Evidence map›Paper›PMID 22017871›Full record

ArticleMolecular cell2011

Regulation of the Sre1 hypoxic transcription factor by oxygen-dependent control of DNA binding.

Chih-Yung S Lee, Tzu-Lan Yeh, Bridget T Hughes, Peter J Espenshade

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. COmBio · 2019
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Regulation of lipid metabolism: a tale of two yeasts.Current opinion in cell biology · 2012
    Review
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Chih-Yung S LeeDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Tzu-Lan Yeh
Bridget T Hughes
Peter J Espenshade
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

JHU-UMD Diabetes Research CenterP30DK079637 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI AHIMA, REXFORD S. · 2013 to 2017
$9.7M
Regulation of Cellular Cholesterol HomeostasisR01HL077588 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ESPENSHADE, PETER J. · 2004 to 2022
$7.8M
NHLBI NIH HHS HL-077588NHLBI NIH HHS R01 HL077588NIDDK NIH HHS P30 DK079637
6 · The paper itself

Abstract

Regulation of gene expression plays an integral role in adaptation of cells to hypoxic stress. In mammals, prolyl hydroxylases control levels of the central transcription factor hypoxia inducible factor (HIF) through regulation of HIFα subunit stability. Here, we report that the hydroxylase Ofd1 regulates the Sre1 hypoxic transcription factor in fission yeast by controlling DNA binding. Prolyl hydroxylases require oxygen as a substrate, and the activity of Ofd1 regulates Sre1-dependent transcription. In the presence of oxygen, Ofd1 binds the Sre1 N-terminal transcription factor domain (Sre1N) and inhibits Sre1-dependent transcription by blocking DNA binding. In the absence of oxygen, the inhibitor Nro1 binds Ofd1, thereby releasing Sre1N and leading to activation of genes required for hypoxic growth. In contrast to the HIF system, where proline hydroxylation is essential for regulation, Ofd1 inhibition of Sre1N does not require hydroxylation and, thus, defines a new mechanism for hypoxic gene regulation.

Indexed as

Binding SitesCell HypoxiaDNA, FungalHydroxylationOxygenProcollagen-Proline DioxygenaseSchizosaccharomycesSchizosaccharomyces pombe ProteinsDNA, FungalOxygenProcollagen-Proline DioxygenaseSchizosaccharomyces pombe ProteinsSre1 protein, S pombe

Identifiers

PMID22017871
PMCPMC3208185
OpenAlexW2046953929

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.