The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models
Abstract
Reactive oxygen species (ROS) may contribute to tissue damage in many pathophysiological conditions and participate in physiological signaling processes. The mechanisms by which cells sense prooxidant states, and activate signaling pathways leading to adaptive responses, remain incompletely understood. Bacteria contain several transcriptional regulators (e.g., OxyR) and a low-molecular-weight heat shock protein (HSP33), whose activity increases upon oxidation of critical sulfhydryl residues. These proteins participate in cellular adaptation to oxidative stress. In higher organisms, heme oxygenase-1 (HO-1) has been widely studied as a model for redox-regulated gene expression. Expression of HO-1 responds to chemical and physical agents that directly or indirectly generate ROS. Depletion of cellular reduced glutathione may act as a signal for HO-1 transcriptional activation. Furthermore, antioxidants and metal-chelating compounds can modulate HO-1 expression. Several signaling molecules (e.g., mitogen-activated protein kinases), transcriptional regulators (activator protein-1, NF-E2-related factor-2, hypoxia-inducible factor-1, Bach-1), as well as two enhancer regions in the ho-1 5' regulatory region, participate in the regulation of the ho-1 gene. HO-1 protein expression can occur in the lung in response to oxidative stress associated with infection, altered oxygen tension, and inflammatory diseases. HO-1 remains widely regarded as a protective mechanism against oxidative tissue injury.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926
Regulation of Mammalian O 2 Homeostasis by Hypoxia-Inducible Factor 1
Semenza, G. L. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.551 · Cited by 1,914
Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782
Self-citationHemoprotein Bach1 regulates enhancer availability of heme oxygenase‐1 gene
Sun, J., Hoshino, H., Takaku, K., Nakajima, O., Muto, A., Suzuki, H., Tashiro, S., Takahashi, S., Shibahara, S., Alam, J., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf516 · Cited by 637
Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
Ryter, S. W., Otterbein, L. E., Morse, D., & Choi, A. M. K. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015957026924 · Cited by 497
Self-citationLi, N., Venkatesan, M. I., Miguel, A., Kaplan, R., Gujuluva, C., Alam, J., & Nel, A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.6.3393 · Cited by 267
Glial HO-1 expression, iron deposition and oxidative stress in neurodegenerative diseases
Schipper, H. M. (1999) · Neurotoxicity Research · doi:10.1007/bf03033339 · Cited by 72
Cited by
Oxidative stress, inflammation, and cancer: How are they linked?
Reuter, S., Gupta, S. C., Chaturvedi, M. M., & Aggarwal, B. B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.006 · Cited by 5,441
Heme Oxygenase-1/Carbon Monoxide: From Basic Science to Therapeutic Applications
Ryter, S. W., Alam, J., & Choi, A. M. K. (2006) · Physiological Reviews · doi:10.1152/physrev.00011.2005 · Cited by 2,307
Self-citationCO AS A CELLULAR SIGNALING MOLECULE
Kim, H. P., Ryter, S. W., & Choi, A. M. K. (2006) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141053 · Cited by 426
Self-citationOxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352
Arsenic in the aetiology of cancer
Tapio, S., & Grosche, B. (2006) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2006.02.001 · Cited by 334
Metadata
- Authors
- Ryter, S. W., & Choi, A. M. K.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2005-01
- Volume
- 7
- Issue
- 1-2
- Pages
- 80-91
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2033474573
- Cited by
- 243
- References
- 10
- FWCI
- 4.48
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models. https://app.cochat.ai/papers/10.1089/ars.2005.7.80
- The paper
- Ryter, S. W., & Choi, A. M. K. (2005). Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models. Antioxidants & Redox Signaling. https://doi.org/10.1089/ars.2005.7.80
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
