Stoner D, Browning C, Bulmer D, Ward T, Macdonell M
Appl Environ Microbiol. 1996; 62(6):1969-76.
PMID: 16535333
PMC: 1388871.
DOI: 10.1128/aem.62.6.1969-1976.1996.
Grune M, Furste J, Klussmann S, Erdmann V, Brown L
Nucleic Acids Res. 1996; 24(13):2592-6.
PMID: 8692701
PMC: 145962.
DOI: 10.1093/nar/24.13.2592.
Kuntzel H, Piechulla B, Hahn U
Nucleic Acids Res. 1983; 11(3):893-900.
PMID: 6835839
PMC: 325760.
DOI: 10.1093/nar/11.3.893.
Stiege W, Zwieb C, Brimacombe R
Nucleic Acids Res. 1982; 10(22):7211-29.
PMID: 6818528
PMC: 326999.
DOI: 10.1093/nar/10.22.7211.
PAPANICOLAOU C, Gouy M, Ninio J
Nucleic Acids Res. 1984; 12(1 Pt 1):31-44.
PMID: 6694903
PMC: 320981.
DOI: 10.1093/nar/12.1part1.31.
Phylogeny of the 5S ribosomal RNA from Synechococcus lividus II: the cyanobacterial/chloroplast 5S RNAs form a common structural class.
Delihas N, Andersen J, Berns D
J Mol Evol. 1984; 21(4):334-7.
PMID: 6443313
DOI: 10.1007/BF02115651.
Sequences of the 5S rRNAs of Azotobacter vinelandii, Pseudomonas aeruginosa and Pseudomonas fluorescens with some notes on 5S RNA secondary structure.
Dams E, Vandenberghe A, De Wachter R
Nucleic Acids Res. 1983; 11(5):1245-52.
PMID: 6402760
PMC: 325793.
DOI: 10.1093/nar/11.5.1245.
Structural requirements for the interaction of 5S rRNA with the eukaryotic transcription factor IIIA.
Pieler T, Erdmann V, Appel B
Nucleic Acids Res. 1984; 12(22):8393-406.
PMID: 6390342
PMC: 320376.
DOI: 10.1093/nar/12.22.8393.
Nuclease protection analysis of ribonucleoprotein complexes: use of the cytotoxic ribonuclease alpha-sarcin to determine the binding sites for Escherichia coli ribosomal proteins L5, L18, and L25 on 5S rRNA.
Huber P, Wool I
Proc Natl Acad Sci U S A. 1984; 81(2):322-6.
PMID: 6364140
PMC: 344668.
DOI: 10.1073/pnas.81.2.322.
Chemical reactivity of E. coli 5S RNA in situ in the 50S ribosomal subunit.
Silberklang M, RajBhandary U, Luck A, Erdmann V
Nucleic Acids Res. 1983; 11(3):605-17.
PMID: 6340064
PMC: 325740.
DOI: 10.1093/nar/11.3.605.
Comparative structural analysis of cytoplasmic and chloroplastic 5S rRNA from spinach.
Pieler T, Digweed M, Bartsch M, Erdmann V
Nucleic Acids Res. 1983; 11(3):591-604.
PMID: 6340063
PMC: 325739.
DOI: 10.1093/nar/11.3.591.
Comparative structural analysis of eubacterial 5S rRNA by oxidation of adenines in the N-1 position.
Pieler T, Schreiber A, Erdmann V
Nucleic Acids Res. 1984; 12(7):3115-26.
PMID: 6201825
PMC: 318733.
DOI: 10.1093/nar/12.7.3115.
Oligonucleotide directed mutagenesis of Escherichia coli 5S ribosomal RNA: construction of mutant and structural analysis.
Goringer H, Wagner R, Jacob W, Dahlberg A, Zwieb C
Nucleic Acids Res. 1984; 12(18):6935-50.
PMID: 6091046
PMC: 320134.
DOI: 10.1093/nar/12.18.6935.
Structure and function of ribosomal RNA.
Brimacombe R, Stiege W
Biochem J. 1985; 229(1):1-17.
PMID: 3899100
PMC: 1145144.
DOI: 10.1042/bj2290001.
Analysis of a sequence region of 5S RNA from E. coli cross-linked in situ to the ribosomal protein L25.
Szymkowiak C, Wagner R
Nucleic Acids Res. 1985; 13(11):3953-68.
PMID: 3892485
PMC: 341289.
DOI: 10.1093/nar/13.11.3953.
Evolutionary changes in the higher order structure of the ribosomal 5S RNA.
McDougall J, Nazar R
Nucleic Acids Res. 1987; 15(1):161-79.
PMID: 3547323
PMC: 340403.
DOI: 10.1093/nar/15.1.161.
TFIIIA binds to different domains of 5S RNA and the Xenopus borealis 5S RNA gene.
Sands M, Bogenhagen D
Mol Cell Biol. 1987; 7(11):3985-93.
PMID: 3431548
PMC: 368067.
DOI: 10.1128/mcb.7.11.3985-3993.1987.
A comparison of the solution structures and conformational properties of the somatic and oocyte 5S rRNAs of Xenopus laevis.
Romaniuk P, de Stevenson I, Ehresmann C, Romby P, Ehresmann B
Nucleic Acids Res. 1988; 16(5):2295-312.
PMID: 3357778
PMC: 338217.
DOI: 10.1093/nar/16.5.2295.
Exploration of the L18 binding site on 5S RNA by deletion mutagenesis.
Gewirth D, Moore P
Nucleic Acids Res. 1988; 16(22):10717-32.
PMID: 3060848
PMC: 338935.
DOI: 10.1093/nar/16.22.10717.
Nuclease S1 analysis of eubacterial 5S rRNA secondary structure.
Macdonell M, Colwell R
J Mol Evol. 1985; 22(3):237-42.
PMID: 3001324
DOI: 10.1007/BF02099753.