Dr. Neelagandan Kamariah, PhD

Institute for Stem Cell Science and Regenerative Medicine

Bangalore, India

Publications:

  1. Kamariah, N., Sathya Moorthy, P., Balasubramanian, M. and Ponnuswamy, M. N. (2007) Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins under unbuffered low-salt conditions. Acta Cryst. F63, 887–889

  2. Sundaresan, S., Charles, P., Kamariah, N. and Ponnuswamy, M. N. (2008) Purification, Crystallization and Preliminary Analysis of Hemoglobin from Rabbit (Oryctolagus cuniculus). Protein Pept. Lett. 15, 318-319

  3. Balasubramanian, M., Sathya Moorthy, P., Kamariah, N.,and Ponnuswamy, M. N. (2009) Preliminary crystallographic study of hemoglobin from buffalo (Bubbalus bubbalis): A low oxygen affinity species. Protein Pept. Lett. 16, 213-215

  4. Sathya Moorthy, P., Kamariah, N., Balasubramanian, M. and Ponnuswamy, M. N. (2009) Purification, crystallization and preliminary X-ray diffraction studies on goat (Capra hircus) hemoglobin – A low oxygen affinity species. Protein Pept. Lett. 16, 454-456

  5. Sathya Moorthy, P., Kamariah, N., Balasubramanian, M. and Ponnuswamy, M. N. (2009) Purification, crystallization and preliminary X-ray diffraction studies on avian hemoglobin from pigeon (Columba livia). Acta Cryst. F65, 120-122

  6. Balasubramanian, M., Sathya Moorthy, P., Kamariah, N. and Ponnuswamy, M. N. (2009) Purification, crystallization and preliminary crystallographic study of low oxygen-affinity hemoglobin from cat (Felis silvestris catus) in two different crystal forms. Acta Cryst. F65, 313-316

  7. Balasubramanian, M., Sathya Moorthy, P., Kamariah, N. and Ponnuswamy, M. N. (2009) Purification, crystallization and preliminary crystallographic study of haemoglobin from camel (Camelus dromedarius): a high oxygen-affinity lowland species. Acta Cryst. F65, 773-775

  8. Toh, Y. K.1, Kamariah, N.1, Maurer-Stroh, S., Roessle, M., Eisenhaber, F., Adhikari, S., Eisenhaber, B and Grüber, G. (2011) Structural insight into the glycosylphosphatidylinositol transamidase subunits PIG-K and PIG-S from yeast. J. Struct. Biol. 173, 271-281

  9. Kamariah, N., Eisenhaber, F., Adhikari, S., Eisenhaber, B., and Grüber, G. (2011) Purification and crystallization of yeast glycosylphosphatidylinositol transamidase subunit PIG-S (PIG-S71-467). Acta. Cryst. F67, 896-899

  10. Kamariah, N., Sathya Moorthy, P., Balasubramanian, M. and Ponnuswamy, M. N. (2014) Structural studies on a low oxygen affinity hemoglobin from mammalian species: sheep (Ovis aries). Biochem. Biophys. Res. Commun. 18, 36-41

  11. Balasubramanian, M., Sathya Moorthy, P., Kamariah, N., Ramadoss, R., Prasanna R., Kolatkar, P.R. and Ponnuswamy, M. N. (2014) Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms. Acta Crystallogr. D70, 1898-906

  12. Dip, P. V.1, Kamariah, N.1, Manimekalai, M. S. S., Nartey, W., Balakrishna, A. M., Eisenhaber, F., Eisenhaber, B., and Grüber, G. (2014) Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli. Acta Crystallogr. D70, 2848-2862

  13. Dip, P. V.1, Kamariah, N.1, Nartey, W.1, Beushausen, C., Kostyuchenko, V. A., Ng, T. S., Lok, S. M., Saw, W. G., Eisenhaber, F., Eisenhaber, B., and Grüber, G. (2014) Key roles of the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress. Biochim. Biophys. Acta 1837, 1932-1943

  14. Rajan, S., Choi, M., Nguyen, Q.T., Ye, H., Liu, W., Toh, H.T., Kang, C.B., Kamariah, N., Li, C., Huang, H., White, C., Baek, K., Grüber, G., and Yoon, H.S. (2015) Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport. Sci. Rep. 5, 10609

  15. Kamariah, N., Manimekalai, M. S., Nartey, W., Eisenhaber, F., Eisenhaber, B., and Grüber, G. (2015) Crystallographic and solution studies of NAD+- and NADH-bound alkyl hydroperoxide reductase subunit F (AhpF) from Escherichia coli provide insight into sequential enzymatic steps. Biochim. Biophys. Acta-Bioenergetics 1847, 1139-1152

  16. Nartey, W., Basak, S., Kamariah, N., Manimekalai, M. S. S., Robson, S., Wagner, G., Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2015) NMR studies reveal a novel grab and release mechanism necessary for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery. FEBS J. 282, 4620-4638

  17. Kamariah, N.1, Nartey, W.1, Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2016) Low resolution solution structure of an enzymatic active AhpC10:AhpF2 ensemble of the Escherichia coli alkyl hydroperoxide reductase. J. Struct. Biol. 193, 13-22

  18. Kamariah, N., Sek M. F., Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2016) Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins. Sci. Rep. 6, 37610

  19. Kamariah, N., Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2017) Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin. J. Biol. Chem. 292, 6667-6679

  20. Kamariah, N., Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2018) Active site CP-loop dynamics modulate substrate binding, catalysis, oligomerization, stability, over-oxidation and recycling of 2-Cys Peroxiredoxins. Free Rad. Biol. Med. 118, 59-70

  21. Kamariah, N., Eisenhaber, B., Eisenhaber, F. and Grüber, G.* (2018) Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions. Sci. Rep. 8, 14151

  22. Bogdanović, N, Sundararaman, L., Kamariah, N., Tyagi, A., Bhushan, S., Ragunathan, P., Shin, J., Dick, T., and Grüber, G.* (2018) Structure and function of Mycobacterium-specific components of F-ATP synthase subunits α and ε. J. Struct. Biol. 280, 420-434

  23. Toh, Y.K., Balakrishna, A., Shin, J., Neelagandan, K., Grüber, A., Eisenhaber, F., Eisenhaber, B. and Grüber, G.* (2019) Effect of the additional cysteine 503 of vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F (AhpF) and the mechanism of AhpF and subunit C assembling. Free Rad. Med. Biol. 138, 10-22

  24. Kamariah, N., Huber, R.G., Nartey, W., Bhushan, S., Bond, P.J. and Grüber, G.* (2019) Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ. J. Struct. Biol. 207, 199-208

  25. Kamariah, N., Ragunathan, P., Shin, J., Saw, W.-G., Wong, C.F., Dick, T., and Grüber, G.* (2020) Unique structural and mechanistic properties of mycobacterial F-ATP synthases: Implications for drug design. Prog. Biophys. Mol. Biol. 152, 64-73

  26. Kamariah, N., Huber, R.G., Bond, P.J., Müller, V., and Grüber, G.* (2020) 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase. Biochim. Biophys. Res. Comm. 527, 518-524

  27. Chong, S. S. M., Kamariah, N., and Grüber, G.* (2020) Critical residues of helix ɑ2 for catalytic efficiency of Mycobacterial Alkylhydroperoxide reductase subunit C. FEBS Lett. 594, 2829-2839

1 (Authors have equal contribution)

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last update 23-Nov-2020