Evidence map›Paper›PMID 26229025›Full record

ArticleAnalytical and bioanalytical chemistry2015

Heavy chain single-domain antibodies to detect native human soluble epoxide hydrolase.

Yongliang Cui, Dongyang Li, Christophe Morisseau, Jie-Xian Dong, Jun Yang, Debin Wan, Martín A Rossotti, Shirley J Gee, Gualberto G González-Sapienza, Bruce D Hammock

Open access · greenAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 33% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

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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

10 authors at 2 institutions in 3 countries.

Yongliang CuiDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Dongyang LiDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Christophe MorisseauDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Jie-Xian DongDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Jun YangDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Debin WanDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Martín A RossottiCátedra de Inmunología, Facultad de Química, Instituto de Higiene, UDELAR Av. A. Navarro 3051, Piso 2, Montevideo, 11600, Uruguay.
Shirley J GeeDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA.
Gualberto G González-SapienzaCátedra de Inmunología, Facultad de Química, Instituto de Higiene, UDELAR Av. A. Navarro 3051, Piso 2, Montevideo, 11600, Uruguay.
Bruce D HammockDepartment of Entomology and Nematology, University of California, Davis, Davis, CA, 95616, USA. bdhammock@ucdavis.edu.
University of California, Davis · USCentro Uruguayo de Imagenología Molecular · UY

Funding

Workshop on Environmental Technology Transfer and EntrepreneurshipP42ES004699 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI MIDDLETON, ELISABETH ROSE · 1987 to 2021
$50.1M
HYDROLYTIC ENZYMES IN THE METABOLISM OF TOXINSR01ES002710 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1985 to 2018
$4.0M
International Training Program in Environmental Toxicology and Public HealthD43TW005718 · FIC · UNIVERSITY OF CALIFORNIA DAVIS · PI LAST, JEROLD ALAN · 2001 to 2011
$1.7M
FIC NIH HHS D43 TW005718NIEHS NIH HHS P42 ES004699NIEHS NIH HHS P42 ES04699NIEHS NIH HHS R01 ES002710NIEHS NIH HHS R01 ES02710
6 · The paper itself

Abstract

The soluble epoxide hydrolase (sEH) is a potential pharmacological target for treating hypertension, vascular inflammation, pain, cancer, and other diseases. However, there is not a simple, inexpensive, and reliable method to estimate levels of active sEH in tissues. Toward developing such an assay, a polyclonal variable domain of heavy chain antibody (VHH) sandwich immunoassay was developed. Ten VHHs, which are highly selective for native human sEH, were isolated from a phage-displayed library. The ten VHHs have no significant cross-reactivity with human microsomal epoxide hydrolase, rat and mouse sEH, and denatured human sEH. There is a high correlation between protein levels of the sEH determined by the enzyme-linked immunosorbent assay (ELISA) and the catalytic activity of the enzyme in S9 fractions of human tissues (liver, kidney, and lung). The VHH-based ELISA appears to be a new reliable method for monitoring the sEH and may be useful as a diagnostic tool for diseases influenced by sEH. This study also demonstrates the broad utility of VHH in biochemical and pharmacological research.

Indexed as

Amino Acid SequenceAnimalsCamelids, New WorldCross ReactionsEnzyme-Linked Immunosorbent AssayEpoxide HydrolasesHumansMolecular Sequence DataSequence Homology, Amino AcidSingle-Domain AntibodiesEpoxide HydrolasesSingle-Domain AntibodiesELISAMagnetic beadssEHSoluble epoxide hydrolaseVHH

Identifiers

PMID26229025
PMCPMC4573264
OpenAlexW1043652376

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.