Evidence map›Paper›PMID 30151692›Full record

ReviewCellular and molecular life sciences : CMLS2018

The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease.

James R Bundred, Eline Hendrix, Mathew L Coleman

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Histidine methyltransferase SETD3 methylates structurally diverse histidine mimics in actin.Protein science : a publication of the Protein Society · 2022
    Article
  11. Article
  12. Enzymatic CJournal of the American Chemical Society · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

James R BundredTumour Oxygenase Group, Institute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Eline HendrixTumour Oxygenase Group, Institute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Mathew L ColemanTumour Oxygenase Group, Institute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. m.coleman@bham.ac.uk.ORCID http://orcid.org/0000-0001-6020-9023
University of Birmingham · GB

Funding

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

Abstract

Hydroxylation is a novel protein modification catalyzed by a family of oxygenases that depend on fundamental nutrients and metabolites for activity. Protein hydroxylases have been implicated in a variety of key cellular processes that play important roles in both normal homeostasis and pathogenesis. Here, in this review, we summarize the current literature on a highly conserved sub-family of oxygenases that catalyze protein histidyl hydroxylation. We discuss the evidence supporting the biochemical assignment of these emerging enzymes as ribosomal protein hydroxylases, and provide an overview of their role in immunology, bone development, and cancer.

Indexed as

AnimalsHistone DemethylasesHumansMixed Function OxygenasesMuscle, SkeletalNeoplasmsNuclear ProteinsProtein Processing, Post-TranslationalRibosomal ProteinsRibosomesHistone DemethylasesMixed Function OxygenasesNuclear ProteinsRibosomal ProteinsBone developmentCancerHistidineHydroxylationImmunologyPost-translational modification

Identifiers

PMID30151692
PMCPMC6182338
OpenAlexW2888982834

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.