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Structure of the Yeast Mitochondrial Large Ribosomal Subunit
Open accessAbstract
Mitoribosomes: Mitochondria—found in all eukaryotic cells—have transferred most of their genes to the nuclear genome. The nuclear-localized mitochondrial genes are expressed and translated in the cytoplasm and the resulting mitochondrial proteins are imported into the mitochondria. Nevertheless, a few genes remain within mitochondria in the mitochondrial genome, and these genes are translated by mitochondrial ribosomes (mitoribosomes). Amunts et al. (p. 1485 ; see the Perspective by Kühlbrandt ) determined the structure of mitoribosomes from yeast using single-particle cryo–electron microscopy. The mitoribosome is highly diverged from the bacterial and eukaryotic ribosomes with, for example, a distinctive exit tunnel for the newly synthesized peptide, and a membrane facing protuberance that might help to anchor the mitoribosome to the mitochondrial membrane.
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Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Mfold web server for nucleic acid folding and hybridization prediction
Zuker, M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg595 · Cited by 13,404
Origin and evolution of the ribosome
Fox, G. E. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003483 · Cited by 258
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Martinez-Outschoorn, U. E., Peiris-Pagés, M., Pestell, R. G., Sotgia, F., & Lisanti, M. P. (2017) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2016.60 · Cited by 1,505
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
Barad, B. A., Echols, N., Wang, R. Y.-R., Cheng, Y., DiMaio, F., Adams, P. D., & Fraser, J. S. (2015) · Nature Methods · doi:10.1038/nmeth.3541 · Cited by 886
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Yan, R., Zhao, X., Lei, J., & Zhou, Q. (2019) · Nature · doi:10.1038/s41586-019-1011-z · Cited by 358
Mechanisms and regulation of protein synthesis in mitochondria
Kummer, E., & Ban, N. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00332-2 · Cited by 349
Organization and regulation of mitochondrial protein synthesis
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Qian, H., Zhao, X., Yan, R., Yao, X., Gao, S., Sun, X., Du, X., Yang, H., Wong, C. C. L., & Yan, N. (2020) · Nature · doi:10.1038/s41586-020-2290-0 · Cited by 108
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Yan, R., Cao, P., Song, W., Qian, H., Du, X., Coates, H. W., Zhao, X., Li, Y., Gao, S., Gong, X., et al. (2021) · Science · doi:10.1126/science.abb2224 · Cited by 100
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Bowman, J. C., Hud, N. V., & Williams, L. D. (2015) · Journal of Molecular Evolution · doi:10.1007/s00239-015-9669-9 · Cited by 99
De novo modeling in cryo-EM density maps with Pathwalking
Chen, M., Baldwin, P. R., Ludtke, S. J., & Baker, M. L. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.004 · Cited by 82
Lightowlers, R. N., Rozanska, A., & Chrzanowska-Lightowlers, Z. M. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.054 · Cited by 70
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Singh, A. P., Salvatori, R., Aftab, W., Kohler, A., Carlström, A., Forne, I., Imhof, A., & Ott, M. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.024 · Cited by 65
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Ast, T., Itoh, Y., Sadre, S., McCoy, J. G., Namkoong, G., Wengrod, J. C., Chicherin, I., Joshi, P. R., Kamenski, P., Suess, D. L. M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.016 · Cited by 58
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Self-citationModulating co-translational protein folding by rational design and ribosome engineering
Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45
Molecular wiring of a mitochondrial translational feedback loop
Salvatori, R., Kehrein, K., Singh, A. P., Aftab, W., Möller-Hergt, B. V., Forne, I., Imhof, A., & Ott, M. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.11.019 · Cited by 34
Structure of the yeast Swi/Snf complex in a nucleosome free state
Wang, C., Guo, Z., Zhan, X., Yang, F., Wu, M., & Zhang, X. (2020) · Nature Communications · doi:10.1038/s41467-020-17229-x · Cited by 25
Origins and Early Evolution of the Ribosome
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Metadata
- Authors
- Amunts, A., Brown, A., Bai, X.-C., Llácer, J. L., Hussain, T., Emsley, P., Long, F., Murshudov, G., Scheres, S. H. W., & Ramakrishnan, V.
- Venue
- Science
- Published
- 2014-03-28
- Volume
- 343
- Issue
- 6178
- Pages
- 1485-1489
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2150790075
- Cited by
- 579
- References
- 4
- FWCI
- 29.20
- Type
- journal article
- Language
- en
- Open access
- green
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