Reconstitution of Bacterial Tyrosine Kinase-Modulator Interaction in a Human Cell Line
Author:
Affiliation:
1. Department of Chemotherapy and Mycoses, National Institute of Infectious Diseases
Publisher
Pharmaceutical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/bpbreports/3/1/3_28/_pdf
Reference22 articles.
1. 1) Grangeasse C, Cozzone AJ, Deutscher J, Mijakovic I. Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem. Sci., 32, 86–94 (2007).
2. 2) Grangeasse C, Nessler S, Mijakovic I. Bacterial tyrosine kinases: evolution, biological function and structural insights. Philos. Trans. R. Soc. Lond. B Biol. Sci., 367, 2640–2655 (2012).
3. 3) Chao JD, Wong D, Av-Gay Y. Microbial protein-tyrosine kinases. J. Biol. Chem., 289, 9463–9472 (2014).
4. 4) Shi L, Ji B, Kolar-Znika L, Boskovic A, Jadeau F, Combet C, Grangeasse C, Franjevic D, Talla E, Mijakovic I. Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates. Genome Biol. Evol., 6, 800–817 (2014).
5. 5) Grangeasse C, Obadia B, Mijakovic I, Deutscher J, Cozzone AJ, Doublet P. Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J. Biol. Chem., 278, 39323–39329 (2003).
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