Conserved thermochemistry of guanosine nucleophile binding for structurally distinct group I ribozymes
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
http://academic.oup.com/nar/article-pdf/24/19/3722/7063556/24-19-3722.pdf
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Novel Heat-Promoted Folding Dynamics of the yybP-ykoY Manganese Riboswitch: Kinetic and Thermodynamic Studies at the Single-Molecule Level;The Journal of Physical Chemistry B;2019-06-06
2. Differential Assembly of Catalytic Interactions within the Conserved Active Sites of Two Ribozymes;PLOS ONE;2016-08-08
3. A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction;RNA;2014-09-22
4. A Link between Hinge-Bending Domain Motions and the Temperature Dependence of Catalysis in 3-Isopropylmalate Dehydrogenase;Biophysical Journal;2009-06
5. Metal ion coordination to 2′ functionality of guanosine mediates substrate–guanosine coupling in group I ribozymes: implications for conserved role of metal ions and for variability in RNA folding in ribozyme catalysis;Inorganica Chimica Acta;2004-11
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