Vinay Kumar Nandicoori

Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host.

Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic function.

Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host.

Comparative Proteomic Analyses of Avirulent, Virulent, and Clinical Strains of Mycobacterium tuberculosis Identify Strain-specific Patterns.

Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.

Protein kinase G confers survival advantage to during latency-like conditions.

The transpeptidase PbpA and noncanonical transglycosylase RodA of play important roles in regulating bacterial cell lengths.

Delineating FtsQ-mediated regulation of cell division in .

LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation.

Deletion of Abates Reactivation of Latent Mycobacterium tuberculosis in Mice.

Deletion of serine/threonine-protein kinase pknL from Mycobacterium tuberculosis reduces the efficacy of isoniazid and ethambutol.

Protocol for competition and sequencing of mycobacterium isolated from infected guinea pigs.

The unique N-terminal region of Mycobacterium tuberculosis sigma factor A plays a dominant role in the essential function of this protein.

The heparin-binding hemagglutinin protein of Mycobacterium tuberculosis is a nucleoid-associated protein.