Structural BiologyR01CA098468 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI REDINBO, MATTHEW R · 2003 to 2018
$3.9M
Novel Protein-Based Therapeutics for Nerve Agent DetoxificationU01NS058089 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI REDINBO, MATTHEW R · 2006 to 2010
$2.5M
Selective Inhibitors to Improve CPT-11 TherapyR01CA108775 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI POTTER, PHILIP M · 2005 to 2013
$2.3M
Modulation of drug metabolism by DanshenR01AT007531 · NCCIH · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI POTTER, PHILIP M · 2013 to 2016
$1.7M
Novel Therapeutic Approaches for Narcotic OverdoseR01DA018116 · NIDA · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI POTTER, PHILIP M · 2005 to 2009
$1.4M
NCCIH NIH HHS R01 AT007531NCI NIH HHS P30 CA021765NCI NIH HHS R01 CA098468NCI NIH HHS R01 CA108775NIDA NIH HHS R01 DA018116NINDS NIH HHS U01 NS058089NINDS NIH HHS U01 NS082328
6 · The paper itself

Abstract

Carboxylesterases (CE) are members of the esterase family of enzymes, and as their name suggests, they are responsible for the hydrolysis of carboxylesters into the corresponding alcohol and carboxylic acid. To date, no endogenous CE substrates have been identified and as such, these proteins are thought to act as a mechanism to detoxify ester-containing xenobiotics. As a consequence, they are expressed in tissues that might be exposed to such agents (lung and gut epithelia, liver, kidney, etc.). CEs demonstrate very broad substrate specificities and can hydrolyze compounds as diverse as cocaine, oseltamivir (Tamiflu), permethrin and irinotecan. In addition, these enzymes are irreversibly inhibited by organophosphates such as Sarin and Tabun. In this overview, we will compare and contrast the two human enzymes that have been characterized, and evaluate the biology of the interaction of these proteins with organophosphates (principally nerve agents).

Indexed as

AnimalsCarboxylic Ester HydrolasesHumansInactivation, MetabolicModels, MolecularOrganophosphatesSubstrate SpecificityCarboxylic Ester HydrolasesOrganophosphatesCarboxylesteraseExpressionHydrolysisOrganophosphorus compoundsStructure

Identifiers

PMID26892220
PMCPMC4985501
OpenAlexW2278057954

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.