The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
Open accessAbstract
The inner membrane system of mitochondria is known to consist of two contiguous but distinct membranes: the inner boundary membrane, which apposes the outer membrane, and the cristal membrane, which forms tubules or lamellae in the interior. Using immunolabeling and transmission electron microscopy of bovine heart tissue, we have calculated that around 94% of both Complex III of the respiratory chain and the ATP synthase are located in the cristal membrane, and only around 6% of either is in the inner boundary membrane. When accounting for the topographical ratio of cristal membrane versus inner boundary membrane, we find that both complexes exist at a 2.2–2.6‐fold higher concentration in the cristal membrane. The residual protein in the inner boundary membrane may be newly assembled complexes destined for cristal membranes. Our results argue for restricted diffusion of complexes through the cristal junctions and indicate that the mitochondrial cristae comprise a regulated submitochondrial compartment specialized for ATP production.
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Cites
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Cited by
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Functions and dysfunctions of mitochondrial dynamics
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Mitochondrial Cristae: Where Beauty Meets Functionality
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Metadata
- Authors
- Gilkerson, R. W., Selker, J. M. L., & Capaldi, R. A.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2003-06-14
- Volume
- 546
- Issue
- 2-3
- Pages
- 355-358
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2093921916
- Cited by
- 340
- References
- 17
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Gilkerson, R. W., Selker, J. M. L., & Capaldi, R. A. (2003). The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Letters. https://doi.org/10.1016/s0014-5793(03)00633-1
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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.