The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Myoglobin: an essential hemoprotein in striated muscle
Abstract
SUMMARY: Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation. Functionally, myoglobin is well accepted as an O2-storage protein in muscle, capable of releasing O2during periods of hypoxia or anoxia. Myoglobin is also thought to buffer intracellular O2 concentration when muscle activity increases and to facilitate intracellular O2 diffusion by providing a parallel path that augments simple diffusion of dissolved O2. The use of gene targeting and other molecular biological techniques has revealed important new insights into the developmental and environmental regulation of myoglobin and provided additional functions for this hemoprotein such as scavenging nitric oxide and reactive O2 species. These recent findings, coupled with additional emerging technologies and the discovery of other tissue globins, provide a framework for addressing new questions about myoglobin and readdressing old ones.
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Cites
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THE PHYSIOLOGICAL BASIS OF DIVING TO DEPTH: Birds and Mammals
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Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Circulating Testosterone as the Hormonal Basis of Sex Differences in Athletic Performance
Handelsman, D. J., Hirschberg, A. L., & Bermon, S. (2018) · Endocrine Reviews · doi:10.1210/er.2018-00020 · Cited by 594
Improving Protein Expression, Stability, and Function with ProteinMPNN
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Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
Silvestri, L., Pagani, A., & Camaschella, C. (2008) · Blood · doi:10.1182/blood-2007-07-100677 · Cited by 311
Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin
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Metadata
- Authors
- Ordway, G. A., & Garry, D. J.
- Venue
- Journal of Experimental Biology
- Publisher
- The Company of Biologists
- Published
- 2004-09-15
- Volume
- 207
- Issue
- 20
- Pages
- 3441-3446
- ISSN
- 0022-0949 (ISSN-L)
- 1477-9145
- OpenAlex
- W2030351692
- Cited by
- 447
- References
- 40
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
