The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae
Open accessAbstract
Ribosomes are highly conserved ribonucleoprotein nanomachines that translate information in the genome to create the proteome in all cells. In yeast these complex particles contain four RNAs (>5400 nucleotides) and 79 different proteins. During the past 25 years, studies in yeast have led the way to understanding how these molecules are assembled into ribosomes in vivo. Assembly begins with transcription of ribosomal RNA in the nucleolus, where the RNA then undergoes complex pathways of folding, coupled with nucleotide modification, removal of spacer sequences, and binding to ribosomal proteins. More than 200 assembly factors and 76 small nucleolar RNAs transiently associate with assembling ribosomes, to enable their accurate and efficient construction. Following export of preribosomes from the nucleus to the cytoplasm, they undergo final stages of maturation before entering the pool of functioning ribosomes. Elaborate mechanisms exist to monitor the formation of correct structural and functional neighborhoods within ribosomes and to destroy preribosomes that fail to assemble properly. Studies of yeast ribosome biogenesis provide useful models for ribosomopathies, diseases in humans that result from failure to properly assemble ribosomes.
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Cites
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A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis
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Self-citationOne core, two shells: bacterial and eukaryotic ribosomes
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Cross-linking, ligation, and sequencing of hybrids reveals RNA–RNA interactions in yeast
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RNA transcription modulates phase transition-driven nuclear body assembly
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Ribosome biogenesis: Emerging evidence for a central role in the regulation of skeletal muscle mass
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Structural and functional insights into the mode of action of a universally conserved Obg GTPase.
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RIOK2 phosphorylation by RSK promotes synthesis of the human small ribosomal subunit
Cerezo, E. L., Houles, T., Lié, O., Sarthou, M.-K., Audoynaud, C., Lavoie, G., Halladjian, M., Cantaloube, S., Froment, C., Burlet-Schiltz, O., et al. (2021) · PLOS Genetics · doi:10.1371/journal.pgen.1009583 · Cited by 26
Through the looking glass: milestones on the road towards mirroring life
Rohden, F., Hoheisel, J. D., & Wieden, H.-J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.06.006 · Cited by 18
Pulse labeling reveals the tail end of protein folding by proteome profiling
Zhu, M., Kuechler, E. R., Wong, R. W. K., Calabrese, G., Sitarik, I. M., Rana, V., Stoynov, N., O’Brien, E. P., Gsponer, J., & Mayor, T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111096 · Cited by 13
The SSU Processome Component Utp25p is a Pseudohelicase
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Metadata
- Authors
- Woolford, J. L., & Baserga, S. J.
- Venue
- Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-11-01
- Volume
- 195
- Issue
- 3
- Pages
- 643-681
- ISSN
- 0016-6731 (ISSN-L)
- 1943-2631
- OpenAlex
- W2124204438
- Cited by
- 757
- References
- 5
- FWCI
- 23.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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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).
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