Probing fast ribozyme reactions under biological conditions with rapid quench-flow kinetics-Reference-Cited by-同舟云学术

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Probing fast ribozyme reactions under biological conditions with rapid quench-flow kinetics

Published:2017-05 Issue: Volume:120 Page:125-134
ISSN:1046-2023
Container-title:Methods
language:en
Short-container-title:Methods

Author:

Bingaman Jamie L.,Messina Kyle J.,Bevilacqua Philip C.

Funder

National Science Foundation

National Institutes of Health

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology,Molecular Biology

Reference60 articles.

1. Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferase;Berthold;J. Biol. Chem.,2008

2. A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics;Anderson;Biochemistry,1988

3. Escherichia coli glutamine synthetase. Determination of rate-limiting steps by rapid-quench and isotope partitioning experiments. Derivation of equations for isotope partitioning experiments for a terreactant enzyme;Meek;Biochemistry,1982

4. The catalytic mechanism of EPSP synthase revisited;Lewis;Biochemistry,1999

5. Direct electron transfer to a metalloenzyme redox center coordinated to a monolayer-protected cluster;Abad;J. Am. Chem. Soc.,2009

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2. Small Molecule Rescue and Glycosidic Conformational Analysis of the Twister Ribozyme;Biochemistry;2019-11-19

3. Mechanistic Origins of Enzyme Activation in Human Glucokinase Variants Associated with Congenital Hyperinsulinism;Biochemistry;2018-02-09

4. Editorial;Methods;2017-05

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