Publikationen

  • Milić D, Dick M, Mulnaes D, Pfleger C, Kinnen A, Gohlke H, Groth G. (2018) Recognition motif and mechanism of ripening inhibitory peptides in plant hormone receptor ETR1. Sci Rep. 2018 March 3; 8:3890. doi: undefined10.1038/s41598-018-21952-3
  • Kessenbrock M, Klein SM, Müller L, Hunsche M, Noga G, Groth G. (2017) Novel Protein-Protein Inhibitor Based Approach to Control Plant Ethylene Responses: Synthetic Peptides for Ripening Control. Front Plant Sci. 2017 Sep 5;8:1528. doi: undefined10.3389/fpls.2017.01528
  • Minges A, Groth G. (2017) Small-molecule inhibition of pyruvate phosphate dikinase targeting the nucleotide binding site. PLoS One. 2017 Jul 10;12(7):e0181139. doi: undefined10.1371/journal.pone.0181139
  • Minges A, Höppner A, Groth G. (2017) undefinedTrapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism. Protein Sci. 2017 May 3. doi: undefined10.1002/pro.3184
  • Minges A, Ciupka D, Winkler C, Höppner A, Gohlke H, Groth G. (2017) Structural intermediates and directionality of the swiveling motion of Pyruvate Phosphate Dikinase.
    Sci Rep. 2017 Mar 30;7:45389. doi: undefined10.1038/srep45389
  • Kessenbrock M, Groth G (2017) Circular Dichroism and Fluorescence Spectroscopy to Study Protein Structure and Protein-Protein Interactions in Ethylene Signaling. Methods Mol Biol. 1573:141-159. doi: undefined10.1007/978-1-4939-6854-1_12
  • Bisson MM, Kessenbrock M, Müller L, Hofmann A, Schmitz F, Cristescu SM, Groth G. (2016) Peptides interfering with protein-protein interactions in the ethylene signaling pathway delay tomato fruit ripening. Sci Rep. 6:30634. doi: undefined10.1038/srep30634
  • Bisson M. M. A. und Groth G. (2015) Targeting Plant Ethylene Responses by Controlling
    Essential Protein-Protein Interactions in the Ethylene Pathway. Mol Plant. 2015
    Apr 3.
  • Paulus, J. K.; Schlieper, D.; Groth, G. (2013) Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution. Nat. Commun. 1518(4): 2041-1723
  • Bisson M. M. A. und Groth G. (2010) New paradigm in ethylene signaling: EIN2, the central regulator of the signaling pathway, interacts directly with the upstream receptors. Article Addendum, Plant Signal & Behav 5(12)
  • Dong C-H., Jang M., Scharein B., Malach A., Rivarola M., Liesch J., Groth G., Hwang I. und Chang C. (2010) Molecular association of the Arabidopsis ETR1 ethylene receptor and a regulator of  ethylene signaling RTE1. JBC epub ahead of print
  • Bisson M. M. A. und Groth G. (2010) New Insight in Ethylene Signaling: AutokinaseActivity of ETR1 Modulates the Interaction ofReceptors and EIN2. Mol Plant 3(5): 882–889
  • Bisson M. M. A., Bleckmann A. ,  Allekotte S. und Groth G. (2009) EIN2, the central regulator of ethylene signalling, is localized at the ER membrane where it interacts with the ethylene receptor ETR1. Biochem. J.  424, 1–6
  • Vollmar M., Schlieper D., Winn M., Büchner C. und Groth G. (2009) Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP Synthase. JBC 284(27): 18228–18235.
  • Meiß E., Konno H., Groth G. und Hisabori T. (2008) Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin. J Biol Chem. 283: 24594-24599.
  • Scharein B., Voet van Vormizeele J., Harter K. und Groth G. (2008) Ethylene signalling: Identification of a putative ETR1-AHP1 phosphorelay complex by fluorescence spectroscopy. Anal Biochem. 377(1):72-6.
  • Voet van Vormizeele J. und Groth G. (2008) Ethylene controls autophosphorylation of the histidine kinase domaine in ethylene receptor ETR1. Mol Plant 1: 380-387.
  • van Lis R., Mendoza-Hernández G., Groth G. und Atteia A. (2007) New insights into the unique structure of the F0F1-ATP synthase from the chlamydomonad algae Polytomella sp. and Chlamydomonas reinhardtii. Plant Physiol. 144(2):1190-9.
  • Lill H., Hisabori T., Groth G. und Bald D. (2004) A thermo-stable enzyme as an experimental platform to study properties of less stable homologues. Protein Engineering, Design and Selection 17: 553‑555.
  • Pavlova P., Shimabukuro K., Hisabori T., Groth G., Lill H. und Bald D. (2004) Complete inhibition and partial re-activation of single F1-ATPase molecules by tentoxin: New properties of the re-activated enzyme. J. Biol. Chem. 279: 9685-9688.
  • Voet van Vormizeele J. und Groth G. (2003) High-level Expression of the Arabidopsis thaliana ethylene receptor protein ETR1 in Escherichia coli and purification of the recombinant protein. Protein Expression and Purification 32(1): 89-94.
  • Schnick C., Koertgen N. und Groth G. (2002) Complete inhibition of the tentoxin resistant F1-ATPase from Escherichia coli by the phytopathogenic inhibitor tentoxin after substitution of critical residues in the alpha- and beta-subunit. J. Biol. Chem. 277: 51003-51007.
  • Groth G., Hisabori T., Lill H. und Bald, D. (2002) Substitution of a single amino acid switches the tentoxin resistant thermophilic ATP synthase into a tentoxin sensitive enzyme. J. Biol. Chem. 277: 20117-20119.  
  • Groth G. (2002) Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin. Proc. Natl. Acad. Sci. USA, 99(6): 3464-3468.
  • Groth G. und Pohl E. (2001) The Structure of the Chloroplast F1-ATPase at 3.2 Å Resolution. J. Biol. Chem. 276: 1345-1352.
  • Groth G., Mills D.A., Christiansen E., Richter M.L. und Huchzermeyer B. (2000) Characterization of a Phosphate Binding Domain on the alpha-subunit of Chloroplast ATP Synthase Using the Photoaffinity Phosphate Analog 4-azido-2-nitro-phenylphosphate. Biochemistry 39: 13781-13787.
  • Schnick C., Forrest L.R., Sansom M.S.P. und Groth G. (2000) Molecular contacts in the transmembrane c-oligomer of F-ATPases identified by Tryptophan substitution mutagenesis. Biochim. Biophys. Acta  1459: 49-60.
  • Groth G. und Schirwitz K. (1999) Rapid purification of membrane extrinsic F1-domain of chloroplast ATP synthase in monodisperse form suitable for 3D-crystallization. Eur. J. Biochem. 260: 15-21.
  • Groth G., Tilg Y. und Schirwitz K. (1998) Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis. J. Mol. Biol. 281: 49-59.
  • Groth G. und Walker J.E. (1997) Model of the c-subunit oligomer in the membrane domain of F‑ATPases. FEBS Letters: 410: 117-123.
  • Häsler K.M., Fritsche O., Groth G. und Junge W. (1996) ATP Synthase: Driven and Activated by Protonmotive Force. Ber. Bunsenges. Phys. Chem. 100: 2024-27.
  • Groth G. und Walker J. E. (1996) ATP synthase from bovine heart mitochondria: reconstitution into unilamellar phosholipid vesicles of the pure enzyme in a functional state. Biochem. J.: 318: 351-357.
  • Groth G. und Junge W. (1995) ATP synthase: activating versus catalytic proton transfer. FEBS Letters 358: 142-144. 
  • Groth G. und Junge W. (1995) ATP Synthase of Chloroplasts: Selective Action of Agents Binding to F1 on partial Reactions of Proton Transfer in F0. Biochemistry 34: 8589-8596.

Reviews 

  • Voet-van-Vormizeele J. und  Groth G. (2008) Mutants, molecules and mechanisms – Deciphering the ethylene signalling network. Curr Top Biochem Res 10(2): 25 - 34
  • Groth G. (2003) Chloroplast F1-ATPase: Structure and Regulation. Recent Research Developments in Biochemistry 4: 903-914.  
  • Groth G. (2000) Molecular models of the structural arrangement of subunits and the mechanism of proton translocation in the membrane domain of F1Fo  ATP synthase. In special issue "The mechanism of F1Fo-ATPase" Biochim. Biophys. Acta  1458: 417-427.
  • Groth G. und Strotmann H. (1999) New results about structure, function and regulation of the chloroplast ATP synthase (CF0CF1). Physiologia Plantarum 106: 142-148.
Verantwortlich für den Inhalt: E-Mail sendenProf. Dr. Georg Groth