The DOI matches its Crossref record; 144 of the 145 references it cites were found in a registry or an index.
Carbon monoxide, reactive oxygen signaling, and oxidative stress
Open accessAbstract
The ubiquitous gas, carbon monoxide (CO), is of substantial biological importance, but apart from its affinity for reduced transition metals, particularly heme-iron, it is surprisingly nonreactive-as is the ferrous-carbonyl-in living systems. CO does form strong complexes with heme proteins for which molecular O2 is the preferred ligand and to which are attributed diverse physiological, adaptive, and toxic effects. Lately, it has become apparent that both exogenous and endogenous CO produced by heme oxygenase engender a prooxidant milieu in aerobic mammalian cells which initiates signaling related to reactive oxygen species (ROS) generation. ROS signaling contingent on CO can be segregated by CO concentration-time effects on cellular function, by the location of heme proteins, e.g., mitochondrial or nonmitochondrial sites, or by specific oxidation-reduction (redox) reactions. The fundamental responses to CO involve overt physiological regulatory events, such as activation of redox-sensitive transcription factors or stress-activated kinases, which institute compensatory expression of antioxidant enzymes and other adaptations to oxidative stress. In contrast, responses originating from highly elevated or protracted CO exposures tend to be nonspecific, produce untoward biological oxidations, and interfere with homeostasis. This brief overview provides a conceptual framework for understanding CO biology in terms of this physiological-pathological hierarchy.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The functions of NO in mammalian systems extend beyond vascular signaling and are relevant in all organ systems, including but not limited to neuronal signaling, and host defense”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [738]
Citations
Cites
3 retracted
Suliman, H. B., Carraway, M. S., Ali, A. S., Reynolds, C. M., Welty‐Wolf, K. E., & Piantadosi, C. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32967 · Cited by 261
Self-citationRetractedRETRACTED: A new activating role for CO in cardiac mitochondrial biogenesis
Suliman, H. B., Carraway, M. S., Tatro, L. G., & Piantadosi, C. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03318 · Cited by 213
Self-citationRetractedWang, X., Wang, Y., Kim, H. P., Nakahira, K., Ryter, S. W., & Choi, A. M. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607610200 · Cited by 192
RetractedWu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases
Maines, M. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.517 · Cited by 2,489
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000
Carbon Monoxide: a Putative Neural Messenger
Verma, A. M., Hirsch, D. B., Glatt, C. E., Ronnett, G. V., & Snyder, S. H. (1993) · Science · doi:10.1126/science.7678352 · Cited by 1,563
Tenhunen, R., Marver, H. S., & Schmid, R. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63477-5 · Cited by 1,357
Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
Kelly, D. P., & Scarpulla, R. C. (2004) · Genes & Development · doi:10.1101/gad.1177604 · Cited by 1,243
Cited by
Sorted by citations
The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,643
Mechanisms of Cell Protection by Heme Oxygenase-1
Gozzelino, R., Jeney, V., & Soares, M. P. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105600 · Cited by 1,241
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Calabrese, E. J., & Mattson, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3074 · Cited by 817
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Developing drug molecules for therapy with carbon monoxide
Romão, C. C., Blättler, W. A., Seixas, J. D., & Bernardes, G. J. L. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15317c · Cited by 524
Metadata
- Authors
- Piantadosi, C. A.
- Affiliations
- Duke University (US)
- Corresponding author
- Piantadosi, Claude A.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 45
- Issue
- 5
- Pages
- 562-569
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC2570053
- OpenAlex
- W2087826558
- Cited by
- 281
- References
- 145
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 15 · 2023: 13 · 2022: 19 · 2021: 16 · 2020: 21 · 2019: 8 · 2018: 16 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 17 · 2013: 16 · 2012: 16
- FWCI
- 1.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL090679)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- carbon monoxide, reactive oxygen species, oxidative stress, heme proteins, heme oxygenase, pro-oxidant activity, redox signaling, stress-activated kinases, redox-sensitive transcription factors, antioxidant enzymes, co-toxicity
- MeSH terms
- Adaptation, Biological, Animals, Carbon Monoxide, Hemeproteins, Humans, Signal Transduction, Reactive Oxygen Species, Oxidative Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review