Evidence map›Paper›PMID 32985654›Full record

ReviewBiochemical Society transactions2020

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators.

Sally C Fletcher, Mathew L Coleman

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
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  6. Article
  7. Review
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  9. Article
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  11. [Latest Findings on the Role of α-Ketoglutarate in Metabolic Syndrome].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Review
  12. Iron, Copper, and Selenium: Cancer's Thing for Redox Bling.Cold Spring Harbor perspectives in medicine · 2024
    Review
  13. Review
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  16. Article
  17. Review
  18. 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

2 authors at 1 institution in 1 country.

Sally C FletcherInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham B15 2TT, U.K.
Mathew L ColemanInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham B15 2TT, U.K.
University of Birmingham · GB

Funding

Cancer Research UK 24552Medical Research Council MR/N021053/1
6 · The paper itself

Abstract

Fe(II)/2-oxoglutarate (2OG)-dependent oxygenases are a conserved enzyme class that catalyse diverse oxidative reactions across nature. In humans, these enzymes hydroxylate a broad range of biological substrates including DNA, RNA, proteins and some metabolic intermediates. Correspondingly, members of the 2OG-dependent oxygenase superfamily have been linked to fundamental biological processes, and found dysregulated in numerous human diseases. Such findings have stimulated efforts to understand both the biochemical activities and cellular functions of these enzymes, as many have been poorly studied. In this review, we focus on human 2OG-dependent oxygenases catalysing the hydroxylation of protein and polynucleotide substrates. We discuss their modulation by changes in the cellular microenvironment, particularly with respect to oxygen, iron, 2OG and the effects of oncometabolites. We also describe emerging evidence that these enzymes are responsive to cellular stresses including hypoxia and DNA damage. Moreover, we examine how dysregulation of 2OG-dependent oxygenases is associated with human disease, and the apparent paradoxical role for some of these enzymes during cancer development. Finally, we discuss some of the challenges associated with assigning biochemical activities and cellular functions to 2OG-dependent oxygenases.

Indexed as

DNA DamageAscorbic AcidBiological PhenomenaCatalysisDNAGene Expression RegulationHumansHydroxylationHypoxiaKetoglutaric AcidsMixed Function OxygenasesModels, MolecularNeoplasmsOxidation-ReductionOxygenOxygenasesAscorbic AcidDNAKetoglutaric AcidsMixed Function OxygenasesOxygenOxygenasesRNAdiseasehydroxylationhypoxianutrient sensingoxygenasepost translational modification

Identifiers

PMID32985654
PMCPMC7609023
OpenAlexW3088395922

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.