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Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension.
Moazed D, Stern S, Noller HF. Moazed D, et al. J Mol Biol. 1986 Feb 5;187(3):399-416. doi: 10.1016/0022-2836(86)90441-9. J Mol Biol. 1986. PMID: 2422386
We have investigated in detail the higher-order structure of 16 S ribosomal RNA, both in its naked form and in 30 S ribosomal subunits. ...Our data also provide information relevant to tertiary and quaternary structure of 16 S rRNA. Data obtained with naked 1 …
We have investigated in detail the higher-order structure of 16 S ribosomal RNA, both in its naked form and in 30 S ribosomal …
Localization of the binding site for protein S4 on 16 S ribosomal RNA by chemical and enzymatic probing and primer extension.
Stern S, Wilson RC, Noller HF. Stern S, et al. J Mol Biol. 1986 Nov 5;192(1):101-10. doi: 10.1016/0022-2836(86)90467-5. J Mol Biol. 1986. PMID: 3820298
We have examined the effect of binding ribosomal protein S4 to 16 S rRNA on the susceptibility of the RNA to a variety of chemical and enzymatic probes. ...We conclude that this is the major, and possibly sole region of contact between 16 S rRNA and S4. Many of the …
We have examined the effect of binding ribosomal protein S4 to 16 S rRNA on the susceptibility of the RNA to a variety of chemical an …
Interaction of proteins S16, S17 and S20 with 16 S ribosomal RNA.
Stern S, Changchien LM, Craven GR, Noller HF. Stern S, et al. J Mol Biol. 1988 Mar 20;200(2):291-9. doi: 10.1016/0022-2836(88)90241-0. J Mol Biol. 1988. PMID: 3373529
We have used rapid chemical probing methods to examine the effect of assembly of ribosomal proteins S16, S17 and S20 on the reactivity of individual residues of 16 S rRNA. ...
We have used rapid chemical probing methods to examine the effect of assembly of ribosomal proteins S16, S17 and S20 on the reactivity of in …
Model for the three-dimensional folding of 16 S ribosomal RNA.
Stern S, Weiser B, Noller HF. Stern S, et al. J Mol Biol. 1988 Nov 20;204(2):447-81. doi: 10.1016/0022-2836(88)90588-8. J Mol Biol. 1988. PMID: 2464693
We have derived a model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA, using interactive computer graphic methods. It is based on (1) the secondary structure derived from comparative sequence analysis, (2) the three-dimensional co-ordinates for t …
We have derived a model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA, using interactive computer graphic …
Probing the assembly of the 3' major domain of 16 S rRNA. Interactions involving ribosomal proteins S2, S3, S10, S13 and S14.
Powers T, Stern S, Changchien LM, Noller HF. Powers T, et al. J Mol Biol. 1988 Jun 20;201(4):697-716. doi: 10.1016/0022-2836(88)90468-8. J Mol Biol. 1988. PMID: 2459390
We have used rapid probing methods to follow the changes in reactivity of residues in 16 S rRNA to chemical and enzymatic probes as ribosomal proteins S2, S3, S10, S13 and S14 are assembled into 30 S subunits. ...In addition, S2 protects residues in the 1160/1170 st …
We have used rapid probing methods to follow the changes in reactivity of residues in 16 S rRNA to chemical and enzymatic probes as r …
Interaction of ribosomal proteins S5, S6, S11, S12, S18 and S21 with 16 S rRNA.
Stern S, Powers T, Changchien LM, Noller HF. Stern S, et al. J Mol Biol. 1988 Jun 20;201(4):683-95. doi: 10.1016/0022-2836(88)90467-6. J Mol Biol. 1988. PMID: 2459389
We have examined the effects of assembly of ribosomal proteins S5, S6, S11, S12, S18 and S21 on the reactivities of residues in 16 S rRNA towards chemical probes. ...These observations are discussed in terms of the effects of S5 and S12 on streptomycin binding, and in term …
We have examined the effects of assembly of ribosomal proteins S5, S6, S11, S12, S18 and S21 on the reactivities of residues in 16 S
Studies on the architecture and function of 16S rRNA.
Noller HF, Stern S, Moazed D, Powers T, Svensson P, Changchien LM. Noller HF, et al. Cold Spring Harb Symp Quant Biol. 1987;52:695-708. doi: 10.1101/sqb.1987.052.01.079. Cold Spring Harb Symp Quant Biol. 1987. PMID: 3454283 No abstract available.
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