Characterization of the phosphorylation sites ofMycobacterium tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH by mass spectrometry

PROTEOMICS ◽  
2006 ◽  
Vol 6 (13) ◽  
pp. 3754-3766 ◽  
Author(s):  
Virginie Molle ◽  
Isabelle Zanella-Cleon ◽  
Jean-Philippe Robin ◽  
Souen Mallejac ◽  
Alain J. Cozzone ◽  
...  
Author(s):  
Li-Rong Yu ◽  
Timothy D. Veenstra

Abstract:: Phosphorylation is arguably the most important post-translational modification that occurs within proteins. Phosphorylation is used as a signal to control numerous physiological activities ranging from gene expression to metabo-lism. Identifying phosphorylation sites within proteins was historically a challenge as it required either radioisotope label-ing or the use of phospho-specific antibodies. The advent of mass spectrometry (MS) has had a major impact on the abil-ity to qualitatively and quantitatively characterize phosphorylated proteins. In this article we describe MS methods for characterizing phosphorylation sites within individual proteins as well as entire proteome samples. The utility of these methods is illustrated in examples that show the information that can be gained using these MS techniques.


PROTEOMICS ◽  
2006 ◽  
Vol 6 (S1) ◽  
pp. S16-S27 ◽  
Author(s):  
Margarita Villar ◽  
Inmaculada Ortega-Pérez ◽  
Felipe Were ◽  
Eva Cano ◽  
Juan Miguel Redondo ◽  
...  

2004 ◽  
Vol 3 (6) ◽  
pp. 1219-1227 ◽  
Author(s):  
Benjamin A. Garcia ◽  
Scott A. Busby ◽  
Cynthia M. Barber ◽  
Jeffrey Shabanowitz ◽  
C. David Allis ◽  
...  

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