The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
RNA-Protein Interactions in 30 S Ribosomal Subunits: Folding and Function of 16 S rRNA
Abstract
Chemical probing methods have been used to "footprint" 16 S ribosomal RNA (rRNA) at each step during the in vitro assembly of twenty 30 S subunit ribosomal proteins. These experiments yield information about the location of each protein relative to the structure of 16 S rRNA and provide the basis for derivation of a detailed model for the three-dimensional folding of 16 S rRNA. Several lines of evidence suggest that protein-dependent conformational changes in 16 S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16 S rRNA in the 30 S subunit.
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Citations
Cites
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684
Greider, C. W., & Blackburn, E. H. (1987) · Cell · doi:10.1016/0092-8674(87)90576-9 · Cited by 1,150
Cited by
Structure of the 30S ribosomal subunit
Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035
Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
Noller, H. F., Hoffarth, V., & Zimniak, L. (1992) · Science · doi:10.1126/science.1604315 · Cited by 728
Self-citationThe assembly of prokaryotic ribosomes
Nierhaus, K. H. (1991) · Biochimie · doi:10.1016/0300-9084(91)90054-5 · Cited by 235
Interaction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA
Woodcock, J., Moazed, D., Cannon, M., Davies, J., & Noller, H. F. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07863.x · Cited by 229
Self-citationA Conformational Switch in Escherichia coli 16 S Ribosomal RNA During Decoding of Messenger RNA
Lodmell, J. S., & Dahlberg, A. E. (1997) · Science · doi:10.1126/science.277.5330.1262 · Cited by 212
Evolution of Protein Synthesis from an RNA World
Noller, H. F. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003681 · Cited by 155
Self-citationTranslational termination: “stop” for protein synthesis or “pause” for regulation of gene expression
Tate, W. P., & Brown, C. M. (1992) · Biochemistry · doi:10.1021/bi00124a001 · Cited by 138
The driving force for molecular evolution of translation
NOLLER, H. F. (2004) · RNA · doi:10.1261/rna.7142404 · Cited by 96
Self-citationInteraction of tetracycline with RNA: photoincorporation into ribosomal RNA of Escherichia coli
Oehler, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1219 · Cited by 66
Ribosomal proteins: Structure, function, and evolution
Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060028 · Cited by 63
Shape changes and cooperativity in the folding of the central domain of the 16S ribosomal RNA
Hori, N., Denesyuk, N. A., & Thirumalai, D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020837118 · Cited by 31
Functional characterization of dynamic nascent RNA folding ensembles in real time
Gor, K., Geissen, E. M., & Duss, O. (2026) · Science Advances · doi:10.1126/sciadv.aec4037 · Cited by 4
Metadata
- Authors
- Stern, S., Powers, T., Changchien, L.-M., & Noller, H. F.
- Venue
- Science
- Published
- 1989-05-19
- Volume
- 244
- Issue
- 4906
- Pages
- 783-790
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2041815688
- Cited by
- 285
- References
- 2
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- closed
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