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Pradip K Chakraborti

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Biochemical and Biophysical Research Communications|May 18, 2005
The carboxy-terminal end of the peptide deformylase from Mycobacterium tuberculosis is indispensable for its enzymatic activityRahul Saxena, Pradip K Chakraborti
Journal of Bacteriology|November 18, 2005
Identification of regions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosisRahul Saxena, Pradip K Chakraborti
The Journal of Biological Chemistry|October 28, 2006
GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknAMeghna Thakur, Pradip K Chakraborti
Frontiers in Microbiology|February 24, 2016
Eukaryotic-Type Ser/Thr Protein Kinase Mediated Phosphorylation of Mycobacterial Phosphodiesterase Affects its Localization to the Cell WallNeha Malhotra, Pradip K Chakraborti
The Biochemical Journal|June 19, 2008
Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesisMeghna Thakur, Pradip K Chakraborti
The Biochemical Journal|June 26, 2010
Intermolecular phosphotransfer is crucial for efficient catalytic activity of nucleoside diphosphate kinaseHaider Hussain Dar, Pradip K Chakraborti
Biochemical and Biophysical Research Communications|March 27, 2025
Oxidation of active site cysteine leads to inactivation of peptide deformylase from Salmonella entericaSanjay Kumar Rohaun, Pradip K Chakraborti
Biochimica Et Biophysica Acta|June 7, 2005
Nucleotide-induced conformational change in the catalytic subunit of the phosphate-specific transporter from M. tuberculosis: implications for the ATPase structureSankalp Gupta, Pradip K Chakraborti, Dibyendu Sarkar
Plos One|November 24, 2011
Amino acids involved in polyphosphate synthesis and its mobilization are distinct in polyphosphate kinase-1 from Mycobacterium tuberculosisPayal Mittal, Subramanian Karthikeyan, Pradip K Chakraborti
European Journal of Biochemistry|February 22, 2002
Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell divisionRachna Chaba, Manoj Raje, Pradip K Chakraborti
Pageof 3

Showing results (1-10 of 26) with videos related to

Sort By:
Pageof 3
Biochemical and Biophysical Research Communications|May 18, 2005
The carboxy-terminal end of the peptide deformylase from Mycobacterium tuberculosis is indispensable for its enzymatic activityRahul Saxena, Pradip K Chakraborti
Journal of Bacteriology|November 18, 2005
Identification of regions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosisRahul Saxena, Pradip K Chakraborti
The Journal of Biological Chemistry|October 28, 2006
GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknAMeghna Thakur, Pradip K Chakraborti
Frontiers in Microbiology|February 24, 2016
Eukaryotic-Type Ser/Thr Protein Kinase Mediated Phosphorylation of Mycobacterial Phosphodiesterase Affects its Localization to the Cell WallNeha Malhotra, Pradip K Chakraborti
The Biochemical Journal|June 19, 2008
Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesisMeghna Thakur, Pradip K Chakraborti
The Biochemical Journal|June 26, 2010
Intermolecular phosphotransfer is crucial for efficient catalytic activity of nucleoside diphosphate kinaseHaider Hussain Dar, Pradip K Chakraborti
Biochemical and Biophysical Research Communications|March 27, 2025
Oxidation of active site cysteine leads to inactivation of peptide deformylase from Salmonella entericaSanjay Kumar Rohaun, Pradip K Chakraborti
Biochimica Et Biophysica Acta|June 7, 2005
Nucleotide-induced conformational change in the catalytic subunit of the phosphate-specific transporter from M. tuberculosis: implications for the ATPase structureSankalp Gupta, Pradip K Chakraborti, Dibyendu Sarkar
Plos One|November 24, 2011
Amino acids involved in polyphosphate synthesis and its mobilization are distinct in polyphosphate kinase-1 from Mycobacterium tuberculosisPayal Mittal, Subramanian Karthikeyan, Pradip K Chakraborti
European Journal of Biochemistry|February 22, 2002
Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell divisionRachna Chaba, Manoj Raje, Pradip K Chakraborti
Pageof 3