Evidence map›Paper›PMID 22465476›Full record

ReviewNitric oxide : biology and chemistry2012

Myoglobin and mitochondria: a relationship bound by oxygen and nitric oxide.

Christelle Kamga, Suhas Krishnamurthy, Sruti Shiva

Abstract readReview
In one paragraph

Review in Nitric oxide : biology and chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 86 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Christelle KamgaVascular Medicine Institute, University of Pittsburgh, Pittsburgh, PA 15261, United States.
Suhas Krishnamurthy
Sruti Shiva
University of Pittsburgh · US

Funding

Myoglobin as a Nitrite Reductase that Regulates Hypoxic Cardiac NO SignalingR01HL096973 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GLADWIN, MARK T, SHIVA, SRUTI · 2010 to 2013
$1.5M
NHLBI NIH HHS R01 HL096973
6 · The paper itself

Abstract

Since their initial discovery over a century ago, our knowledge of the functions of myoglobin and the mitochondrion has gradually evolved. The mitochondrion, once thought to be solely responsible for energy production, is now known to be an integral redox and apoptotic signal transducer within the cell. Likewise, myoglobin, traditionally thought of only as an oxygen store, has emerged as a physiological catalyst that can modulate reactive oxygen species levels, facilitate oxygen diffusion and scavenge or generate nitric oxide (NO) depending on oxygen tensions within the cell. By virtue of its unique ability to regulate O(2) and NO levels within the cell, myoglobin can modulate mitochondrial function in energy-demanding tissues such as the beating heart and exercising muscle. In this review, we present the conventional functions of myoglobin and mitochondria, and describe how these roles have been reassessed and advanced, particularly in the context of NO and nitrite signaling. We present the mechanisms by which mitochondria and myoglobin regulate one another within the cell through their interactions with NO and oxygen and discuss the implications of these interactions in terms of health and disease.

Indexed as

AnimalsFacilitated DiffusionHumansMitochondriaMyoglobinNitric OxideNitrite ReductasesOxidative PhosphorylationOxygenOxygenasesMyoglobinNitric Oxidenitric oxide dioxygenaseNitrite ReductasesOxygenOxygenases

Identifiers

PMID22465476
PMCPMC3391710
OpenAlexW1970186817

What OpenQuestion holds

Textmetadata
LicenceTDM
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.