Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases-Reference-Cited by-同舟云学术

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Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

Published:2010-04-05 Issue:16 Volume:107 Page:7521-7526
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Prisic S.,Dankwa S.,Schwartz D.,Chou M. F.,Locasale J. W.,Kang C.-M.,Bemis G.,Church G. M.,Steen H.,Husson R. N.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference29 articles.

1. Ser/Thr/Tyr Protein Phosphorylation in Bacteria – For Long Time Neglected, Now Well Established

2. Eukaryotic-like protein kinases in the prokaryotes and the myxobacterial kinome

3. Mycobacterial Ser/Thr protein kinases and phosphatases: Physiological roles and therapeutic potential

4. The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape

5. Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria

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