Evidence map›Paper›PMID 26558415›Full record

ReviewExpert opinion on drug metabolism & toxicology2015

Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology.

Brian C Jackson, David C Thompson, Georgia Charkoftaki, Vasilis Vasiliou

Abstract readReview
In one paragraph

Review in Expert opinion on drug metabolism & toxicology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. [ALDH3B1 expression is correlated with histopathology and long-term prognosis of gastric cancer].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Arabidopsis β-Amylase2 Is a KPlant physiology · 2017
    Article
  8. Article
  9. 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

4 authors at 2 institutions in 1 country.

Brian C Jacksona Department of Pharmaceutical Sciences , University of Colorado Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado , Aurora , CO 80045 , USA.
David C Thompsonb Department of Clinical Pharmacy , University of Colorado Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado , Aurora , CO 80045 , USA.
Georgia Charkoftakic Department of Environmental Health Sciences , Yale School of Public Health , 60 College St, New Haven , CT 06250 , USA.
Vasilis Vasiliouc Department of Environmental Health Sciences , Yale School of Public Health , 60 College St, New Haven , CT 06250 , USA.
University of Colorado Anschutz Medical Campus · USYale University · US

Funding

Mouse Models for Alcohol Metabolism and Tissue InjuryR24AA022057 · NIAAA · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2013 to 2022
$4.5M
Novel Role of Corneal Crystallins as Modulators of Cell Growth and TransparencyR01EY017963 · NEI · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2007 to 2019
$3.7M
The role of ALDH1B1 in ethanol metabolism and colon cancerU01AA021724 · NIAAA · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2014 to 2017
$1.7M
The role of ALDH1B1 in ethanol metabolism and colon cancerR01AA021724 · NIAAA · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2018 to 2018
$397k
Biochemical, Structural and Polymorphic Characterization of Human ALDH1B1F31AA020728 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI JACKSON, BRIAN CHRISTOPHER · 2011 to 2014
$104k
NEI NIH HHS R01 EY017963NIAAA NIH HHS F31 AA020728NIAAA NIH HHS R01 AA021724NIAAA NIH HHS R24 AA022057NIAAA NIH HHS U01 AA021724
6 · The paper itself

Abstract

introductionDead enzymes are gene products (proteins) that lack key residues required for catalytic activity. In the pre-genome era, dead enzymes were thought to occur only rarely. However, they now have been shown to represent upwards of 10% of the total enzyme population in many families. The aldehyde dehydrogenase (ALDH) gene family encodes proteins that, depending on the isozyme, may be either catalytically-active or -inactive. Importantly, several ALDHs exhibit biological activities independent of their catalytic activity. For many of these, the physiological and pathophysiological functions remain to be established. AREAS COVERED: This article reviews the non-enzymatic functions of the ALDH superfamily. In addition, a search for additional non-catalytic ALDH records is undertaken. Our computational analyses reveal that there are currently 182 protein records (divided into 19 groups) that meet the criteria for dead enzymes. EXPERT OPINION: Dead enzymes have the potential to exert biological actions through protein-protein interaction and allosteric modulation of the activity of an active enzyme. In addition, a dead enzyme may also influence availability of substrate for other active enzymes by sequestering substrate, and/or anchoring the substrate to a particular subcellular space. A large number of putatively non-catalytic ALDH proteins exist that warrant further study.

Indexed as

Aldehyde DehydrogenaseAllosteric RegulationAnimalsCatalysisDrug-Related Side Effects and Adverse ReactionsHumansIsoenzymesPharmaceutical PreparationsAldehyde DehydrogenaseIsoenzymesPharmaceutical Preparationsaldehyde dehydrogenasecomputational analysisdead enzymes

Identifiers

PMID26558415
PMCPMC4937717
OpenAlexW2188571889

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.