Evidence map›Paper›PMID 40070406›Full record

ReviewFrontiers in chemistry2025

Major heme proteins hemoglobin and myoglobin with respect to their roles in oxidative stress - a brief review.

Rajarshi Sil, Abhay Sankar Chakraborti

Abstract readReview
In one paragraph

Review in Frontiers in chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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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

2 authors.

Rajarshi SilAllied Scientific Products, Kolkata, India.
Abhay Sankar ChakrabortiDepartment of Biophysics, Molecular Biology and Bioinformatics, University College of Science, University of Calcutta, Kolkata, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative stress is considered as the root-cause of different pathological conditions. Transition metals, because of their redox-active states, are capable of free radical generation contributing oxidative stress. Hemoglobin and myoglobin are two major heme proteins, involved in oxygen transport and oxygen storage, respectively. Heme prosthetic group of heme proteins is a good reservoir of iron, the most abundant transition metal in human body. Although iron is tightly bound in the heme pocket of these proteins, it is liberated under specific circumstances yielding free ferrous iron. This active iron can react with H

Indexed as

fenton reactionfree ironhemoglobinmyoglobinoxidative stress

Identifiers

PMID40070406
PMCPMC11893434

What OpenQuestion holds

Textmetadata
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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.