Guanosine triphosphate and guanosine diphosphate as conformation-determining molecules. Differential interaction of a fluorescent probe with the guanosine nucleotide complexes of bacterial elongation factor Tu
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00702a017
Cited by 37 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. Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change;Biochemistry;1995-03
2. Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu;Archives of Biochemistry and Biophysics;1989-11
3. A Mutation That Hinders The GTP Induced Aminoacyl-tRNA BINDING of ELONGATION Factor TU;The Guanine — Nucleotide Binding Proteins;1989
4. Fluorescence Investigations on the Elongation Factor Tu System;Fluorescent Biomolecules;1989
5. GTP‐mediated macromolecular interactions: the common features of different systems;The FASEB Journal;1988-05
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