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- Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA Journal Article
- A universal mode of helix packing in RNA Journal Article
- Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: delineation of a novel sub-family of bacterial DEAD proteins Journal Article
- Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA Journal Article
- Escherichia coli DbpA is a 3' --> 5' RNA helicase. Journal Article
- Interaction of Escherichia coli DbpA with 23S rRNA in different functional states of the enzyme. Journal Article
- Kinetic analysis of the RNA-dependent adenosinetriphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA Journal Article
- RNA aptamers to the peptidyl transferase inhibitor chloramphenicol Journal Article
- The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA Journal Article
- The carboxy-terminal domain of the DExD/H protein YxiN is sufficient to confer specificity for 23 S rRNA Journal Article
- The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. Journal Article
- Unlinked rRNA genes are widespread among bacteria and archaea Journal Article
- Use of specific rRNA oligonucleotide probes for microscopic detection of Mycobacterium avium complex organisms in tissue Journal Article