Evidence map›Paper›PMID 29709390›Full record

ReviewTrends in biochemical sciences2018

Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases.

Caitlyn Q Herr, Robert P Hausinger

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
7.5field-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

113 citing papers in PubMed, 227 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. A Substrate-Dependent Bifunctional Dioxygenase fromMolecules (Basel, Switzerland) · 2026
    Article
  10. Article
  11. Total Synthesis of (+)-12-The Journal of organic chemistry · 2026
    Article
  12. Review
  13. Review
  14. Article
  15. Genetic Dereplication of MultipleJournal of natural products · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Ether lipids influence cancer cell fate by modulating iron uptake.bioRxiv : the preprint server for biology · 2025
    Article

53 more citing papers are in PubMed but not listed here.

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.

Caitlyn Q HerrDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Robert P HausingerDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA; Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA. Electronic address: hausinge@msu.edu.
Michigan State University · US

Funding

Study of alpha-ketoglutarate-dependent dioxygenasesR01GM063584 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HAUSINGER, ROBERT P · 2002 to 2014
$3.8M
NIGMS NIH HHS R01 GM063584
6 · The paper itself

Abstract

Since their discovery in the 1960s, the family of Fe(II)/2-oxoglutarate-dependent oxygenases has undergone a tremendous expansion to include enzymes catalyzing a vast diversity of biologically important reactions. Recent examples highlight roles in controlling chromatin modification, transcription, mRNA demethylation, and mRNA splicing. Others generate modifications in tRNA, translation factors, ribosomes, and other proteins. Thus, oxygenases affect all components of molecular biology's central dogma, in which information flows from DNA to RNA to proteins. These enzymes also function in biosynthesis and catabolism of cellular metabolites, including antibiotics and signaling molecules. Due to their critical importance, ongoing efforts have targeted family members for the development of specific therapeutics. This review provides a general overview of recently characterized oxygenase reactions and their key biological roles.

Indexed as

Models, MolecularAnimalsBinding SitesDNA-Binding ProteinsHalogenationHumansHydroxylationIronIsoenzymesKetoglutaric AcidsMixed Function OxygenasesProtein BiosynthesisProtein Processing, Post-TranslationalRibosomesRNA, MessengerRNA Processing, Post-TranscriptionalDNA-Binding ProteinsIronIsoenzymesKetoglutaric AcidsMixed Function OxygenasesRNA, MessengerRNA, Transferbiodegradationbiosynthesischromatin modificationNonheme iron oxygenasetranscriptiontranslation

Identifiers

PMID29709390
PMCPMC6014900
OpenAlexW2799591361

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.