Herschlag D - Search Results

1

Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution.

Zalatan JG, Fenn TD, Brunger AT, Herschlag D. Zalatan JG, et al. Among authors: herschlag d. Biochemistry. 2006 Aug 15;45(32):9788-803. doi: 10.1021/bi060847t. Biochemistry. 2006. PMID: 16893180 Free article.

2

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 …

3

The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase.

Hollfelder F, Herschlag D. Hollfelder F, et al. Among authors: herschlag d. Biochemistry. 1995 Sep 26;34(38):12255-64. doi: 10.1021/bi00038a021. Biochemistry. 1995. PMID: 7547968

4

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., & …

5

The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction.

Herschlag D, Eckstein F, Cech TR. Herschlag D, et al. Biochemistry. 1993 Aug 17;32(32):8312-21. doi: 10.1021/bi00083a035. Biochemistry. 1993. PMID: 7688573

6

Dissection of the role of the conserved G.U pair in group I RNA self-splicing.

Knitt DS, Narlikar GJ, Herschlag D. Knitt DS, et al. Among authors: herschlag d. Biochemistry. 1994 Nov 22;33(46):13864-79. doi: 10.1021/bi00250a041. Biochemistry. 1994. PMID: 7947795

7

Comparison of pH dependencies of the Tetrahymena ribozyme reactions with RNA 2'-substituted and phosphorothioate substrates reveals a rate-limiting conformational step.

Herschlag D, Khosla M. Herschlag D, et al. Biochemistry. 1994 May 3;33(17):5291-7. doi: 10.1021/bi00183a036. Biochemistry. 1994. PMID: 8172903

8

Catalysis of the hydrolysis of phosphorylated pyridines by alkaline phosphatase has little or no dependence on the pKa of the leaving group.

Labow BI, Herschlag D, Jencks WP. Labow BI, et al. Among authors: herschlag d. Biochemistry. 1993 Aug 31;32(34):8737-41. doi: 10.1021/bi00085a003. Biochemistry. 1993. PMID: 8395879

9

pH dependencies of the Tetrahymena ribozyme reveal an unconventional origin of an apparent pKa.

Knitt DS, Herschlag D. Knitt DS, et al. Among authors: herschlag d. Biochemistry. 1996 Feb 6;35(5):1560-70. doi: 10.1021/bi9521147. Biochemistry. 1996. PMID: 8634287

10

Mechanistic investigations of a ribozyme derived from the Tetrahymena group I intron: insights into catalysis and the second step of self-splicing.

Mei R, Herschlag D. Mei R, et al. Among authors: herschlag d. Biochemistry. 1996 May 7;35(18):5796-809. doi: 10.1021/bi9527653. Biochemistry. 1996. PMID: 8639540

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