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NC1=NC(=S)N(C=C1)[C@H]2O[C@H](CO)[C@@H](O)[C@H]2O
L Wang et al.
Nucleic acids research, 25(21), 4355-4361 (1997-10-23)
The hammerhead domain is one of the smallest known ribozymes. Like other ribozymes it catalyzes site-specific cleavage of a phosphodiester bond. The hammerhead ribozyme has been the subject of a vast number of biochemical and structural studies aimed at determining
Akihiro Ohkubo et al.
Organic & biomolecular chemistry, 10(10), 2008-2010 (2012-01-28)
In this paper, we report DNA and 2'-OMe-RNA probes containing 5-methyl-2-thiocytidine (m(5)s(2)C) residues that can bind selectively and strongly to the corresponding RNA targets containing inosine residues by the significant stacking effect and steric hindrance of the 2-thiocarbonyl group.
D J Earnshaw et al.
Biochemistry, 39(21), 6410-6421 (2000-06-01)
The hairpin ribozyme achieves catalytic cleavage through interaction of essential nucleotides located in two distinct helical domains that include internal loops. Initial docking of the two domains is ion dependent and appears to be followed by a structural rearrangement that
R L Joshi et al.
FEBS letters, 208(2), 189-193 (1986-11-24)
A new approach for the fluorescence labeling of an aminoacyl-tRNA at the 3'-end is applied to study its interaction with bacterial elongation factor Tu (EF-Tu) and GTP at equilibrium. The penultimate cytidine residue in yeast tRNATyr-C-C-A was replaced by 2-thiocytidine
T Döring et al.
The EMBO journal, 13(11), 2677-2685 (1994-06-01)
A photo-reactive diazirine derivative was attached to the 2-thiocytidine residue at position 32 of tRNA(Arg)I from Escherichia coli. This modified tRNA was bound under suitable conditions to the A, P or E site of E.coli ribosomes. After photo-activation of the
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