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Page 1
Evidence for processivity and two-step binding of the RNA substrate from studies of J1/2 mutants of the Tetrahymena ribozyme.
Herschlag D. Herschlag D. Biochemistry. 1992 Feb 11;31(5):1386-99. doi: 10.1021/bi00120a015. Biochemistry. 1992. PMID: 1736996
These paradoxical enhancements are caused by decreased affinity of the ribozyme for S and P [Young, B., Herschlag, D., & Cech, T.R. (1991) Cell 67, 1007]. An additional property of these mutant ribozymes, decreased fidelity of RNA cleavage, is now analyzed. ...
These paradoxical enhancements are caused by decreased affinity of the ribozyme for S and P [Young, B., Herschlag, D., & C …
Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 2. Kinetic description of the reaction of an RNA substrate that forms a mismatch at the active site.
Herschlag D, Cech TR. Herschlag D, et al. Biochemistry. 1990 Nov 6;29(44):10172-80. doi: 10.1021/bi00496a004. Biochemistry. 1990. PMID: 2271646
The site-specific endonuclease reaction catalyzed by the ribozyme from the Tetrahymena pre-rRNA intervening sequence has been characterized with a substrate that forms a "matched" duplex with the 5' exon binding site of the ribozyme [G2CCCUCUA5 + G in equilibrium with G2CCCUCU + …
The site-specific endonuclease reaction catalyzed by the ribozyme from the Tetrahymena pre-rRNA intervening sequence has been characterized …
Contributions of 2'-hydroxyl groups of the RNA substrate to binding and catalysis by the Tetrahymena ribozyme. An energetic picture of an active site composed of RNA.
Herschlag D, Eckstein F, Cech TR. Herschlag D, et al. Biochemistry. 1993 Aug 17;32(32):8299-311. doi: 10.1021/bi00083a034. Biochemistry. 1993. PMID: 7688572
The 2'-hydroxyl at position -1 exerts its large effect nearly exclusively on the chemical step [Herschlag, D., Eckstein, F., & Cech, T.R. (1993) Biochemistry (following paper in this issue)]. ...
The 2'-hydroxyl at position -1 exerts its large effect nearly exclusively on the chemical step [Herschlag, D., Eckstein, F., & …
286 results