Evidence map›Paper›PMID 35419301›Full record

ReviewJournal of cancer prevention2022

Non-canonical vs. Canonical Functions of Heme Oxygenase-1 in Cancer.

Achanta Sri Venakata Jagadeesh, Xizhu Fang, Seong Hoon Kim, Yanymee N Guillen-Quispe, Jie Zheng, Young-Joon Surh, Su-Jung Kim

Open access · diamondAbstract readReview
In one paragraph

Review in Journal of cancer prevention, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Heme oxygenase-1 in thyroid cancer: a context-dependent regulator.Journal of endocrinological investigation · 2026
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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

7 authors at 1 institution in 1 country.

Achanta Sri Venakata JagadeeshCancer Research Institute, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-6073-7202
Xizhu FangResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0001-6926-6614
Seong Hoon KimResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-6573-9071
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
Jie ZhengResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-6446-2250
Young-Joon SurhCancer Research Institute, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0001-8310-1795
Su-Jung KimDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, Korea.ORCID https://orcid.org/0000-0002-3636-0644
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heme oxygenase-1 (HO-1) is a critical stress-responsive enzyme that has antioxidant and anti-inflammatory functions. HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron. The upregulation of HO-1 under pathological conditions associated with cellular stress represents an important cytoprotective defense mechanism by virtue of the anti-oxidant properties of the bilirubin and the anti-inflammatory effect of the CO produced. The same mechanism is hijacked by premalignant and cancerous cells. In recent years, however, there has been accumulating evidence supporting that the upregulation of HO-1 promotes cancer progression, independently of its catalytic activity. Such non-canonical functions of HO-1 are associated with its interaction with other proteins, particularly transcription factors. HO-1 also undergoes post-translational modifications that influence its stability, functional activity, cellular translocation, etc. HO-1 is normally present in the endoplasmic reticulum, but distinct subcellular localizations, especially in the nucleus, are observed in multiple cancers. The nuclear HO-1 modulates the activation of various transcription factors, which does not appear to be mediated by carbon monoxide and iron. This commentary summarizes the non-canonical functions of HO-1 in the context of cancer growth and progression and underlying regulatory mechanisms.

Indexed as

CancerHeme oxygenase-1Post-translational modificationProtein-protein interaction

Identifiers

PMID35419301
PMCPMC8984652
OpenAlexW4224049875

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.