Evidence map›Paper›PMID 24180238›Full record

ReviewAntioxidants & redox signaling2014

Signaling function of heme oxygenase proteins.

Phyllis A Dennery

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

68 citing papers in PubMed, 127 citations in OpenAlex.

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8 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Phyllis A DenneryDepartment of Pediatrics, University of Pennsylvania , Philadelphia, Pennsylvania.
California University of Pennsylvania · US

Funding

Role of Heme Oxygenase in Neonatal Hyperoxic InjuryR01HL058752 · NHLBI · STANFORD UNIVERSITY · PI DENNERY, PHYLLIS A. · 1999 to 2013
$4.5M
Regulation of the Lung Circadian Clock by Heme Oxygenase-1R21HL111907 · NHLBI · CHILDREN'S HOSP OF PHILADELPHIA · PI DENNERY, PHYLLIS A. · 2013 to 2014
$520k
NHLBI NIH HHS HL-111907NHLBI NIH HHS HL-58752
6 · The paper itself

Abstract

significanceMany reports have underscored the importance of the heme degradation pathway that is regulated by heme oxygenase (HO). This reaction releases bile pigments and carbon monoxide (CO), which are important antioxidant and signaling molecules. Thus, the reaction of HO-1 would have significant cytoprotective effects. Nevertheless, the importance of this protein goes beyond its enzymatic action. New evidence outlines significant effects of inactive forms of the HO-1 protein. RECENT ADVANCES: In fact, the role of the HO protein in cellular signaling, including transcription factor activation, binding to proteins, phosphorylation, and modulation of protein function, among others, has started being elucidated. The mechanism by which the inducible form of HO-1, in particular, can migrate to various cellular compartments to mediate important signaling or how and why it binds to key transcription factors and other proteins that are important in DNA repair is also described in several physiologic systems. CRITICAL ISSUES: The signaling functions of HO-1 may have particular relevance in clinical circumstances, including cancer, as redistribution of HO-1 into the nuclear compartment is observed with cancer progression and metastasis. In addition, along with oxidative stress, the pleiotropic functions of HO-1 modulate antioxidant defense. In organ transplantation, HO and its byproducts suppress rejection at multiple levels and in sepsis-induced pulmonary dysfunction, inhaled CO or modulation of HO activity can change the course of the disease in animals. FUTURE DIRECTIONS: It is hoped that a more detailed understanding of the various signaling functions of HO will guide therapeutic approaches for complex diseases.

Indexed as

AnimalsEnzyme InductionHeme Oxygenase (Decyclizing)HumansModels, MolecularNeoplasmsOxidative StressProtein ConformationProtein TransportSignal TransductionHeme Oxygenase (Decyclizing)

Identifiers

PMID24180238
PMCPMC3961771
OpenAlexW2094527041

What OpenQuestion holds

Textmetadata
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.