The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA.
Open accessAbstract
Refinement of the diffraction data at 2.5-A resolution from orthorhombic crystals of yeast tRNAPhe has proceeded to the point where spermine and magnesium ions can be located in the difference electron density map. Two spermine molecules are found: one is located in the major groove at one end of the anticodon stem; the other is near the variable loop and curls around phosphate 10 in a region where the polynucleotide chain takes a sharp turn. Four distinct magnesium ions have been identified: one in the anticodon loop, two in the D loop, and one coordinated with phosphates 8, 9, 11, and 12, where the polynucleotide chain is coiled. The conformation of the anticodon stem and loop is stabilized by the cations at the end of the molecule. The positions of these ions may be related to aspects of the biological activity of tRNA. The spermine and magnesium ions appear to be important in maintaining the overall folding of the tRNA molecule.
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Cites
1,4-Diaminobutane (Putrescine), Spermidine, and Spermine
Tabor, C. W., & Tabor, H. (1976) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.45.070176.001441 · Cited by 1,198
Structure of yeast phenylalanine tRNA at 3 Å resolution
Robertus, J. D., Ladner, J. E., Finch, J. T., Rhodes, D., Brown, R. S., Clark, B. F. C., & Klug, A. (1974) · Nature · doi:10.1038/250546a0 · Cited by 1,032
Transfer RNA: Molecular Structure, Sequence, and Properties
Rich, A., & RajBhandary, U. L. (1976) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.45.070176.004105 · Cited by 650
Self-citationQuigley, G. J., & Rich, A. (1976) · Science · doi:10.1126/science.790568 · Cited by 530
Self-citationThree-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain
Kim, S. H., Quigley, G. J., Suddath, F. L., McPherson, A., Sneden, D., Kim, J. J., Weinzierl, J., & Rich, A. (1973) · Science · doi:10.1126/science.179.4070.285 · Cited by 421
Self-citationA crystallographic study of metal-binding to yeast phenylalanine transfer RNA
Jack, A., Landner, J. E., Rhodes, D., Brown, R. S., & Klug, A. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80054-5 · Cited by 321
RNA - ligand interactions:(I) magnesium binding sites in yeast tRNAPhe
Holbrook, S. R., Sussman, J. L., Warrant, R. W., Church, G. M., & Kim, S.-H. (1977) · Nucleic Acids Research · doi:10.1093/nar/4.8.2811 · Cited by 219
Tertiary Structure in Transfer Ribonucleic AcidsPreprint
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Cited by
Magnesium in man: implications for health and disease
de Baaij, J. H. F., Hoenderop, J. G. J., & Bindels, R. J. M. (2015) · Physiological Reviews · doi:10.1152/physrev.00012.2014 · Cited by 1,726
Polyamines: Mysterious Modulators of Cellular Functions
Igarashi, K., & Kashiwagi, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2601 · Cited by 888
Modulation of cellular function by polyamines
Igarashi, K., & Kashiwagi, K. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.07.009 · Cited by 851
Probing the structure of RNAs in solution
Ehresmann, C., Baudin, F., Mougel, M., Romby, P., Ebel, J.-P., & Ehresmann, B. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.22.9109 · Cited by 730
Draper, D. E., Grilley, D., & Soto, A. M. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144511 · Cited by 484
Metadata
- Authors
- Quigley, G. J., Teeter, M. M., & Rich, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1978-01
- Volume
- 75
- Issue
- 1
- Pages
- 64-68
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2050560798
- Cited by
- 381
- References
- 9
- FWCI
- 8.60
- Type
- journal article
- Language
- en
- Open access
- green
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- Quigley, G. J., Teeter, M. M., & Rich, A. (1978). Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.75.1.64
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