The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
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
Cited by
Cancer metabolism: a therapeutic perspective
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
Structure of the human LAT1–4F2hc heteromeric amino acid transporter complex
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
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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