Contributions of basic residues to ribosomal protein L11 recognition of RNA
- 21 January 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 295 (3) , 569-580
- https://doi.org/10.1006/jmbi.1999.3372
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Engrailed homeodomain-DNA complex at 2.2 å resolution: a detailed view of the interface and comparison with other engrailed structures 1 1Edited by T. RichmondJournal of Molecular Biology, 1998
- The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centreJournal of Molecular Biology, 1998
- The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNAJournal of Molecular Biology, 1997
- Affinities and selectivities of divalent cation binding sites within an RNA tertiary structureJournal of Molecular Biology, 1997
- Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11Biochemistry, 1996
- Stabilization of a ribosomal RNA tertiary structure by ribosomal protein L11Journal of Molecular Biology, 1995
- Thermodynamics of RNA Folding in a Conserved Ribosomal RNA DomainJournal of Molecular Biology, 1994
- Sequence logos: a new way to display consensus sequencesNucleic Acids Research, 1990
- Ribosomal proteins EL11 from Escherichia coli and L15 from Saccharomyces cerevisiae bind to the same site in both yeast 26 S and mouse 28 S rRNAJournal of Molecular Biology, 1987
- Ion effects on ligand-nucleic acid interactionsJournal of Molecular Biology, 1976