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Derouiche A, Shi L, Kalantari A, et al. Substrate Specificity of the . Front Microbiol. 2016;7:1525doi: 10.3389/fmicb.2016.01525.
Derouiche, A., Shi, L., Kalantari, A., & Mijakovic, I. (2016). Substrate Specificity of the . Frontiers in microbiology, 71525. https://doi.org/10.3389/fmicb.2016.01525
Derouiche, Abderahmane, et al. "Substrate Specificity of the ." Frontiers in microbiology vol. 7 (2016): 1525. doi: https://doi.org/10.3389/fmicb.2016.01525
Derouiche A, Shi L, Kalantari A, Mijakovic I. Substrate Specificity of the . Front Microbiol. 2016 Sep 26;7:1525. doi: 10.3389/fmicb.2016.01525. eCollection 2016. PMID: 27725816; PMCID: PMC5035731.
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Front Microbiol. 2016 Sep 26;7:1525. doi: 10.3389/fmicb.2016.01525. eCollection 2016.

Substrate Specificity of the .

Frontiers in microbiology

Abderahmane Derouiche, Lei Shi, Aida Kalantari, Ivan Mijakovic

Affiliations

  1. Division of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology Gothenburg, Sweden.
  2. Division of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of TechnologyGothenburg, Sweden; Novo Nordisk Foundation Center for Biosustainability, Technical University of DenmarkLyngby, Denmark.

PMID: 27725816 PMCID: PMC5035731 DOI: 10.3389/fmicb.2016.01525

Abstract

Bacterial protein-tyrosine kinases (BY-kinases) are known to regulate different aspects of bacterial physiology, by phosphorylating cellular protein substrates. Physiological cues that trigger BY-kinases activity are largely unexplored. In

Keywords: bacterial protein-tyrosine kinase; kinase activator; kinase specificity; protein phosphorylation; transcription factor

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