Evidence map›Paper›PMID 35648190›Full record

ReviewArchives of toxicology2022

Roles of selected non-P450 human oxidoreductase enzymes in protective and toxic effects of chemicals: review and compilation of reactions.

Slobodan P Rendić, Rachel D Crouch, F Peter Guengerich

Open access · bronzeAbstract readReview
In one paragraph

Review in Archives of toxicology, 2022. 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
5.3field-weighted citation impact, top 4% 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, 31 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

3 authors at 3 institutions in 2 countries.

Slobodan P Rendić, Haulikova 6, 10 000, Zagreb, Croatia. slobodanrendic@yahoo.com.ORCID 0000-0002-0970-1407
Rachel D CrouchCollege of Pharmacy and Health Sciences, Lipscomb University, Nashville, TN, 37204, USA.ORCID 0000-0002-4525-6072
F Peter GuengerichDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232-0146, USA.ORCID 0000-0002-7458-3048
Lipscomb University · USUniversity of Zagreb · HRVanderbilt University · US

Funding

Metabolism of Carcinogens and Drugs by Human P450sR01GM118122 · NIGMS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 2016 to 2023
$3.3M
NIGMS NIH HHS R01 GM118122
6 · The paper itself

Abstract

This is an overview of the metabolic reactions of drugs, natural products, physiological compounds, and other (general) chemicals catalyzed by flavin monooxygenase (FMO), monoamine oxidase (MAO), NAD(P)H quinone oxidoreductase (NQO), and molybdenum hydroxylase enzymes (aldehyde oxidase (AOX) and xanthine oxidoreductase (XOR)), including roles as substrates, inducers, and inhibitors of the enzymes. The metabolism and bioactivation of selected examples of each group (i.e., drugs, "general chemicals," natural products, and physiological compounds) are discussed. We identified a higher fraction of bioactivation reactions for FMO enzymes compared to other enzymes, predominately involving drugs and general chemicals. With MAO enzymes, physiological compounds predominate as substrates, and some products lead to unwanted side effects or illness. AOX and XOR enzymes are molybdenum hydroxylases that catalyze the oxidation of various heteroaromatic rings and aldehydes and the reduction of a number of different functional groups. While neither of these two enzymes contributes substantially to the metabolism of currently marketed drugs, AOX has become a frequently encountered route of metabolism among drug discovery programs in the past 10-15 years. XOR has even less of a role in the metabolism of clinical drugs and preclinical drug candidates than AOX, likely due to narrower substrate specificity.

Indexed as

Biological ProductsOxidoreductasesAldehyde OxidaseHumansMolybdenumMonoamine OxidaseAldehyde OxidaseBiological ProductsMolybdenumMonoamine OxidaseOxidoreductasesBioactivationFlavin-containing monooxygenaseMolybdenum hydroxylasesMonoamine oxidaseNAD(P)H quinone oxidoreductaseNatural productsXenobiotics

Identifiers

PMID35648190
PMCPMC9159052
OpenAlexW4281636345

What Socratic holds

Textmetadata
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 Socratic graph.