Ravishankar Ramachandran

Affiliations: 
Max Planck Institute of Biochemistry, Martinsried 
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"Ravishankar Ramachandran"
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Publications

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Afsar M, Shukla A, Kumar N, et al. (2021) Salt bridges at the subdomain interfaces of the adenylation domain and active-site residues of Mycobacterium tuberculosis NAD-dependent DNA ligase A (MtbLigA) are important for the initial steps of nick-sealing activity. Acta Crystallographica. Section D, Structural Biology. 77: 776-789
Shukla A, Afsar M, Kumar N, et al. (2020) Structure based identification of first-in-class fragment inhibitors that target the NMN pocket of M. tuberculosis NAD-dependent DNA Ligase A. Journal of Structural Biology. 107655
Anas M, Shukla A, Tripathi A, et al. (2020) Structural-functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding. The Biochemical Journal
Jaiswal S, Chatterjee A, Pandey S, et al. (2018) Mycobacterial Protein tyrosine kinase A phosphorylates PtpA at Tyrosine residues and the mechanism is stalled by the novel series of inhibitors. Journal of Drug Targeting. 1-26
Lata K, Afsar M, Ramachandran R. (2017) Biochemical characterization and novel inhibitor identification of Mycobacterium tuberculosis Endonuclease VIII 2 (Rv3297). Biochemistry and Biophysics Reports. 12: 20-28
Gaur A, Sharma VK, Shree S, et al. (2017) Characterization of EccA3, a CbbX family ATPase from the ESX-3 secretion pathway of M. tuberculosis. Biochimica Et Biophysica Acta
Dey A, Shree S, Pandey SK, et al. (2016) Crystal Structure of Mycobacterium tuberculosis H37Rv AldR (rv2779c), a regulator of the ald gene: DNA-binding, and identification of small-molecule inhibitors. The Journal of Biological Chemistry
Khanam T, Rai N, Ramachandran R. (2015) Mycobacterium tuberculosis class II AP-endonuclease/3'-5' exonuclease III (XthA) exhibits DNA regulated modes of interaction with the sliding DNA β-clamp. Molecular Microbiology
Tripathi SM, Agarwal A, Ramachandran R. (2015) Mutational analysis of Mycobacterium tuberculosis lysine ɛ-aminotransferase and inhibitor co-crystal structures, reveals distinct binding modes. Biochemical and Biophysical Research Communications. 463: 154-60
Khanam T, Shukla A, Rai N, et al. (2015) Critical determinants for substrate recognition and catalysis in the M. tuberculosis class II AP-endonuclease/3'-5' exonuclease III. Biochimica Et Biophysica Acta. 1854: 505-16
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