Dr. S.M. Malathy Sony, Ph.D

Nanyang Technological University

School of Biological Sciences
60 Nanyang Drive
Singapore 637551

Email: malathy@ntu.edu.sg

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Publications:

  1. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Bhasker Reddy, V., Padmavathi, V, and Fun, H.K. (2002) 9,9-Dimethoxy-7,11-diphenyl-2,4-diazaspiro[5.5]undecane-1,3,5-trione monohydrate. Acta Cryst. C58, 678-680

  2. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Manonmani, J., Kandaswamy, M., and Fun, H.K (2002) Crystal Structure of µ-phenoxo bridged dicopper complex: {N-[(2-hydroxylato-5-methyl) benzyl-(2’-hydroxylato-3’-5’-dimethyl benzyl)] ethyl amine dicopper(II)}. Cryst. Res. Technol. 37, 1360-1367

  3. Sampath, N., Malathy Sony, S.M., Ponnuswamy, M.N., and Nethaji, M. (2003) t-3-Isopropyl-1-methyl-r-2,c-6-diphenylpiperidin-4-one thiosemicarbazone. Acta Cryst. C59, 346-348

  4. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Murali, V., and Rajakumar, P. (2003) Structure and Conformational analysis of a macrocyclic ligand: [24,26-dioxo-3,6,14,17-tetraazapentacyclo(21.0.11,19.13,6.18,12.114,17)hexacosan-1(23),8(25),9,11,19,21-hexaene]. Mol. Cryst. Liq. Cryst. 399, 85-92

  5. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Murali, V., and Rajakumar, P. (2003) Role of weak interactions in the structure of 3-(a,a’-dibromomethyl 1-4 benzotriazole. Mol. Cryst. Liq. Cryst. 403, 15-22

  6. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Manonmani, J., Kandaswamy, M., and Fun, H.K (2003) A Comparative Study on structure and conformation of three hydroxybenzylamine ligands. J. Chem. Cryst. 33, 925-932

  7. Malathy Sony, S.M., Saraboji, K., Ponnuswamy, M.N., Manaonmani, J., Kandasamy, M., and Fun, H.K. (2004) Structure and conformation of a nickel complex: {2-Hydroxo-3-piperidine-1-yl-methyl-N,N'(bis-5-bromobenzylpropylenediimine)nickel(II)perchlorate}. Cryst. Res. Tech. 39, 185-192

  8. Thirumurughan, RA., Malathy Sony, S.M., Shanmugam, G., Jeyakumar, R., and Ponnuswamy, M.N. (2004) Structure and Conformation of N-(t-butoxycarbonyl)-l-isoleucyl-l-leucine methyl ester. Mol. Cryst. Liq. Cryst. 414, 39-48

  9. Malathy Sony, S.M., Charles, P., Ponnuswamy, M.N.,  and Yathirajan, H.S. (2004) 2-2’{(Z)-Ethane-1,2-diylbis[(Z)-o-phenylene-nitrilomethylidyne]}diphenol (EIEP). Acta Cryst. E60, 1078-1080

  10. Sampath, N., Malathy Sony, S.M., Ponnuswamy, M.N., and Nethaji, M. (2004) Crystal structure of 2,6-diphenyl azabicyclo [3.3.1] nonan-9-one Thiosemicarbazone. Cryst. Res. Technol. 39, 821-826

  11. Malathy Sony, S.M., Sukumar, N., Ponnuswamy, M.N., and Jayakumar. R. (2004) Presence of pseudo-peptide bond in the crystal structure of n-(t-butoxycarbonyl)-ε-n'-benzyloxycarbony-l-lysyl-l-isoleucine (boc-lys(obzl)-ile). Cryst. Res. Technol. 39, 368-374

  12. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Manonmani, J., Kandasamy, M., Sivakumar K., and Fun, H.K. (2004) Crystal Structure of a Copper (II) Complex: 4-chloro-3-methyl-6(3’-N,N-dimethylamino-1’-iminomethyl) phenolato copper(II)acetate. Anal. Sci. 20, 85-86

  13. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Padmavathi, V., and Bhaskar Reddy, D. (2004) Crystal Structure of Dimethyl-2,6-diaryl-4-N-methylcyclohexanimine-1,1-dicarboxylate. Anal. Sci. 20, 103-104

  14. Malathy Sony, S.M., Charles, P., Ponnuswamy, M.N., Yathirajan, H.S., and Nethaji, M. (2005) 4’-{[2-(But-2-enyl)-4-chloro-5-formyl-1H-imidazol-1-yl]methyl}biphenyl-2-carbonitrile.  Acta Cryst. E61, 25-26

  15. Malathy Sony, S.M., Charles, P., Ponnuswamy, M.N., and Yathirajan, H.S. (2005) Valdecoxib, a non-steroidal anti-inflammatory drug. Acta Cryst. E61, 108-110

  16. Malathy Sony, S.M., Charles, P., Ponnuswamy, M.N., Yathirajan, H.S., and Nethaji, M. (2005) Ethyl 5-amino-3-methylisoxazole-4-carboxylate. Acta Cryst. E61, 198-200

  17. Malathy Sony, S.M., Palani, K., Charles, P., Ponnuswamy, M.N., Sureshbabu, N., Srinivasan, P.C., and Nethaji, M. (2005) 3-Benzyl-2-methyl-1-phenylsulfonyl-1H-indole. Acta Cryst. E61, 521-523

  18. Malathy Sony, S.M., Palani, K., Charles, P., Ponnuswamy, M.N., Sureshbabu, N., Srinivasan, P. C., and Nethaji, M. (2005) 2-(1-Benzoyl-1-phenylethyl)-3-phenylsulfanyl-1-phenylsulfonyl-1H-indole. Acta Cryst. E61, 578-580

  19. Malathy Sony, S.M., Charles, P., Ponnuswamy, M.N., Yathirajan, H.S., and Nethaji, M. (2005) N-(2-Benzoyl-4-chlorophenyl)-2-chloroacetamide. Acta Cryst. E61, 632-634

  20. Malathy Sony, S.M., Charles. P., Ponnuswamy, M.N., and Nethaji. M. (2005) 2-Methoxy-5-Methylphenyl phenyl ketone. Acta Cryst. E61, 801-803

  21. Narasegowda, R.S., Malathy Sony, S.M., Mondal, S., Nagaraj, B., Yathirajan, H.S., Narasimhamurthy, T., Charles, P., Ponnuswamy, M.N., Nethaji, M., and Rathore, R.S. (2005) 2,2’-Diaminodibenzyl: a rare case of crystallographically non-complant molecular symmetry. Acta Cryst. E61, 843-845

  22. Sukumar, N., Malathy Sony, S.M., Ponnuswamy, M.N., and Jayakumar, R. (2005) Crystal Structure and Conformation of N-(t-Butoxycarbonyl)-L-Isoleucyl-L-Valine methyl ester (Boc-Ile-Val-Ome). Mol. Cryst. Liq. Cryst. 428, 77-85

  23. Malathy Sony, S.M., Saraboji, K., Sukumar, N., and Ponnuswamy, M.N. (2006) Role of amino acid properties to determine backbone t(N-Ca-C˘) stretching angle in peptides and proteins. Biophys. Chem. 120, 24-31

  24. Malathy Sony, S.M., Kuppayee, M., Ponnuswamy, M.N., Manonmani, J., Kandasamy, M., Sivakumar K., and Fun, H.K. (2006) Crystal Structure of a Ternary Mononuclear Copper (II) Complex: 4-Chloro-3-methyl-6[(N-2-picolyl)-1’-iminomethyl]phenolato copper(II)perchlorate. Cryst. Res. Technol. 41, 517-522

  25. Malathy Sony, S.M., and Ponnuswamy, M.N. (2006) Nature of π-Interactions in Nitrogen-Containing Heterocyclic Systems: A Structural Database Analysis. Cryst. Growth Des. 6, 736-742

  26. Ponnuswamy, M.N., Gromiha, M.M., Malathy Sony, S.M., and Saraboji, K. (2006) Conformational Aspects and Interaction Studies of Heterocyclic Drugs. Top. Heterocycl. Chem. 3, 81-147

  27. Malathy Sony, S.M., and Ponnuswamy, M.N. (2006) Geometrical Analysis to Understand the Ability of Halogen Atoms to Act as Hydrogen Bond Acceptors: A Structural Database Study. Bull. Chem. Soc. Jpn. 79, 1766-1772

  28. Malathy Sony, S.M., and Ponnuswamy, M.N. (2007): Molecular basis behind the substrate specificity of Polygalacturonase through computational study. Polymer 48, 910-916

  29. Rishikesan, S., Thaker, R. Y., Priya, R., Gayen, S., Manimekalai, M. S. S., Hunke, C., and Grüber, G. (2008) Spectroscopical identification of residues of subunit G of the yeast V-ATPase in its connection with subunit E. Mol. Mem. Biol. 25, 400-410

  30. Mizutani, H., Saraboji, K., Malathy Sony, S. M., Ponnuswamy, M. N., Kumarevel, T., Krishna Swamy, B. S., Simanshu, D. K., Murthy M. R. N., and Kunishima, N (2008) Systematic study on crystal-contact engineering of diphthine synthase: influence of mutations at crystal-packing regions on X-ray diffraction quality. Acta Cryst. D64, 1020-1033

  31. Kumar, A., Manimekalai, M. S. S., and Grüber, G. (2008) Structure of the nucleotide binding subunit B of the energy producer A1AO ATP synthase in complex with adenosine diphosphate. Acta Cryst. D64, 1110–1115

  32. Kumar, A., Manimekalai, M. S. S., Balakrishna, A. M., Hunke, C., Weigelt, S., Sewald, N. and Grüber, G. (2009) Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A1AO ATP synthase. PROTEINS: Structure, Function and Bioinformatics 75, 807-819

  33. Manimekalai, M S. S., Kumar, A., Balakrishna, A. M., and Grüber, G. (2009) A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1AO ATP synthase. J. Struct. Biol. 166, 39-45

  34. Rishikesan, S., Gayen, S., Thaker, R. Y., Vivekanandan, S., Manimekalai, M. S. S., Yau, Y. H., Greifman Shochat, S. and Grüber, G. (2009) Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G1-59) of the Saccharomyces cerevisiae V1VO ATPase. Biochim. Biophys. Acta-Bioenergetics 1787, 242-25

  35. Kumar, A., Manimekalai, M. S. S., Balakrishna, A. M., Jeyakanthan, J., and Grüber, G. (2010) Nucleotide-binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution. J. Mol. Biol. 396, 301-320

  36. Hunke, C., Tadwal, V. S., Manimekalai, M. S. S., Rössle, M., and Grüber, G. (2010) The effect of NBD-Cl in nucleotide-binding of the major subunit a and B of the motor proteins F1FO ATP synthase and A1AO ATP synthase. J. Bioenerg. Biomembr. 42, 1-10

  37. Grüber, A.1, Manimekalai, M. S. S.1, Balakrishna, A. M., Hunke, C., Jeyakanthan, J., Preiser, P., and Grüber, G. (2010) Structural determination of functional units of the nucleotide binding domain (NBD94) of the reticulocyte binding protein Py235 of Plasmodium yoelii. PLoS ONE 5, 9146-9157

  38. Balakrishna, A. M., Manimekalai, M. S. S,. Hunke, C., Gayen, S., Rössle, M., Jeyakanthan, J., and Grüber, G. (2010) Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering. J. Bioenerg. Biomembr. 42, 311-320

  39. Rishikesan, S., Manimekalai, M. S. S.,  and Grüber, G. (2010) The NMR solution structure of subunit G (G61-101) of the eukaryotic V1VO ATPase Saccharomyces cerevisiae. Biochim. Biophys. Acta-Biomembranes 1798, 1961-1968

  40. Kumar, A.1, Manimekalai, M. S. S.1, Balakrishna, A. M., Priya, R., Biuković, G., Jeyakanthan, J., and Grüber, G. (2010) The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide-binding. J. Mol. Biol. 401, 892-905

  41. Grüber, A., Manimekalai, M. S. S., Preiser, P., and Grüber, G. (2010) Crystallographic studies of the coupling segment NBD94674-781 of the nucleotide binding domain of the Plasmodium yoelii reticulocyte binding protein Py235. Acta. Cryst. F66, 1631-1634

  42. Basak, S., Gayen, S., Thaker, Y. R., Manimekalai, M. S. S., Roessle, M., Hunke, C., and Grüber, G. (2011) Solution structure of subunit F (Vma7p) of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae derived from SAXS and NMR spectroscopy. Biochim. Biophys. Acta-Biomembranes 1808, 360-368

  43. Manimekalai, M. S. S.1, Kumar, A.1, Jeyakanthan, J., and Grüber, G. (2011) The transition-like state and Pi entrance into the catalytic A subunit of the biological engine A-ATP synthase. J. Mol. Biol., 408, 736-754

  44. Grüber, A., Gunalan, K., Ramalingam J. K., Manimekalai, M. S. S., Grüber, G., and Preiser, P. R. (2011) Structural characterization of the Erythrocyte Binding Domain of the Reticulocyte Binding Protein Homologues family of Plasmodium yoelii. Infection and Immunity, 79, 2880-2885

  45. Priya, R., Kumar, A., Manimekalai, M. S. S., and Grüber, G. (2011) Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance. J. Mol. Biol. 413, 657-666

  46. Tadwal, V. S., Manimekalai, M. S. S., and Grüber, G. (2011) Engineered tryptophan in the adenine binding site of catalytic subunit A of the A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady state and time-resolved fluorescence spectroscopy. Acta Cryst. F67, 1485-1491

  47. Grüber, A., Manimekalai, M. S. S., Preiser, P. R., and Grüber, G. (2012) Structural architecture and interplay of the nucleotide- and erythrocyte binding domain of the reticulocyte binding protein Py235 from Plasmodium yoelii. Internat. J. Parasitol. 42, 1083-1089

  48. Basak, S., Balakrishna, A. M., Manimekalai, M. S. S., and Grüber, G. (2012) Crystallization and preliminary X-ray crystallographic analysis of subunit F, F1-94, an essential coupling subunit of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae. Acta Cryst. F68, 1055-1059

  49. Tadwal, V. S., Sundararaman, L., Manimekalai, M. S. S., Hunke, C., and Grüber, G. (2012) Relevance of the conserved histidine and asparagine residues in the phosphate-binding loop of the nucleotide binding subunit B of A1AO ATP synthases. J. Struct. Biol. 180, 509-518

  50. Cs, J. H., Rydstrom, A., Manimekalai, M. S. S., Svanborg, C., and Grüber, G. (2012) Low resolution solution structure of HAMLET and the importance of its alpha-domains in tumoricidal activity. PLoS ONE 7, e53051

  51. Biuković, G., Basak, S., Manimekalai, M. S. S., Rishikesan, S., Roessle, M., Dick, T., Rao, S., Hunke, C., and Grüber, G. (2013) Variations of subunit ɛ of the Mycobacterium tuberculosis F1FO ATP synthase and a novel model for mechanism of action of the TB drug TMC207. Antimicrob. Agents Chemother. 57, 168-176

  52. Priya, R., Biuković, G., Manimekalai, M. S. S., Lim, J., Rao, S. P. S., and Grüber, G. (2013) Solution structure of subunit γ (γ1-204) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ165-178, representing a novel TB drug target. J. Bioenerg. Biomembr. 45, 121-129

  53. Basak, S., Lim, J., Manimekalai, M. S. S., Balakrishna, A. M., and Grüber, G. (2013) Crystal- and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J. Biol. Chem. 288, 11930-11939

  54. Grüber, G., Manimekalai, M. S. S., Mayer, F. and Müller, V. (2014) ATP synthases from archaea: The beauty of a molecular motor. Biochim. Biophys. Acta-Bioenergetics 1837, 940-952

  55. Dip, P. V., Kamariah, N., 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

  56. Wei, L., Jiang, P., Manimekalai, M. S. S., Hunke, C., Grüber, G., Pervushin, K. and Mu, Y. (2015) Extended structure of rat islet amyloid polypeptide in solution. Adv. Exp. Med. Biol., Dongqing Wei et al. (Eds): Advance in Structural Bioinformatics 827, 85-92

  57. Balakrishna, A. M., Basak, S., Manimekalai, M. S. S., and Grüber, G.* (2015) Crystal structure of subunits D and F in complex give insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J. Biol. Chem. 290, 3183-3196

  58. Balakrishna, A. M., Manimekalai, M. S. S., and Grüber, G. (2015) Protein-protein interactions within the ensemble, Eukaryotic V-ATPase, and its concerted interactions with cellular machineries. Progr. Biophys. Mol. Biol. 119, 84-93

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

  60. 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 peroxiridoxin machinery. FEBS J. 282, 4620-4638

  61. Saw, W. G., Tria, G., Grüber, A., Manimekalai, M. S. S., Zhao, Y., Chandramohan, A., Anand, G. S., Matsui, T., Weiss, T., Vasudevan, S. and Grüber, G. (2015) Structural insight and flexibility features of NS5 proteins from all four serotypes of Dengue virus in solution. Acta Crystallogr. D71, 2309-2327

  62. Manimekalai, M.S.S., Saw, W. G., Pan, A., Grüber, A. and Grüber, G. (2016) Identification of the critical linker residues conferring differences in compactness of DENV-4 NS5 from Dengue virus serotypes 1-3. Acta Crystallogr. D72, 795-807

  63. Kumar, A., Balakrishna, A. M.1, Nartey, W.1, Manimekalai, M. S. S., and Grüber, G. (2016) Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol. Free Rad. Biol. Med. 97, 588-601

  64. Saw, W. G.1, Pan, A.1, Manimekalai, M.S.S. and Grüber, G.* (2017) Structural features of Zika virus non-structural proteins 3 and -5 and its individual domains in solution as well as insights into NS3 inhibition. Antiviral Res. 141, 73-90

  65. Pan, A., Saw, W.G., Manimekalai, M.S.S., Grüber, A., Shin, J., Matsui, T., Weiss, T. and Grüber, G.* (2017) Structural features of NS3 of Dengue virus serotypes 2 and 4 in solution and insight into RNA binding and the inhibitory role of quercetin. Acta Crystallogr. D73, 402-419

  66. Kumar, A., Nartey, W., Shin, J., Manimekalai, M. S. S., and Grüber, G. (2017) Structural and mechanistic insights into Mycothiol Disulphide Reductase and the Mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis. Biochim. Biophys. Acta-General Subject 1861, 2354-2366

  67. Ragunathan, P, Sielaff, H., Sundararaman, L., Biuković, G., Manimekalai, M.S.S., Singh, D., Kundu, S., Wohland, T., Frasch, W., Dick, T. and Grüber, G.* (2017) The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation. J. Biol. Chem. 292, 11262-11279

  68. Wong, C.F., Shin, J., Manimekalai, M.S.S., Saw, W.G., Zhan, Y., Bhushan, S. Kumar, A., Ragunathan, P. and Grüber, G.* (2017) The uniqueness of AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C. Sci. Rep. 7, 5159

  69. Singal, B., Balakrishna, A., Nartey, W., Manimekalai, M.S.S., Jeyakanthan, J. and Grüber, G.* (2017) Crystallographic and solution structure of the N-terminal domain of the Rel protein from Mycobacterium tuberculosis. FEBS Letters 591, 2323-2337

  70. Toh, Y.K., Balakrishna, A.M., Manimekalai, M.S.S., Chionh, B.B., Seetharaman, R.R.C., Eisenhaber, B., Eisenhaber, F. and Grüber, G. (2017) Novel insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F. Biochim. Biophys. Acta-General Subject 1861, 3201-3214

  71. Gopal, P., Nartey, W., Ragunathan, P., Sarathy, J., Kaya, F., Yee, M., Setzer, C., Manimekalai, M.S.S., Dartois, V., Grüber, G. and Dick, T. (2017) Pyrazinoic acid inhibits mycobacterial coenzyme A biosynthesis by binding to aspartate decarboxylase PanD. ACS Infect Dis. 2017, 3, 807-819

  72. Hao, C., Gabryelczyk, B., Manimekalai, M.S.S., Grüber, G., Salentinig, S. and Miserez, A. (2017) Self-Coacervation of Modular Squid Beak Proteins – A Comparative Study. Soft Matter 13, 7740-7752

  73. Liu, C., Liew, C.W., Wong, Y.H., Tan, S.T., POH, W., Manimekalai, M.S.S., Rajan, S., Xin, L., Liang, Z.-X., Grüber, G., Rice, S. and Lescar, J. (2018) Insights into biofilm dispersal regulation from the crystal structure of the PAS-GGDEF-EAL region of RbdA from Pseudomonas aeruginosa. J. Bacteriol. 200, e00515-00517

  74. Beldar, S., Manimekalai, M.S.S., Cho, N.J., Baek, K., Grüber, G. and Yoon, H.S. (2018) Self-association and conformational variation of NS5A domain 1 of hepatitis C virus. J. Gen. Virol. 99, 194-208

  75. Kumar, A., Manimekalai, M.S.S., and Grüber, G.* (2018) Substrate-induced structural alterations of Mycobacterial mycothiol disulphide reductase and critical residues involved. FEBS Lett. 592, 568-585

  76. Shin, J., Ragunathan, P., Sundararaman, L., Nartey, W., Kundu, S., Manimekalai, M.S.S., Bogdanović, N., Dick, T. and Grüber, G.* (2018) The NMR solution structure of Mycobacterium tuberculosis F-ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine. FEBS J. 285, 1111-1128

  77. Saw, W.G.1, Pan, A.1, Manimekalai, M.S.S., Grüber, A., and Grüber, G.* (2018) Structure and flexibility of Non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution. Progr. Biophys. Mol. Biol. 143, 67-77

  78. Scherr, N., Bieri, R., Thomas, S., Chauffour, A., Kalia, N.P., Schneide, P., Ruf, M.-T., Lamelas, A., Manimekalai, M.S.S., Grüber, G., Ishii, N., Suzuki, K., Tanner, M., Moraski, G.C. Miller, M.J., Witschel, M., Jarlier, V., Pluschke, G., and Pethe, K. (2018) Targeting the Mycobacterium ulcerans cytochrome bc1:aa3 for the treatment of Buruli ulcer. Nature Commun. 9, 5370

  79. Kannaian B., Sharma, B., Phillips, M., Chowdhury, A., Manimekalai, M.S.S., Adav, S.S., Ng, J.T.Y, Kumar, A., Lim, S., Mu, Y., Sze, S.K., Grüber, G., and Pervushin, K. (2019) Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fibrils. Sci. Rep. 9, 12579

  80. Sorayah, R., Manimekalai, M.S.S., Shin, S.J., Koh, W-J., Grüber, G., and Pethe, K. (2019) Naturally-occurring polymorphisms in QcrB are responsible for resistance to Telacebec in Mycobacterium abscessus. ACS Infect. Dis. 2019, 5, 2055-2060

  81. Chong, S. S. M., Manimekalai, M.S.S., Sarathy, J., Williams, Z., Harold, L., Cook, G.M.C., Dick, T., Pethe, K., Bates, R.W., and Grüber, G.* (2020) Anti-tuberculosis activity of the anti-malaria cytochrome bcc oxidase inhibitor SCR0911. ACS Infect. Dis. 6, 725-737

  82. Sviriaeva, E., Manimekalai, M.S.S., Grüber, G.*, and Kevin, P.* (2020) Features and functional importance of key residues of the Mycobacterium tuberculosis cytochrome bd oxidase. ACS Infect. Dis. 6, 1697-1707

  83. Shin, J., Singal, B., Manimekalai, M.S.S., Chen, M.W., Ragunathan, P., and Grüber, G.* (2020) Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein. FEBS J. 288, 2377-2397

  84. Lee, B.S., Hards, K., Engelhart, C.A., Hasenoehrl, E.J., Kalia, N.P., Mackenzie, J.S., Sviriaeva, E., Chong, S.M.S., Manimekalai, M.S.S., Koh, V.H., Chan, J., Xu, J., Alonso, S., Miller, M.J., Steyn, Grüber, G., Schnappinger, D., Berney, M., Cook, G.M., Moraski, G.C., and Pethe, K. (2021) Dual inhibition of the terminal oxidases eradicates antibiotic-tolerant Mycobacterium tuberculosis. EMBO Mol. Med., e13207

  85. Ragunathan, P., Cole, M., Latka, C., Aragaw, W.W., Hegde, P., Shin, J., Manimekalai, M.S.S., Rishikesan, S., Aldrich, C., Dick, T., and Grüber, G.* (2021) Mycobacterium tuberculosis PanD structure-function analysis and identification of a potent pyrazinoic acid-derived enzyme inhibitor. ACS Chem. Biol.16, 1030-1039

1 (Authors have equal contribution)

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last update 10-Feb-2022