Evidence map›Paper›PMID 34688156›Full record

ReviewRedox biology2021

The non-canonical effects of heme oxygenase-1, a classical fighter against oxidative stress.

Jiajia Wu, Siyu Li, Cheng Li, Liying Cui, Jiajia Ma, Yang Hui

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.1field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 75 citations in OpenAlex.

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  16. Relationships Between HAntioxidants (Basel, Switzerland) · 2025
    Article
  17. Dihydromyricetin mitigates abdominal aortic aneurysmActa pharmaceutica Sinica. B · 2025
    Article
  18. Article
  19. Article
  20. Article
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

6 authors at 1 institution in 1 country.

Jiajia WuDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China.
Siyu LiDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China.
Cheng LiDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China.
Liying CuiDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China.
Jiajia MaDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China.
Yang HuiDepartment of Biochemistry and Molecular Biology, Harbin Medical University, Harbin, PR China; Basic Medical Institute of Heilongjiang Medical Science Academy, PR China; Translational Medicine Center of Northern China, PR China. Electronic address: huiyang79@126.com.
Harbin Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of heme oxygenase-1 in resisting oxidative stress and cell protection has always been a hot research topic. With the continuous deepening of research, in addition to directly regulating redox by catalyzing the degradation of heme, HO-1 protein also participates in the gene expression level in a great diversity of methods, thereby initiating cell defense. Particularly the non-canonical nuclear-localized HO-1 and HO-1 protein interactions play the role of a warrior against oxidative stress. Besides, HO-1 may be a promising marker for disease prediction and detection in many clinical trials. Especially for malignant diseases, there may be new advances in the treatment of HO-1 by regulating abnormal ROS and metabolic signaling. The purpose of this review is to systematically sort out and describe several aspects of research to facilitate further detailed mechanism research and clinical application promotion in the future.

Indexed as

Heme Oxygenase-1Heme Oxygenase (Decyclizing)AnimalsHemeHumansOxidation-ReductionOxidative StressHemeHeme Oxygenase-1Heme Oxygenase (Decyclizing)Disease diagnosis and treatmentGene expression controlHeme oxygenase-1Protein-protein interactionRedox system regulation

Identifiers

PMID34688156
PMCPMC8577501
OpenAlexW3210044565

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.