Publications

Grüber, G.*, Godovac-Zimmermann, J., and Nawroth, T. (1994) ATP-synthesis and -hydolysis of the ATP-synthase from Micrococcus luteus regulated by an inhibitor subunit and membrane energization. Biochim. Biophys. Acta 1186, 43-51

Grüber, G.*, Engelbrecht, S., Junge, W., Dose, K., and Nawroth, T. (1994) Purification and characterization of the inhibitory subunit δ of the ATP-synthase from Micrococcus luteus. FEBS Lett. 356, 226-228

Grüber, G., and Capaldi, R.A. (1996) Differentiation of catalytic sites on Escherichia coli F1 ATPase by laser photoactivated labeling with [3H] 2- azido-ATP using the mutant β3Glu381Cys:εSer108Cys to identify different β subunits by their interactions. Biochemistry 35, 3875-3879

Grüber, G., and Capaldi, R.A. (1996) The Trapping of Different Conformations of the Escherichia coli F1 ATPase by Disulfide Bond Formation: Effect on nucleotide binding affinities on the catalytic sites. J. Biol. Chem. 271, 32623-32628

Capaldi, R.A., Aggeler, R., Wilkens, S., and Grüber, G. (1996) Structural Changes in the γ and ε Subunits of the Escherichia coli F1FO-type ATPase During Energy Coupling. J. Bioenerg. Biomembr. 28, 397-401

Grüber, G., Hausrath, A., Sagermann, M. and Capaldi, R.A. (1997) An improved purification of ECF1 and ECF1FO by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes. FEBS Lett. 410, 165-168

Aggeler, R., Grüber, G., and Capaldi, R.A. (1998) Trapping of conformations of the Escherichia coli F1 ATPase by disulfide bond formation. A state of the enzyme with all three catalytic sites open and with equal low affinity for nucleotides. FEBS Lett. 426, 37-40

Svergun, D.I., Aldag, I., Sieck, T., Altendorf, K., Koch, M.H.J., Kane, D., Kozin, M.B., and Grüber, G.* (1998) A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the δ subunit during ATP hydrolysis. Biophys. J. 75,  2212-2219

Svergun, D.I., Konrad, S., Huß, M., Koch, M.H.J., Wieczorek, H., Altendorf, K., Volkov, V.V., and Grüber, G.* (1998) Quaternary structure of V1- and F1 ATPase: significance of structural homologies and diversities. Biochemistry 37, 17659-17663

Rademacher, M., Ruiz, T., Harvey, W.R., Wieczorek, H., and Grüber, G.* (1999) Molecular Architecture of Manduca sexta midgut V1 ATPase visualized by electron microscopy. FEBS Lett. 453, 383-386

Wieczorek, H., Grüber, G., Harvey, W.R., Huss, M., and Merzendorfer, H.  (1999) The plasma membrane H+ V-ATPase from tobacco hornworm midgut. J. Bioenerg. Biomembr. 31, 67-74

Hausrath, A.C., Grüber, G., Matthews, B.W., and Capaldi, R.A. (1999) Structural Features of the γ Subunit of the Escherichia coli F1 ATPase Revealed by a 4.4 Å Resolution Map Obtained by X-ray Crystallography. Proc. Natl. Acad. Sci. USA 96,  13697-13702 

Grüber, G.*, Rademacher, M., Ruiz, T., Godovac-Zimmermann, J., Canas, B., Kleine-Kohlbrecher, D., Huss, M., Harvey, W.R., and Wieczorek, H. (2000) Three-dimensional structure and subunit topology of the V1 ATPase from Manduca sexta midgut. Biochemistry 39, 8609-8616

Grüber, G.*, Svergun, D.I., Godovac-Zimmermann, J., Harvey, W.R., Wieczorek, H., and Koch, M.H.J. (2000) Evidence for major structural changes in the Manduca sexta midgut V1 ATPase due to redox-modulation: A small-angle X-ray scattering study. J. Biol. Chem. 275, 30082-30087

Wieczorek, H., Grüber, G., Harvey, W. R., Huss, M., Merzendorfer, H., and Zeiske, W. (2000) Structure and Regulation of Insect Plasma Membrane H+ V-ATPase. J. Exp. Biol. 203, 137-135

Svergun, D.I., Becirević, A., Schrempf, H., Koch, M.H.J., and Grüber, G.* (2000) Solution structure and conformational changes of the Streptomyces Chitin-Binding Protein (CHB1). Biochemistry 39, 10677-10683

Grüber, G.* (2000) Structural and Functional Features of the Escherichia coli F1 ATPase. J. Bioenerg. Biomembr. 32, 341-346

Grüber, G.*, Svergun, D., Coskun, Ü., Lemker, T., Koch, M. H. J., Schägger, H., and Müller V. (2001) Structural Insights into the A1 ATPase from the Archeon, Methanosarcina mazei Gö1. Biochemistry 40, 1890-1896

Radermacher, M., Ruiz, T., Wieczorek, H., and Grüber, G. (2001) Three-Dimensional Electron Microscopy Reveals The Structure of The V1-ATPase. J. Struct. Biol. 135, 26–37

Schäfer, H.-J., Coskun, Ü., Eger, O., Godovac-Zimmermann, J., Wieczorek, H., Kagawa, Y., and Grüber, G.* (2001) 8-N3-3'-biotinyl-ATP, a novel monofunctional reagent: Differences of the F1 and V1-ATPases by means of the ATP analogue. Biochem. Biophys. Res. Comm. 286, 1218-1227

Grüber, G.*, Wieczorek, H., Harvey, W.R., and Müller, V. (2001) Structure-Function Relationships of A-, F- and V-ATPases. J. Exp. Biol. 204, 2597-2605

Coskun, Ü., Grüber, G.*, Koch, M.H.J., Godovac-Zimmermann, J., Lemker, T., and Müller, V. (2002) Crosstalk in the A1-ATPase from Methanosarcina mazei Gö1 due to nucleotide-binding. J. Biol. Chem. 277, 17327-17333

Grüber, G.*, Godovac-Zimmermann, J., Link, T.A., Coskun, Ü., Rizzo, V.F., Betz, C., and Bailer, S.M. (2002) Expression, purification and characterization of subunit E, an essential subunit of the vacuolar ATPase. Biochem. Biophys. Res. Comm. 298, 383-391

Rizzo, V.F., Coskun, Ü., Radermacher, M., Ruiz, T., Armbrüster, A., and Grüber, G.* (2003) Resolution of the V1 ATPase from Manduca sexta into subcomplexes and visualization of an ATPase active A3B3EG-complex by electron microscopy. J. Biol. Chem. 278, 270-275

Müller, V.*, and Grüber, G.* (2003) ATP synthases: structure function and evolution of unique secondary energy converters. Cell Mol. Life Sci., 60, 474-494

Lemker, T., Grüber, G., Schmidt, R., and Müller, V. (2003) Defined subcomplexes of the A1 ATPase from the archaeon Methanosarcina mazei Gö1: biochemical properties and redox regulation. FEBS Lett. 544, 206-209

Armbrüster, A., Bailer, S. M., Koch, M. H. J., Godovac-Zimmermann, J., and Grüber, G.* (2003) Dimer Formation of subunit G of the Yeast V-ATPase. FEBS Lett. 546, 395-400

Grüber, G.* (2003) Frontiers in Vacuolar ATPase Research. In: Minireview Series: V‑type ATPase: News and Views of a Marvelous Ion Pump (G. Grüber, Series Editor). J.  Bioenerg. Biomembr. 35, 277-280

Coskun, Ü., Rizzo, V. F., Koch, M. H. J., and Grüber, G.* (2004) Ligand-dependent structural changes in the V1 ATPase from Manduca sexta. J. Bioenerg. Biomembr. 36, 249-256

Coskun, Ü., Radermacher, M., Müller, V., Ruiz, T., and Grüber, G.* (2004) Three-dimensional organization of the archaeal A1 ATPase from Methanosarcina mazei Gö1. J. Biol. Chem. 279, 22759-22764

Armbrüster, A., Svergun, D. I., Coskun, Ü., Juliano, S., Bailer, S., and Grüber, G.* (2004) Structural analysis of the stalk subunit Vma5p of the Yeast V-ATPase in solution. FEBS Lett. 570, 119-125

Coskun, Ü., Chaban, Y.L., Lingl, A., Müller, V., Keegstra, W., Boekema, E.J., and Grüber G.* (2004) Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon methanococcus jannaschii visualized by electron microscopy. J. Biol.Chem. 279, 38644-38648

Chaban, Y.L., Coskun, Ü., Keegstra, W., Oostergetel, G.T., Boekema, E.J., and Grüber G.* (2004) Structural characterization of an ATPase active F1-/V1-ATPase (α3/β3/E/G) hybrid complex. J. Biol.Chem. 279, 47866-47870

Grüber, G.* (2005) Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1VO ATPases. Biochem. Soc. Trans. 33, 883-885

Chaban, Y. L. Juliano, S., Boekema E. J., and Grüber G.* (2005) Interaction between subunit C (Vma5p) of the yeast vacuolar ATPase and the stalk of the C-depleted V1 ATPase from Manduca sexta midgut. Biochim. Biophys. Acta-Bioenergetics 1708, 106-200

Müller, V., Lemker, T., Lingl, A., Weidner, C. Coskun, Ü., and Grüber, G.* (2005) Bioenergetics of archaea: ATP synthesis under harsh environmental conditions. J. Mol. Microbiol. Biotechnol. 10, 167-180

Armbrüster, A., Hohn, C., Hermesdorf, A., Schumacher, K., Börsch, M., and Grüber G.* (2005) Evidence for Major Structural Changes in subunit C of the vacuolar ATPase due to Nucleotide binding. FEBS Lett. 597, 1961-1977

Hong-Hermesdorf, A., Brux, A., Grüber, A., Grüber, G., and Schumacher, K. (2006) A WNK kinase binds and phosphorylates V-ATPase subunit C. FEBS Lett. 580, 932-939

Schäfer, I., Bailer, S. M., Düser, M. G., Börsch, M., Ricardo, A. B., Stock, D., and Grüber, G.* (2006) Crystal structure of the archaeal A1AO ATPsynthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1AO subunits A and B. J. Mol. Biol. 358, 725-740

Schäfer, I., Rössle, M., Biuković, G., Müller, V., and Grüber, G.* (2006) Structural and functional analysis of the coupling subunit F in solution and topological arrangement of the stalk domains of the methanogenic A1AO ATPsynthase. J. Bioenerg. Biomembr. 38, 83-92

Biuković, G., Rössle, M., Gayen, S., Mu, Y., and Grüber, G.* (2007) Small-angle X-ray scattering reveals the solution structure of the peripheral stalk subunit H of the A1AO ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit. Biochemistry 46, 2070-2078

Hunke, C., Chen, W.-Y., Schäfer, H.-J., and Grüber, G.* (2007) Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the catalytic V1VO ATPase from Aedes albopictus. Prot. Expr. Purif. 53, 378-383

Gayen, S., Vivekanandan, S., Biuković, G., Grüber, G.*, and Yoon, H. S. (2007) Backbone 1H, 13C, and 15N resonance assignments of subunit F of the A1AO ATP synthase from Methanosarcina mazei Gö1. Biomol. NMR Assign. 1, 23-25

Thaker, Y. R., Rössle, M., and Grüber, G.* (2007) The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. J. Bioenerg. Biomembr. 39, 275-289

Gayen, S., Vivekanandan, S., Biuković, G., Grüber, G.*, and Yoon, H. S. (2007) The NMR solution structure of subunit F of the methanogenic A1AO ATP synthase and its interaction with the nucleotide-binding subunit B. Biochemistry 46, 11684-11694

 Luo, D. H., Xu, T., Hunke, C., Grüber, G., Vasudevan, S. G., and Lescar, J. (2008)  Crystal structure of the NS3 protease-helicase from Dengue virus. J. Virol. 82, 173-183

Gayen, S., Balakrishna, A. M., Biuković, G., Yulei, W., Hunke, C., and Grüber, G.* (2008) Identification of critical residues of subunit H in its interaction with subunit E of the A-ATP synthase from Methanocaldococcus jannaschii. FEBS J., 1803-1812

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

 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

Grüber, G.* and Marshansky, V. (2008) New insights into structure-function relationships between archeal ATP synthase (A1AO) and vacuolar type ATPase (V1VO). BioEssays 30, 1096-1109

Priya, R., Tadwal, V. S., Rössle, M., Gayen, S., Hunke, C., Peng, W. C., Torres, J., and Grüber, G.* (2008) Low resolution structure of subunit b (b22-156) of Escherichia coli F1FO ATP synthase in solution and the b-d assembly. J. Bioenerg. Biomembr., 40, 245-255

Ramalingam, J. K., Hunke, C., Gao, X., Grüber, G.*, and Preiser, P.R. (2008) ATP/ADP-binding to a novel nucleotide binding domain of the reticulocyte binding protein Py235 of Plasmodium yoelii. J. Biol. Chem. 283, 36389-36396

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

Manimekalai, M. S. S., Kumar, A., Balakrishna, A., 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

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, 242-251

Thaker, R. Y., Hunke, C., Yau, Y. H., Greifman Shochat, S., Ying, L., and Grüber, G.* (2009) Association of the eukaryotic V1VO ATPase subunits a with d and d with A. FEBS Lett. 583, 1090-1095

Biuković, G., Gayen, S., Pervushin, K., and Grüber, G.* (2009) The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47. Biophys. J. 97, 286-294

Gayen, S., Balakrishna, A. M., and Grüber, G.* (2009) NMR solution structure of the N–terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii. J. Bioenerg. Biomembr. 41, 343-348

Priya, R., Biuković, G., Gayen, S., Vivekanandan, S., and Grüber, G.* (2009) Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase. J. Bacteriology 191, 7538-7544

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

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

Gayen, S., and Grüber, G.* (2010) Disulfide linkage in the coiled-coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H85-104. FEBS Lett. 584, 713-718

Balakrishna, A. M., Hunke, C., and Grüber, G.* (2010) Purification and crystallization of the entire recombinant subunit E of the energy producer A1AO ATP synthase. Acta. Cryst. F66, 324-326

Grüber, A., Manimekalai, M. S. S., 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

Merkulova, M. Bakulina, A., Thaker, Y. R., Grüber, G., and Marshansky, V. (2010) Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO. Biochim. Biophys. Acta-Bioenergetics 1797, 1398-1409

Raghunathan D., Gayen, S., Grüber, G.*, and Verma, C. (2010) Crosstalk along the stalk: Dynamics of the interaction of subunits B and F in the ATP synthase of Methanosarcina mazei Gö1. Biochemistry 49, 4181-90

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

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

Kumar, A., Manimekalai, M. S. S., 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

Merkulova, M., McKee, M., Dip, P. V., Grüber, G., and Marshansky, M. (2010) N-terminal domain of the V-ATPase a2-subunit displays integral membrane protein properties. Protein Science 19, 1850-1862

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

Toh, Y. K, Kamariah, N., 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

Rose, I., Biuković, G., Aderhold, P., Müller, V., Grüber, G.*, and Averhoff, B. (2011) Identification and characterization of a unique, zinc-containing transport ATPase essential for natural transformation in Thermus thermophilus HB27. Extremophiles 15, 191-202

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

Rishikesan, S., Thaker, Y. R., and Grüber, G.* (2011) NMR Solution Structure of Subunit E (fragment E1-69) of the Saccharomyces cerevisiae V1VO ATP. J. Bioenerg. Biomembr., 43, 187-193

Basak, S., Gayen, S., Ramalingam, J., Grüber, A., Preiser, R. P., and Grüber, G.* (2011) NMR solution structure of NBD94483-502 of the nucleotide binding domain of the Plasmodium yoelii reticulocyte binding protein Py235. FEMS Microbiol. Letters, 318, 152-158

Manimekalai, M. S. S., Kumar, A., 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

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

Hunke, C., Antosch, M., Müller, V., and Grüber, G.* (2011) Binding of subunit E into the A-B interface of the A1AO ATP synthase. Biochim. Biophys. Acta-Biomembranes, 1808, 2111–2118

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

Rishikesan, S., and Grüber, G.* (2011) Structural elements of the C-terminal domain of subunit E (E133-222) from the Saccharomyces cerevisiae V1VO ATPase determined by solution NMR spectroscopy. J. Bioenerg. Biomembr. 43, 447-455

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

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

Raghunathan, D., Gayen, S., Kumar, A., Hunke, C., Grüber, G.*, and Verma, C. (2012) Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A1AO ATP synthase of Methanosarcina mazei Gö1. J. Bioenerg. Biomembr. 44, 213-224

Balakrishna, A. M., Hunke, C., and Grüber, G.* (2012) The structure of subunit E of the Pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk. J. Mol. Biol., 420, 155-163

Dip, P. V., Saw, W. G., Roessle, M., Marshansky, V., and Grüber, G.* (2012) Solution structure of subunit a, a104-363, of the Saccharomyces cerevisiae V-ATPase and the importance of its C-terminus in structure formation. J. Bioenerg. Biomembr. 44, 341-350

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

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

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

Zhang, Q., Hunke, C., Yau, Y. H., Seow, V., Lee, S., Tanner, L. B., Guan, X. L., Wenk, M. R., Fibriansah, G., Chew, P. L., Kukkaro, P., Biuković, G., Shi, P. Y., Shochat, S. G., Grüber, G., Lok, S. M. (2012) The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation. J. Biol. Chem. 287, 40525-40534

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

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

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

Hosokawa, H., Dip, P. V., Merkulova, M., Zhuang, Z., Khatri, A., Jian, X., Keating, S. M., Bueler, S. A., Rubinstein, J. L., Randazzo, P. A., Ausiello, D. A., Grüber, G., and Marshansky, M. (2013) N-terminal part of a-subunit isoforms is involved in signaling between V-ATPase and Cytohesin-2. J. Biol. Chem. 288, 5896-5913

Saw, W. G., Eisenhaber, B., Eisenhaber, F., and Grüber, G.* (2013) Low resolution structure of the soluble domain GPAA1 (yGPAA170-247) of the glycosylphosphatidylinositol transamidase subunit GPAA1 from Saccharomyces cerevisiae. Biosci. Rep. 33, e00033

Alag, R., Balakrishna, A. M., Rajan, S., Qureshi, I., Shin, J., Lescar, J., Grüber, G., and Yoon, H. S. (2013) Structural insights into substrate binding by PvFKBP35, a peptidylprolyl cis-trans isomerase from the human malarial parasite Plasmodium vivax. Eukaryotic Cell 12, 627-634

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

Dutt Konar,A., Vass, E. Hollósi, M., Majer, Z., Grüber, G., Frese,, K., and Sewald, N. (2013) Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid by N-Methyl Alanine in Efrapeptin C. Chem. Biodivers. 10, 942-951

Salzer, R. Herzberg, M., Nies, D., Biuković, G., Grüber, G., Müller, V., and Averhoff, B. (2013) The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content. Extremophiles 17, 697-698

Srinivasaraghavan, K., Nacro, K., Grüber, G., and Verma, C. (2013) Effect of Ser392 Phosphorylation on Structure and Dynamics of PB domain of ARNO protein: A Molecular Simulations study. Biochemistry 52, 7339-7349

Balakrishna, A. M., Seelert, H., Marx, S.-H. Dencher, N.A., and Grüber, G.* (2014) Crystallographic structure of the turbine c-ring from spinach chloroplast F-ATP synthase. Biosci. Rep. 34, e00102

Marshansky, V., Rubinstein, J. and Grüber, G. (2014) Eukaryotic V-ATPase: Novel structural findings and functional insights. Biochim. Biophys. Acta-Bioenergetics 1837, 857-879

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

Eisenhaber, B., Eisenhaber, S., Toh, Y. K, Grüber, G., and Eisenhaber, F. (2014) Transamidase subunit GAA1/GPAA1 is a M28 family metallo- peptide-synthetase that catalyzes the peptide bond formation between the substrate protein's omega-site and the GPI lipid anchor's phosphoethanolamine. Cell Cycle 13, 1912-1917

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

Dip, P. V., Kamariah, N., Nartey, W., Beushausen, C., Kostyuchenko, V. A., Ng, T. S., Lok, S. M., Saw, W. G., Eisenhaber, F., Eisenhaber, B. and Grüber, G.* (2014) Key roles for 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

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

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

Tay, M. Y. F., Saw, W. G., Zhao, Y., Chan, W. K. K., Singh, D, Chong, Y., Forwood, J. K., Ooi, E. E., Grüber, G., Lescar, J., Luo, D., and Vasudevan, S. G. (2015) The C-terminal 50 amino acid residues of Dengue NS3 protein are important for NS3-NS5 interaction and viral replication. J. Biol. Chem. 290, 2379-2394

Ho, J., Sielaff, H., Nadeem, A., Svanborg, C. and Grüber, G.* (2015) The molecular motor F-ATP synthase is targeted by the tumoricidal protein HAMLET. J. Mol. Biol. 427, 1866-1874

Grüber, G.* (2015) The Beauty of a Visualized Peroxo-diiron(III) Intermediate. Structure 23, 805-806

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. Scientific Rep. 5, 10609

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

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

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

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

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

Singh, D., Sielaff, H., Sundararaman, L., Bhushan, S. and Grüber, G.* (2016) The stimulating role of subunit F in ATPase activity inside the A1-complex of the Methanosarcina mazei Gö1 A1AO ATP synthase. Biochim. Biophys. Acta-Bioenergetics 1857, 177-187

Hu, L., Miao, J.* and Grüber, G.* (2016) Disk-Like Nanojets with Steerable Trajectory Using Platinum Nozzle Nanoengines. RSC Advances 6, 3399-3405

Marshansky, M., Futai, M., and Grüber, G. (2016) Eukaryotic V-ATPase and its super complexes: From structure and function to disease and drug targeting. Series “Advances in Biochemistry in Health and Disease”, (Edited by Sajal Chakraborti and Naranjan S. Dhalla) Book: “Regulation of Ca2+-ATPases, V-ATPases and F-ATPases”. Springer, New York, DOI: 10.1007/978-3-319-24780-9_16, pages 301-335

Hotra, A., Suter, M., Biuković, G., Ragunathan, P., Kundu, S., Dick, T. and Grüber G.* (2016) Deletion of a unique loop in the mycobacterial F-ATP synthase γ subunit sheds light in its inhibitory role in ATP hydrolysis driven H+-pumping. FEBS J. 283, 1947-1961

Liu, W., Zhang, J., Fan, J.-S., Tria, G., Grüber, G. and Yang, D. (2016) A new method for determining structure ensemble of multi-domain protein: Application to a RNA binding protein. Biophys. J. 110, 1943-1956

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

Kumar, A., Balakrishna, A. M., Nartey, W., 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

Kundu, S., Biuković, G., Grüber, G. and Dick, T. (2016) Bedaquiline targets the ε subunit of mycobacterial F-ATP synthase. Antimicrob. Agents Chemother. 60, 6977-6979

Sielaff, H., Martins, J. Singh, D., Biuković, G., Grüber, G.*, Frasch, W.* (2016) Power Stroke Angular Velocity Profiles of Archaeal A-ATP synthase versus Thermophilic and Mesophilic F-ATP synthase Molecular Motors. J. Biol, Chem. 291, 25351-35363

Hu, L., Tao, K., Miao, J. and Grüber, G. (2016) Hydrogen-peroxide-fuelled platinum-nickel-SU-8 microrocket with steerable propulsion using eccentric nanoengine. RSC Advances 6, 102513 – 102518

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

Hu, L., Miao, J. and Grüber, G. (2017) Temperature effects on disk-like gold-nickel-platinum nanoswimmer's propulsion fuelled by hydrogen peroxide. Sens. Actuators B Chem. 239, 586-596

Saw, W. G., Pan, A., 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

Singh, D., Sielaff, H., Börsch, M.*, and Grüber, G.* (2017) Dynamics of subunit F in the A3B3DF-complex of Methanosarcina mazei Gӧ1 A-ATP synthase monitored by single-molecule FRET. FEBS Letters 591, 854-862

Zhu, G., Saw, W. G., Nalaparaju, A., Grüber, G. and Lu L. (2017) Coarse-Grained Molecular Modeling of Solution Structure Ensemble of Dengue Virus Non-Structural Protein 5 with Small-Angle X-Ray Scattering Intensity. J. Phys. Chem. B. 121, 2252-2264

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

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

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

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

Kalia, N.P., Hasenoehrl, E.J., Ab Rahman, N.B., Koh, V.H., Ang, M.L., Sajorda, D.R., Hards, K., Grüber, G., Alonso, S., Cook, G.M., Berney, M., and Pethe, K. (2017) Exploiting the synthetic lethality between terminal respiratory oxidases to kill Mycobacterium tuberculosis and clear host infection. Proc. Natl. Acad. Sci. USA 114, 7426-7431

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

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

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

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

Cai, H., 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

Singh, D. and Grüber, G.* (2018) Crystallographic and enzymatic insights into the mechanisms of Mg-ADP inhibition in the A1 complex of the A1AO ATP synthase. J. Struct. Biol. 201, 26-35

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

Pan, A., Balakrishna, A.M., Nartey, W., Kohlmeier, A., Dip, P.V., Bhushan, S., Grüber, G.* (2018) Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C. Free Rad. Biol. Med. 115, 252-265

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

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

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

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

Boon, P.L.S.1, Saw, W.G.1, Lim, X.X.1, Raghuvamsi, P.V., Huber, R.G., Marzinek, J.K., Holdbrook, D.A., Ganesh, S.A., Grüber, G.* and Bone, P.J. (2018) Partial Intrinsic Disorder Governs the Dengue Capsid Protein Conformational Ensemble. ACS Chem Biol. DOI: 10.1021/acschembio.8b00231

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

Sielaff, H., Singh, D., Grüber, G.* and Börsch, M.* (2018) Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase. Proc. SPIE 105007; DOI: 10.1117/12.2286785

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

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

Saw, W.G.1, Pan, A.1, Manimekalai, M.S.S., Grüber, A., and Grüber, G.* (2019) Structure and flexibility of Non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution. Progr. Biophys. Mol. Biol. 143, 67-77

Zhu, G., Pan, A., Grüber, G. and Lu, L. (2019) Conformational States of Zika Virus Non-Structural Protein 3 Determined by Molecular Dynamics Simulations with Small-Angle X-Ray Scattering Data. Progr. Biophys. Mol. Biol. 143, 13-19

Marshansky, V., Hosokawa, H., Merkulova, M., Bakulina, A., Bjargava, A., Tonra, J., Dip, P.V., Thaker, Y.R., and Grüber, G. (2019) Structural model of a2-subunit N-terminus and its binding interface for Arf-GEF CTH2: Implication for regulation of V-ATPase, CTH2 function and rational drug design. Curr. Top. Membr. 83, 77-106

Bogdanović, N., Trifunovic, D., Sielaff, H., Westphal, L., Bhushan, S., Müller, V. and Grüber, G.* (2019) The structural features of Acetobacterium woodii F-ATP synthase reveal the importance of the unique subunit γ-loop in Na+ translocation and ATP synthesis. FEBS J. 286, 1894-1907

Ng, I.H.W., Chan, K., Tan, M.J.A., Gwee, C.P., Smith, K.M., Jeffress, S.J., Saw, W.G., Swarbrick, C.M.D., Watanabe, S., Jans, D., Grüber, G., Forwood, J.K. and Vasudevan, S.G. (2019) Zika virus NS5 forms supramolecular nuclear bodies that sequester importin alpha and modulate the host immune and pro-inflammatory response in neuronal cells. ACS Infect. Dis. 2019, 5, 932-948

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

Saw, W.G., Chan, K., Vasudevan, S.G. and Grüber, G.* (2019) Zika virus non-structural protein 5 residue 681 is critical for dimer formation and enzymatic activity. FEBS Lett. 593, 1272-1291

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

Sarathy, J., Ragunathan, P., Shin, J., Cooper, C., Upton, A., Grüber, G.*, and Dick, T.* (2019) TBAJ-876 retains Bedaquiline’s activity against subunit c and ε of Mycobacterium tuberculosis F-ATP synthase. Antimicrob. Agents Chemother. 63, e01191-19

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

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

 Saw, W.-G.1, Wu, M.-L1, Ragunathan, P.1, Biuković, G, Lau, A.-M., Shin, J., Harikishore, A., Cheung, C.-Y., Hards, K., Sarathy, J., Bates, R. W., Cook, G. M. C., Dick, T.*, and Grüber, G.* (2019) Disrupting coupling within mycobacterial F-ATPsynthase subunit ε causes dysregulated energy production and cell wall biosynthesis. Sci. Rep. 9, 16759

Gopal, P., Grüber, G., Dartois, V., and Dick, T. (2019) Pharmacological and molecular mechanisms behind the sterilizing activity of Pyrazinamide. Trends Pharmacol. Sci. 40, 930-940

Sarathy, J., Grüber, G., and Dick, T. (2019) Re-understanding the mechanisms of action of the anti-mycobacterial drug Bedaquiline. Antibiotics 8, 261

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

Saw, W.-G., Wong, C.F., Dick, T., Grüber, G.* (2020) Overexpression, purification, enzymatic and microscopic characterization of recombinant mycobacterial F-ATP synthase. Biochem. Biophys. Res. Comm. 522, 374-380

Sarathy, J., Ragunathan, P., Cooper, C., Upton, A., Grüber, G.*, and Dick, T.* (2020) TBAJ-876 displays Bedaquiline-like mycobactericidal potency without retaining the parental drug’s uncoupler activity. Antimicrob. Agents Chemother. 64, e01540-19

Harikishore, A., Chong, S. S. M., Ragunathan, P., Bates, R. W., and Grüber, G.* (2020) Targeting the menaquinol binding loop of mycobacterial cytochrome bd oxidase. Mol. Div., doi: 10.1007/s11030-020-10034-0

Grüber, G.* (2020) Introduction: Novel insights into TB research and drug discovery. Prog. Biophys. Mol. Biol. 152, 2-5

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

Gopal, P., Sarathy, J., Yee, Y., Ragunathan, P., Shin, J., Bhushan, S., Zhu, J., Akopian, T., Kandror, O., Lim, T.K., Gengenbacher, M., Lin, Q., Rubin, E.J., Grüber, G., and Dick, T. (2020) Pyrazinamide triggers degradation of its target aspartate decarboxylase. Nature Commun. 11, 1661

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

Hotra, A., Ragunathan P., Ng, P.S., Seankongsuk, P., Harikishore, A., Sarathy, J.P., Saw, W.-G., Lakshmanan, U., Sae-Lao, P., Kalia, N.P., Shin, J., Kalyanasundaram, R., Anbarasu, S., Parthasarathy, K., Pradeep, C.N., Makhija, H., Dröge, P., Poulsen, A., Tan, J.H.L., Pethe, K., Dick, T., Bates, R.W., and Grüber, G.* (2020) Discovery of a novel Mycobacterial F-ATP synthase inhibitor and its potency in combination with diarylquinolines. Angewandte Chemie i.Ed, 132, 13397-13406

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

Chong, S. S. M., Kamariah, N., and Grüber, G.* (2020) Residues of helix ɑ2 are critical for catalytic efficiency of mycobacterial alkylhydroperoxide reductase subunit C. FEBS Lett. 594, 2829-2839

Wong, C.F., and Grüber, G.* (2020) The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity. Antimicrob. Agents and Chemother. 64, e01568-20

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

Wong, C.F., Lau, A.-M., Harikishore, A., Saw, W.-G., Shin J., Ragunathan, P., Bhushan, S., Ngan, S. F. C., Sze, S. K., Bates, R.W., Dick, T., and Grüber, G.* (2021) A systematic assessment of mycobacterial F1-ATPase subunit ε’s role in latent ATPase hydrolysis. FEBS J. 288, 818-836

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

Qiao, Z., Lampugnani, E., Yan, X.-F., Khan, G., Saw, W.G., Hannah, P., Qian, F., Calabria, J. Miao, J., Grüber, G., Persson, S., and Gao, Y.G. (2021) Crystal structure of Arabidopsis CESA3 catalytic domain with UDP-Glucose provides insight into the mechanism of cellulose synthesis. Proc. Natl. Acad. Sci. USA 118, e2024015118

Ragunathan, P., Cole, M., Latka, C., Aragaw, W.W., Hegde, P., Joon, S., 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

Shin, J., Singal, B., Grüber, A., Wong, M.K.D., Ragunathan, P., and Grüber, G.* (2021) Atomic structure of the TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA. FEBS Lett. 595, 3006-3018

Harikishore, A., Wong, C.F., Ragunathan, P., Litty, D., Müller, V., and Grüber, G.* (2021) Targeting mycobacterial F-ATP synthase C-terminal α subunit interaction motif on rotary subunit γ. Antibiotics 10, 1456

Harikishore, A., Saw, W.-G., Ragunathan, P., Litty, D., Dick, T., Müller, V., and Grüber, G.* (2022) Mutational analysis of mycobacterial F-ATP synthase subunit δ leads to a potent δ enzyme inhibitor. ACS Chem. Biol. 17, 529-535

Ragunathan, P., Dick, T., and Grüber, G.* (2022) Anti-Mycobacterium abscessus activity of tuberculosis F-ATP synthase inhibitor GaMF1. Antimicrob. Agents and Chemother. 66, e0001822

Joon, S., Harikishore, A., Wong, C.F., Ragunathan, P., Dick, T., and Grüber, G.* (2022) Atomic solution structure of Mycobacterium abscessus F-ATP synthase subunit ε and identification of Ep1MabF1 as a targeted inhibitor. FEBS J. 289: 6308-6323

Saw, W.-G., Leow, C.Y., Harikishore, A., Shin, J., Cole, M., Aragaw, W.W., Ragunathan, P., Hegde, P., Aldrich, C.C., Dick, T., and Grüber, G.* (2022) Structural and mechanistic insights into Mycobacterium abscessus aspartate decarboxylase PanD and a pyrazinoic acid-derived inhibitor. ACS Infect. Dis. 7, 1324–1335

Krah, A, Grüber, G., and Bond, P.J.B. (2022) Binding properties of the anti-TB drugs bedaquiline and TBAJ-876 to a mycobacterial F-ATP synthase. Curr. Res. Struct. Biol. 4:278-284

Hedge, P.V., Aragaw, W.W., Cole, M.S., Jachak, G., Ragunathan, P., Harikishore, A., Grüber, G.*, Dick, T.*, and Aldrich, C.C.* (2022) Structure activity relationship of pyrazinoic acid analogs as potential antimycobacterial agents. Bioorganic and Med. Chem. 74:117046

Wong, C.F., Saw, W.-G., Basak, S., Sano, M., Ueno, H., Kerk, H. W., Litty, D., Ragunathan, P., Dick, T., Müller, V., Noji, H., and Grüber, G.* (2022) Structural elements involved in ATP hydrolysis inhibition and ATP synthesis of tuberculosis and non-tuberculous mycobacterial F-ATP synthase decipher new targets for inhibitors. Antimicrobe. Agents and Chemother. 66(12):e0105622

Mathiyazakan, V., Wong, C.F., Harikishore, A., Pethe, K.*, and Grüber, G.* (2023) Cryo-EM structure of the Mycobacterium tuberculosis cytochrome bcc:aa3 supercomplex and a novel inhibitor targeting subunit cytochrome cI. Antimicrobe. Agents and Chemother. 9;e0153122

Ahmed, S.M., Ragunathan, P., Shin, J., Peter, S., Schäfer, R., Kries, J.P.V., Grüber, G., and Dröge, P. (2023) FGFR inhibitor PD173074 binds to the C-terminus of oncofetal HMGA2 and modulates DNA-binding and transcriptional activation functions. FEBS Lett. 597, 1977-1988

Wong, C.F., Leow, C.Y., and Grüber, G.* (2023) Cryo-EM structure of the Mycobacterium abscessus F1-ATPase. Biochem. Biophys. Res. Comm. 671, 140-145

Saw, W.G., Minh, K.L.C., Joon, S., Min, J.K.H., Wong, C.F., Ragunathan, P., Müller, V., and Grüber G.* (2023) Atomic insights of an up-and down conformation of the Acinetobacter baumannii F1-ATPase subunit ε and deciphering the residues critical for ATP hydrolysis inhibition and ATP synthesis. FASEB J. 37(7):e23040. doi: 10.1096/fj.202300175RR

Harikishore, A., Mathiyazakan, V., Pethe, K., and Grüber, G.* (2023) Novel targets and inhibitors of the Mycobacterium tuberculosis cytochrome bd oxidase to foster anti-tuberculosis drug discovery. Expert Opin Drug Discov 1-11. doi: 10.1080/17460441.2023.2224553

Ragunathan, P.  Ng, P. S., Singh, S., Poh, W.H., Litty, D., Kalia, N.P., Larsson, S., Harikishore, A., Rice, S.A., Ingham, P.W., Müller, V., Moraski, G., Miller, M.J., Dick, T., Pethe, K., and Grüber, G.* (2023) GaMF1.39's antibiotic efficacy and its enhanced antitubercular activity in combination with Clofazimine, Telacebec, ND-011992 or TBAJ-876. Microbiology Spectrum 11(6):e0228223. doi:10.1128/spectrum.02282-23 

Krah, A., Ragunathan, P., Bond, P.J., and Grüber, G.* (2024) Variations of the Mycobacterium abscessus F-ATP synthase subunit a-c interface alter binding and potency of the anti-TB drug bedaquiline. Biochem. Biophys. Res. Comm. 690:149249. doi: 10.1016/j.bbrc.2023.149249

Ragunathan, P. Sae-Lao, P., Hamela, C., Alcaraz, M., Krah, A. Poh, W.H., Pee, C.J.E., Lim, A.Y.H., Rice, S.A., Pethe, P., Bond, P.J., Dick, T., Kremer, L.*, Bates, R.W.*, and Grüber, G.* (2024) High efficacy of the F-ATP synthase inhibitor TBAJ-5307 against non-tuberculous mycobacteria in vitro and in vivo. J. Biol. Chem. 300(2):105618. doi:10.1016/j.jbc.2023.105618 

Bui, M.H., Hiew, S.H., Saw, W.G., Webster, R.D, Grüber. G., Mu, Y., and Miserez, A. (2024) Barnacle Cement Protein: An Efficient Bioinspired Corrosion Inhibitor. Comm. Mater. 5-11. https://doi.org/10.1038/s43246-024-00445-z

Le, K.C.M., Wong, C.F., Müller, V., and Grüber G.* (2024) Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits γ and ε, unveiling novel compound targets. FASEB J. 38:e70131. doi:10.1096/fj.202401629R

Harikishore, A., Wong, C.F., Ragunathan, P., Joon, S., Dick, T., and Grüber, G.* (2024) Mycobacterial F-ATP synthase: from structures to target sites to inhibitors. (Edited by Krupakar Parthasarathy and Radhakrishnan Manikkam) Book: “Translational Research in Biomedical Sciences: Recent Progress and future prospects”. Springer Nature, doi:10.1007/978-981-97-1777-4.

Harikishore, A.* and Grüber, G.* (2024) Mycobacterium tuberculosis F-ATP Synthase Inhibitors and Targets. Antibiotics 13, 1169. https://doi.org/10.3390/antibiotics13121169.

Ragunathan, P. Sae-Lao, P., Harikishore, A., Daher, D. Roquet-Banères, F., Kremer, L., Bates, R.W., and Grüber, G.* (2025) SQ31f is a potent non-tuberculous mycobacteria antibiotic by targeting specifically the mycobacterial F-ATP Synthase. J. Antimicrob. Chemoth. 80, 270-280. https://doi.org/10.1093/jac/dkae406

Krah, A.*, Grover, V., Fong, T.C., Bond, P.J.*, and Grüber, G.* (2025) Water occupancy in the Acinetobacter baumannii F-ATP synthase c-ring and its implications as a novel inhibitor target. Structure doi.org/10.1016/j.str.2025.01.004.

Mathiyazakan, V., Suvetha S.K., Pok, W.N., Sorayah, R., Pethe, K.* and Grüber, G.* (2025) Whole-Cell Study Unveils Critical Mechanistic Elements, Regulatory Elements, and Inhibitor Targets of the Mycobacterium abscessus Cytochrome bd Oxidase. ACS Infect. Dis. doi.org/10.1021/acsinfecdis.5c00092