Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition-Reference-Cited by-同舟云学术

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Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition

Published:2019-07 Issue:15 Volume:431 Page:2700-2717
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Piserchio Andrea,Will Nathan,Giles David H.,Hajredini Fatlum,Dalby Kevin N.,Ghose Ranajeet

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference71 articles.

1. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues;Nairn;Proc. Natl. Acad. Sci. U. S. A.,1985

2. Functional properties of phosphorylated elongation factor 2;Carlberg;Eur. J. Biochem.,1990

3. Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation;Ryazanov;FEBS Lett.,1989

4. Interaction of phosphorylated elongation factor EF-2 with nucleotides and ribosomes;Dumont-Miscopein;FEBS Lett.,1994

5. Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation;Ryazanov;Nature,1988

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5. Structural basis for the calmodulin-mediated activation of eukaryotic elongation factor 2 kinase;Science Advances;2022-07-08

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