Theoretical Modeling of PrkCc, Serine–Threonine Protein Kinase Intracellular Domain, Complexed with ATP Derivatives
Author:
Publisher
Wiley
Subject
Organic Chemistry,Computer Science Applications,Drug Discovery
Reference42 articles.
1. A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium
2. Protein Phosphorylation in Bacteria?Regulation of Gene Expression, Transport Functions, and Metabolic Processes
3. The PrpC Serine-Threonine Phosphatase and PrkC Kinase Have Opposing Physiological Roles in Stationary-Phase Bacillus subtilis Cells
4. Characterization of a membrane-linked Ser/Thr protein kinase inBacillus subtilis, implicated in developmental processes
5. Mass Spectrometry and Site-directed Mutagenesis Identify Several Autophosphorylated Residues Required for the Activity of PrkC, a Ser/Thr Kinase from Bacillus subtilis
Cited by 3 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. Signatures of the ATP-binding pocket as a basis for structural classification of the serine/threonine protein kinases of gram-positive bacteria;Proteins: Structure, Function, and Bioinformatics;2012-02-13
2. ATP and its N6-substituted analogues: parameterization, molecular dynamics simulation and conformational analysis;Journal of Molecular Modeling;2010-07-29
3. Phosphorylation and ATP-binding induced conformational changes in the PrkC, Ser/Thr kinase from B. subtilis;Journal of Computer-Aided Molecular Design;2010-06-19
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