Evidence map›Paper›PMID 39790223›Full record

ArticleJournal of cancer prevention2024

Non-canonical Function of Prolyl Hydroxylase Domain 2 in Breast Cancer Cell Growth and Progression: Role of Peptidyl-prolyl Cis-trans Isomerase NIMA-interacting 1.

Yanymee N Guillen-Quispe, Su-Jung Kim, Soma Saeidi, Gyo-Jin Choi, Chaithanya Chelakkot, Tianchi Zhou, Sang-Beom Bang, Tae-Won Kim, Young Kee Shin, Young-Joon Surh

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cancer prevention, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Yanymee N Guillen-QuispeDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0003-2157-4727
Su-Jung KimResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-3636-0644
Soma SaeidiDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-4943-5596
Gyo-Jin ChoiDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0009-0007-0696-7270
Chaithanya ChelakkotDepartment of Pharmacy, Laboratory of Molecular Pathology and Cancer Genomics, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-4548-5510
Tianchi ZhouMRC Human Genetics Unit, Institute of Genetics and Cancer, The University of Edinburgh, Edinburgh, UK.ORCID https://orcid.org/0009-0003-9453-1813
Sang-Beom BangDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-4852-8643
Tae-Won KimDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0009-0007-9157-0699
Young Kee Shin *Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0003-0896-718X
Young-Joon Surh *Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0001-8310-1795

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prolyl hydroxylase domain 2 (PHD2) is the primary oxygen sensing enzyme involved in hydroxylation of hypoxia-inducible factor (HIF). Under normoxic conditions, PHD2 hydroxylates specific proline residues in HIF-1α and HIF-2α, promoting their ubiquitination and subsequent proteasomal degradation. Although PHD2 activity decreases in hypoxia, notable residual activity persists, but its function in these conditions remains unclear

Indexed as

Breast cancerHypoxia-inducible factorPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1Prolyl hydroxylase domain 2Protein-protein interaction

Identifiers

PMID39790223
PMCPMC11706723

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.