All Stories

  1. Protein Phosphatases of Pathogenic Bacteria: Role in Physiology and Virulence
  2. Expression profiling of lymph nodes in tuberculosis patients reveal inflammatory milieu at site of infection
  3. Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase
  4. ChemInform Abstract: Novel 1,4-Substituted-1,2,3-Triazoles as Antitubercular Agents.
  5. Inside Cover: Novel 1,4-Substituted-1,2,3-Triazoles as Antitubercular Agents (ChemMedChem 5/2015)
  6. Novel 1,4-Substituted-1,2,3-Triazoles as Antitubercular Agents
  7. Identification of Ser/Thr kinase and Forkhead Associated Domains in Mycobacterium ulcerans: Characterization of Novel Association between Protein Kinase Q and MupFHA
  8. clpC operon regulates cell architecture and sporulation in Bacillus anthracis
  9. HupB, a Nucleoid-Associated Protein of Mycobacterium tuberculosis, Is Modified by Serine/Threonine Protein Kinases In Vivo
  10. Regulation of homocysteine metabolism by Mycobacterium tuberculosis S-adenosylhomocysteine hydrolase
  11. Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis
  12. Unveiling the Novel Dual Specificity Protein Kinases inBacillus anthracis
  13. Interaction of Mycobacterium tuberculosis Elongation Factor Tu with GTP Is Regulated by Phosphorylation
  14. Phosphorylation of Mycobacterium tuberculosis Ser/Thr Phosphatase by PknA and PknB
  15. Understanding the Role of PknJ in Mycobacterium tuberculosis: Biochemical Characterization and Identification of Novel Substrate Pyruvate Kinase A
  16. Forkhead-associated Domain-containing Protein Rv0019c and Polyketide-associated Protein PapA5, from Substrates of Serine/Threonine Protein Kinase PknB to Interacting Proteins ofMycobacterium tuberculosis
  17. Faculty of 1000 evaluation for Unveiling the novel dual specificity protein kinases in Bacillus anthracis: Identification of the first prokaryotic dual specificity tyrosine phosphorylation-regulated kinase (DYRK)-like kinase.