Evidence map›Paper›PMID 26152730›Full record

ReviewThe Journal of biological chemistry2015

Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.

Suzana Markolovic, Sarah E Wilkins, Christopher J Schofield

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

102 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
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  12. Regulation of mFunctional & integrative genomics · 2024
    Review
  13. The Effects ofMicroorganisms · 2024
    Article
  14. Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7.Protein science : a publication of the Protein Society · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

42 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

3 authors at 3 institutions in 2 countries.

Suzana MarkolovicChemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom.
Sarah E WilkinsChemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom. Electronic address: sarah.wilkins@chem.ox.ac.uk.
Christopher J SchofieldChemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom. Electronic address: christopher.schofield@chem.ox.ac.uk.
Mansfield University · USOxford Research Group · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L009846/1British Heart FoundationCancer Research UK 18245Wellcome Trust
6 · The paper itself

Abstract

The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen biosynthesis. 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible factors that play important roles in the adaptive response to hypoxia. Subsequently, they have been shown to catalyze N-demethylation (via hydroxylation) of N(ϵ)-methylated histone lysyl residues, as well as hydroxylation of multiple other residues. Recent work has identified roles for 2OG oxygenases in the modification of translation-associated proteins, which in some cases appears to be conserved from microorganisms through to humans. Here we give an overview of protein hydroxylation catalyzed by 2OG oxygenases, focusing on recent discoveries.

Indexed as

Protein Processing, Post-TranslationalBacteriaBiocatalysisCollagenDioxygenasesGene ExpressionHistone DemethylasesHistonesHumansHydroxylationHypoxia-Inducible Factor-Proline DioxygenasesIronKetoglutaric AcidsMixed Function OxygenasesModels, MolecularCollagenDioxygenasesHistone DemethylasesHistonesHypoxia-Inducible Factor-Proline DioxygenasesIronKetoglutaric AcidsMixed Function Oxygenases2-oxoglutaratechemical biologydioxygenaseenzyme catalysisgene expressionhydroxylasehydroxylationpost-translational modification (PTM)protein chemical modificationprotein synthesis

Identifiers

PMID26152730
PMCPMC4543633
OpenAlexW2140300092

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.