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Gerald Brosch, Ph.D., Associate Professor

EMail:gerald.brosch[at]i-med.ac.at

Phone: +43/(0)512/9003-70211

Fax: +43/(0)512-9003-73100

Short curriculum 

Research fields

• Protein methylation in filamentous fungi

DNA of the eukaryotic nucleus is organized by histones, small basic proteins which are subject to reversible, postsynthetic modifications, such as phosphorylation, acetylation and methylation. During the past years it became evident that a complex interplay between these modifications occurring on the histone tails exist which are all involved in gene-specific regulation. Histone methylation is carried out by histone methyltransferases (HMTs) which are classified due to their substrate specificity. Whereas protein arginine methyltransferases (PRMTs) can use arginine residues on H3 and H4 as substrate, SET domain containing HMTs catalyse the methylation of lysines on the same histone molecules. The recent identification and analysis of different HMTs revealed enzymes that stimulate either gene repression or gene activation, depending on the residue being modified and the type of methylation being introduced. The long-term objective of our research is to investigate the functional role of protein methylation in filamentous fungi. We are performing our studies in the model organism A. nidulans since this fungus is not only well suited to study general mechanisms of chromatin regulation, but, in addition allows to explore the significance of chromatin modifications for fungal virulence (e.g. aspergillosis) and secondary metabolism (e.g. production of antibiotics, immunosuppressants, toxins). We have identified three distinct PRMTs which all exhibit histone methyltransferase activity in vitro and in vivo. One of these proteins, termed RmtB, has an exceptional position because it displays both enzymatic and structural properties that are different from other known PRMTs. To study the functional role of PRMTs in A. nidulans we are currently deleting the corresponding PRMT genes by targeted gene replacement and are analysing putative growth defects of rmtA/ rmtB, and rmtC deletion mutants under various growth conditions. These studies will be completed by the generation of double and triple mutant strains and the concomitant investigation of physiological and developmental effects. Finally, the analysis of global gene expression patterns, the study of effects of rmtA, rmtB, and rmtC deletion on the regulation of genes involved in secondary metabolism pathways, and the identification of novel substrate proteins of PRMTs will help to clarify the role of arginine methylation in Aspergillus.

• Synthesis and identification of drugs as inhibitors of histone deacetylases and protein arginine methyltransferases

Current research project

Protein methylation in Aspergillus nidulans: Isolation and identification of novel substrate proteins of a protein arginine methyltransferase specific for filamentous fungi (supported by the Austrian Science Foundation (FWF), Project P21087-B03)

Teaching

From the online catalog of the Innsbruck Medical University (in German): Current lectures

Head of the Bachelor´s and Master's Programme in Molecular Medicine

Publications

1. Hess, L., Moos, V., Lauber, A.A., Reiter, W., Schuster, M., Hartl, N., Lackner, D., Boenke, T., Koren, A., Guzzardo, P.M, Gundacker, B., Riegler, A., Vician, P., Miccolo, C., Leiter, S., Chandrasekharan, M.B., Vcelkova, T., Tanzer. A., Jun, J.Q., Bradner, .J, Brosch, G., Hartl, M., Bock, C., Bürckstümmer, T., Kubicek, S., Chiocca, S., Bhaskara, S., Seiser, C. (2022) A toolbox for class I HDACs reveals isoform specific roles in gene regulation and protein acetylation. PLoS Genet. 18(8).                                         doi: 10.1371/journal.pgen.1010376.
2. Zwergel, C., Di Bello, E., Fioravanti, R., Conte, M., Nebbioso, A., Mazzone, R., Brosch, G., Mercurio, C., Varasi, M., Altucci, L., Valente, S., Mai, A. (2021) Novel Pyridine-Based Hydroxamates and 2'-Aminoanilides as Histone Deacetylase Inhibitors: Biochemical Profile and Anticancer Activity. ChemMedChem. 16(6):989-999.                                                                                                                      doi: 10.1002/cmdc.202000854
3. Bauer, I., Gross S., Merschak, P., Kremser, L., Karahoda, B., Sarikaya Bayram, Ö., Abt, B., Binder, U., Gsaller, F., Lindner, H., Bayram, Ö., Brosch, G. and Graessle, S. (2020) RcLS2F – A Novel Fungal Class 1 KDAC Co-repressor Complex in Aspergillus nidulans. Front. Microbiol. 11:43. doi:10.3389/fmicb.2020.00043
4. Bauer, I., Lechner, L., Pidroni, A., Petrone, A., Merschak, P., Lindner, H., Kremser, L., Graessle, S., Golderer, G., Allipour, S. and Brosch, G. (2019). Type I and II PRMTs regulate catabolic as well as detoxifying processes in Aspergillus nidulans. Fungal Genet and Biol. 129, 86-100. doi: 10.1016/j.fgb.2019.05.006
5. Bauer, I., Pidroni, A., Bayram, Ö., Brosch, G., Graessle, S. (2019). Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay. J. Vis. Exp. 147: e59527. doi:10.3791/59527.
6. Bauer I., Varadarajan D., Pidroni A., Gross S., Vergeiner S., Faber B., Herrmann M., Tribus M., Brosch G., Graessle S. (2016). A class 1 histone deacetylase with potential as an antifungal target. mBio 7(6):e00831-16.
7. Wang, L., Kofler, M., Brosch, G., Melesina, J., Sippl, W., Martinez, E.D., Easmon, J. (2015). 2-Benzazolyl-4-Piperazin-1-Ylsulfonylbenzenecarbohydroxamic Acids as Novel Selective Histone Deacetylase-6 Inhibitors with Antiproliferative Activity. PLoS One 10(12).
8. Schafferer, L., Beckmann, N., Binder, U., Brosch, G., Haas, H (2015). AmcA-a putative mitochondrial ornithine transporter supporting fungal siderophore biosynthesis. Front Microbiol. 6:252.
9. Valente, S., Trisciuoglio, D., De Luca, T., Nebbioso, A., Labella, D., Lenoci, A., Bigogno, C., Dondio, G., Miceli, M., Brosch, G., Del Bufalo, D., Altucci, L., Mai, A. (2014). 1,3,4-oxadiazole-containing histone deacetylase inhibitors: anticancer activities in cancer cells. J Med Chem. 57(14), 6259-65.
10. Hagelkruys, A., Lagger, S., Krahmer, J., Leopoldi, A., Artaker, M., Pusch, O., Zezula, J., Weissmann, S., Xie, Y., Schöfer, C., Schlederer, M., Brosch, G., Matthias, P., Selfridge, J., Lassmann, H., Knoblich, J.A., Seiser, C. (2014). A single allele of Hdac2 but not Hdac1 is sufficient for normal mouse brain development in the absence of its paralog. Development. 141(3), 604-16.
11. Winter, M., Moser, M., Meunier, D., Fischer, C., Machat, G., Mattes, K., Lichtenberger, B., Brunmeir, R., Weissmann, S., Murko, C., Humer, C., Meischel, T., Brosch, G., Matthias, P., Sibilia, M., Seiser, C. (2013). Divergent roles of HDAC1 and HDAC2 in the regulation of epidermal development and tumorigenesis. EMBO Journal, 32(24), 3176-91.
12. Valente S, Tardugno M, Conte M, Cirilli R, Perrone A, Ragno R, Simeoni S, Tramontano A, Massa S, Nebbioso A, Miceli M, Franci G, Brosch G, Altucci L, Mai A. (2011). Novel Cinnamyl Hydroxyamides and 2-Aminoanilides as Histone Deacetylase Inhibitors: Apoptotic Induction and Cytodifferentiation Activity. Chem. Med. Chem., 6(4),698-712.
13. Bauer, I., Graessle, S., Loidl, P., Hohenstein, K., Brosch, G. (2010). Novel insights into the functional role of three protein arginine methyltransferases in Aspergillus nidulans. Fungal Genet Biol. 47(6), 551-561.
14. Castellano, S., Milite, C., Ragno, R., Simeoni, S., Mai, A., Limongelli, V., Novellino, E., Bauer, I., Brosch, G., Spannhoff, A., Cheng, D., Bedford, M.T., Sbardella, G. (2010). Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1). Chem.Med.Chem. 5(3), 398-414.
15. Tribus, M., Bauer, I., Galehr, J., Rieser, G., Brosch, G., Loidl, P., Trojer, P., Haas, H. and Graessle, S. (2010). A novel motif in fungal class 1 histone deacetylases is essential for growth and development of Aspergillus. Molecular Biology of the Cell Vol. 21, 345-353.
16. Mai A, Valente S, Nebbioso A, Simeoni S, Ragno R, Massa S, Brosch G, De Bellis F, Manzo F, Altucci L. (2009). New pyrrole-based histone deacetylase inhibitors: binding mode, enzyme- and cell-based investigations. Int J Biochem Cell Biol. 41(1):235-47.
17. Mai A, Cheng D, Bedford MT, Valente S, Nebbioso A, Perrone A, Brosch G, Sbardella G, De Bellis F, Miceli M, Altucci L. (2008). epigenetic multiple ligands: mixed histone/protein methyltransferase, acetyltransferase, and class III deacetylase (sirtuin) inhibitors. J Med Chem. 51(7):2279-90.
18. Brosch, G., Loidl, P. & Graessle, S. (2008). Histone Modifications and Chromatin Dynamics: A Focus on Filamentous Fungi. FEMS Microbiol. Rev. 32, 409-439.
19. Ragno, R., Simeoni, S., Rotili, D., Caroli, A., Botta, G., Brosch, G., Massa, S., Mai, A. (2008). Class II-selective histone deacetylase inhibitors. Part 2: Alignment-independent GRIND 3-D QSAR, homology and docking studies. Eur. J. Med. Chem. 43, 621-632.
20. Mai A, Valente S, Rotili D, Massa S, Botta G, Brosch G, Miceli M, Nebbioso A, Altucci L. (2007) Novel pyrrole-containing histone deacetylase inhibitors endowed with cytodifferentiation activity. Int. J. Biochem. Cell Biol. 39, 1510-1522.
21. Spannhoff A, Machmur R, Heinke R, Trojer P, Bauer I, Brosch G, Schule R, Hanefeld W, Sippl W, Jung M. (2007). A novel arginine methyltransferase inhibitor with cellular activity. Bioorg. Med. Chem. Lett. 17, 4150-4153.
22. Mai A, Jelicic K, Rotili D, Di Noia A, Alfani E, Valente S, Altucci L, Nebbioso A, Massa S, Galanello R, Brosch G, Migliaccio AR, Migliaccio G. (2007). Identification of two New Synthetic Histone Deacetylase Inhibitors that Modulate Globin Gene Expression in Erythroid Cells from Normal Donors and Thalassemic Patients. Mol. Pharmacol. 72, 1111-1123.
23. Spannhoff, A., Heinke, R., Bauer, I., Trojer, P., Metzger, E., Gust, R., Schuele, R., Brosch, G., Sippl, W. and Jung, M. (2007). Target-based approach to inhibitors of histone arginine methyltransferases. J. Med. Chem. 50, 2319-2325.
24. Mai, A., Rotili, D., Massa, S., Brosch, G., Simonetti, G., Passariello, C., Palamara, A. T. (2007). Discovery of uracil-based histone deacetylase inhibitors able to reduce acquired antifungal resistance and trailing growth in Candida albicans. Bioorg. Med. Chem. Lett. 17,1221-1225.
25. Mai, A., Valente, S., Cheng, D., Perrone, A., Ragno, R., Simeoni, S., Sbardella, G., Brosch, G., Nebbioso, A., Conte, M., Altucci, L., and Bedford, M.T. (2007). Synthesis and Biological Validation of Novel Synthetic Histone/Protein Methyltransferase Inhibitors. Chem. Med. Chem. 2, 987-991.
26. Ragno, R., Simeoni, S., Castellano, S., Vicidomini, C., Mai, A., Caroli, A., Tramontano, A., Bonaccini, C., Trojer, P., Bauer, I., Brosch, G. and Sbardella, G. (2007). Small Molecule Inhibitors of Histone Arginine Methyltransferases: Homology Modeling, Molecular Docking, Binding Mode Analysis and Biological Evaluations. J. Med. Chem. 50, 1241-1253.
27. Mai, A., Massa, S., Valente, S., Simeoni, S., Ragno, R., Bottoni, P., Scatena, R. and Brosch, G. (2006). Aroyl-pyrrolyl hydroxyamides: influence of pyrrole C4-phenylacetyl substitution on histone deacetylase inhibition. Chem. Med. Chem. 1, 225-237.
28. Mai, A., Massa, S., Rotili, D., Simeoni, S., Ragno, R., Botta, G., Nebbioso, A., Miceli, M., Altucci, L.. and Brosch, G. (2006). Synthesis and biological properties of novel, uracil-containing histone deacetylase inhibitors. J. Med. Chem. 49, 6046-6056.
29. Mai, A., Massa, S., Rotili, D., Pezzi, R., Bottoni, P., Scatena, R., Meraner, J. & Brosch, G. (2005). Exploring the connection unit in the HDAC inhibitor pharmacophore model: Novel uracil-based hydroxamates. Bioorg. Med. Chem. Lett. 15, 4656-4661.
30. Mai, A., Massa, S., Pezzi, R., Valente, S., Loidl, P. & Brosch, G. (2005). Synthesis and Biological Evaluation of 2-, 3-, and 4-Acylaminocinnamyl-N-hydroxyamides as Novel Synthetic HDAC Inhibitors. Med. Chem. 1, 245-254.
31. Vietor, I., Kurzbauer, R., Brosch, G., & Huber, L.A. (2005). TIS7 regulation of the beta-catenin / TCF-4 target gene OPN is histone deacetylase dependent. J. Biol. Chem. 280, 39795-39801.
32. Tribus, M., Galehr, J., Trojer, P., Brosch, G., Loidl, P., Marx, F., Haas, H., & Graessle, S. (2005). HdaA, a Major Class 2 Histone Deacetylase of Aspergillus nidulans Affects Growth Under Conditions of Oxidative Stress. Eukaryot. Cell 4, 1736-1745.
33. Mai, A., Massa, S., Pezzi, R., Simeoni, S., Rotili, D., Nebbioso, A., Scognamiglio, A., Altucci, L., Loidl, P., & Brosch, G. (2005). Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J. Med. Chem. 48, 3344-3353.
34. Vance, K.W., Carreira, S., Brosch, G. and Goding, C.R. (2005). Tbx2 is overexpressed and plays an important role in maintaining proliferation and suppression of senescence in melanomas. Cancer Res. 65, 2260-2268.
35. Ragno, R., Mai, A., Massa, S., Cerbara, I., Valente, S., Bottoni, P., Scatena, R., Jesacher, F., Loidl, P. and Brosch, G. (2004). 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a New Class of Synthetic Histone Deacetylase Inhibitors. 3. Discovery of Novel Lead Compounds Through Structure-Based Drug Design and Docking Studies. J. Med. Chem. 47, 1351-1359.
36. Mai, A., Massa, S., Cerbara, I., Valente, S., Ragno, R., Bottoni, P., Scatena, R., Loidl, P. and Brosch, G. (2004). 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 2. Effect of pyrrole-C2 and/or -C4 substitutions on biological activity. J. Med. Chem. 47, 1098-1109.
37. Trojer, P., Dangl, M., Bauer, I., Graessle, S., Loidl, P. and Brosch, G. (2004). Histone methyltransferases in Aspergillus nidulans: evidence for a novel enzyme with a unique substrate specificity. Biochemistry 43, 10834-10843.
38. Mai, A., Massa, S., Pezzi, R., Rotili, D., Loidl, P. and Brosch, G. (2003). Discovery of (aryloxopropenyl)pyrrolyl-hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A. J. Med. Chem. 46, 4826-4829.
39. Trojer, P., Brandtner, E.M., Brosch, G., Loidl, P., Galehr, J., Linzmaier, R., Haas, H., Mair, K., Tribus, M. and Graessle, S. (2003). Histone deacetylases in fungi: novel members new facts. Nucl. Acids Res., 31(14), 3971-3981.
40. Mai, A., Massa, S., Ragno, R., Cerbara, I., Jesacher, F., Loidl, P. and Brosch, G. (2003). 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a New Class of Synthetic Histone Deacetylase Inhibitors. 1. Design, Synthesis, Biological Evaluation, and Binding Mode Studies Performed Through Three Different Docking Procedures.J. Med. Chem., 13;46(4), 512-24.
41. Vietor, I., Vadivelu, S.K., Wick, N., Hoffman, R., Cotten, M., Seiser, C., Fialka, I., Wunderlich, W., Haase, A., Korinkova, G., Brosch, G. and Huber, L.K. (2002). TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells. The EMBO Journal, 21(17): 4621-4631.
42. Baidyaroy, D., Brosch, G., Graessle,S., Trojer, P. and Walton, J.D. (2002) Characterization of inhibitor-resistant histone deacetylase activity in plant-pathogenic fungi. Eukaryotic Cell, 1 (4): 538-547.
43. Wittich, S., Scherf, H., Xie, C., Brosch, G., Loidl, P., Gerhäuser, C. and Jung, M. (2002). Structure-activity relationships on phenylalanine containing inhibitors of histone deacetylase - In-vitro enzyme inhibition, induction of differentiation and inhibition of proliferation in Friend leukemic cells. J. Med. Chem., 45(15): 3296-3309.
44. Mai, A., Massa, S., Ragno, R., Esposito, M., Sbardella, G., Nocca, G., Scatena, R., Jesacher, F., Loidl, P. and Brosch, G. (2002). Binding Mode Analysis of 3-(4-Benzoyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide: A New Synthetic Histone Deacetylase Inhibitor Inducing Histone Hyperacetylation, Growth Inhibition, and Terminal Cell Differentiation. J. Med. Chem., 45(9):1778-1784.
45. Chiocca, S., Kurtev, V., Colombo, R., Boggio, R., Sciurpi, M.T., Brosch, G., Seiser, C., Draetta, G.F., Cotten, M. (2002). Histone deacetylase 1 inactivation by an adenovirus early gene product. Curr. Biol., 12(7), 594-8.
46. Brosch, G., Dangl, M., Graessle, S., Loidl, A., Trojer, P., Brandtner, E.M., Mair, K., Walton, J.D., Baidyaroy, D. and Loidl, P. (2001). An inhibitor-resistant histone deacetylase in the plant pathogenic fungus Cochliobolus carbonum. Biochemistry, 40(43), 12845-12863.
47. Wagner, M., Brosch, G., Zwerschke, W., Seto, E., Loidl, P. and Jansen-Dürr, P., (2001). Histone deacetylases in replicative senescence: Evidence for a senescence-specific form of HDAC-2. FEBS Lett. 499, 101-106.
48. Brosch, G., Baidyaroy, D., Ahn, J., Graessle, S., Wegener, S., Tonukari, N.J., Caballero, O., Loidl, P. and Walton, J.D. (2001). A gene related to yeast HOS2 histone deacetylase affects extracellular depolymerase expression and virulence in a plant pathogenic fungus. Plant Cell, 13(7), 1609-1624.
49. Massa, S., Mai, A., Sbardella, G., Esposito, M., Ragno, R., Loidl, P. and Brosch, G. (2001). 3-(4-Aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors. J. Med. Chem. 44, 2069-2072.
50. Graessle, S., Loidl, P. and Brosch, G. (2001). Histone acetylation: plants and fungi as model systems for the investigation of histone deacetylases. Cell. Mol. Life Sci. 58, 704-720.
51. Dangl, M., Brosch, G., Haas, H., Loidl, P. and Lusser, A. (2001) Comparative analysis of HD2 type histone deacetylases in higher plants.Planta 213, 280-285.
52. Lechner, T., Carrozza, M.J., Yu, Y., Grant, P.A., Eberharter, A., Vannier, D., Brosch, G., Stillmann, D.J., Shore, D., and Workman, J.L. (2000). Sds3 (Suppressor of Defective Silencing 3) is an integral component of the yeast Sin3/Rpd3 HDAC complex and is required for histone deacetylase activity. J. Biol. Chem. 275(52), 40961-6.
53. Hoffmann, K., Brosch, G., Loidl, P., and Jung, M. (2000). First non-radioactive assay for in vitro screening of histone deacetylase inhibitors. Pharmazie 55(8), 601-6.
54. Graessle, S., Dangl, M., Haas, H., Mair, K., Trojer, P., Brandtner, E., Walton, J.D., Loidl, P., and Brosch, G. (2000). Characterization of two putative histone deacetylase genes from Aspergillus nidulans. Biochim. Biophys. Acta, 1492, 120-126.
55. Lechner, T., Lusser, A., Pipal, A., Brosch, G., Loidl, A., Goralik-Schramel, M., Sendra, R., Wegener, S., Walton, J.D., and Loidl, P. (2000). RPD3-Type Histone Deacetylases in Maize Embryos. Biochemistry, 39, 1683-92.
56. Jung, M., Brosch, G., Kolle, D., Scherf, H., Gerhauser, C., and Loidl, P. (1999) Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J. Med. Chem., 42, 4669-79.
57. Doetzlhofer, A., Rotheneder, H., Lagger, G., Koranda, M., Kurtev, V., Brosch, G., Wintersberger, E., and Seiser, C. (1999) Histone deacetylase 1 can repress transcription by binding to Sp1. Mol. Cell. Biol., 19, 5504-11.
58. Koelle, D., Brosch, G., Lechner, T., Pipal, A., Helliger, W., Taplick, J., and Loidl, P. (1999). Different types of maize histone deacetylases are distinguished by a highly complex substrate- and site-specificity. Biochemistry, 25 (21), 6769-73.
59. Hoffmann, K., Brosch, G., and Loidl, P., and Jung, M., (1999). A non-isotopic assay for histone deacetylase activity. Nucl. Acids Res.,27,2057-8.
60. Koelle, D., Brosch, G., Lechner, T., Lusser, A., Loidl, P. (1998). Biochemical methods for analysis of histone deacetylases. Methods, 15(4), 323-31.
61. Bauer, A., Mikulits, W., Lagger, G., Stengl, G., Brosch, G., and Beug, H. (1998). The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors. EMBO J, 17(15), 4291-303.
62. Aravind, L., Koonin, EV., Dangl, M., Lusser, A., Brosch, G., Loidl, A., Haas, H., Loidl, P. (1998). Second Family of Histone Deacetylases. SCIENCE. 280 (5367), 1167.
63. Jung, M., Hoffmann, K., Brosch, G., and Loidl, P. (1997). Analogues of Trichostatin A and Trapoxin B as histone deacetylase inhibitors. Bioorg. Biomed. Chem. Lett. 7 (13), 1655-1658.
64. Lusser, A., Brosch, G., Loidl, A., Haas H., and Loidl, P. (1997). Identification of Maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science, 277, 88-91.
65. Brosch, G., Lusser, A., López-Rodas, G., and Loidl P. (1997). Histone acetyltransferases during the cell cycle and differentiation of Physarum polycephalum. Eur. J. Cell Biol.,74 (1), 102-110.
66. Brosch, G., Lusser, A., Goralik-Schramel, M., and Loidl, P. (1996). Purification and characterization of a high molecular weight histone deacetylase complex (HD2) of maize embryos. Biochemistry, 35, 15907-15915.
67. Brosch, G., Goralik-Schramel, M., and Loidl, P. (1996). Purification of histone deacetylase HD1-A of germinating maize embryos. FEBS Lett., 393, 287-291.
68. Lechner, T., Lusser, A., Brosch, G., Eberharter, A., Goralik-Schramel, M., and Loidl, P. (1996). A comparative study of histone deacetylases of plant, fungal and vertebrate cells. Biochim. Biophys. Acta, 1296, 181-188.
69. Brosch, G., Ransom, R., Lechner, T., Walton, J., and Loidl, P. (1995). Inhibition of maize histone deacetylases by HC toxin, the host-selective toxin of Cochliobolus carbonum. Plant Cell 7 (33), 1941-1950.
70. Loidl, P., Brosch, G., Eberharter, A., and Lechner, T. (1995). Cell cycle dependent association of proteins with the nuclear matrix. Keystone Symposium on "The Nuclear Matrix: Involment in replication, transcription, gene splicing and cellular regulation". Hilton Head Island, South Carolina, April 4-10, 1995. J. Cellul. Biochem. Suppl. 21B, p. 125.
71. Grabher, A., Brosch, G., Sendra, R., Lechner, T., Eberharter, A., Georgieva, E.I., López-Rodas, G., Franco, L., Dietrich, H. and Loidl, P. (1994). Subcellular location of enzymes involved in core histone acetylation. Biochemistry 33, 14887-14895.
72. Georgieva, E., López-Rodas, G., Hittmair, A., Feichtinger, H., Brosch, G., and Loidl, P. (1994). Maize embryo germination: I. Cell cycle analysis. Planta 192, 118-124.
73. Brosch., G. (1994). Charakterisierung und partielle Reinigung von Histonacetyltransferasen und Histondeacetylasen aus niederen Eukaryonten und Pflanzen. (Dissertation am Institut für medizinische Mikrobiologie der Universität Innsbruck).
74. López-Rodas, G., Brosch, G., Georgieva, E.I., Sendra, R., Franco, L. and Loidl, P. (1993). Histone deacetylase - a key enzyme for the binding of regulatory proteins to chromatin. FEBS Lett., 317, 175-180.
75. Brosch, G., Georgieva, E., López-Rodas, G., Lindner, H. and Loidl, P. (1992). Specificity of Zea mays Histone Deacetylase Is Regulated by Phosphorylation. J. Biol. Chem. 267, 20561-20564.
76. Brosch, G., López-Rodas, G., Golderer, G., Lindner, H., Gröbner, P., and Loidl, P. (1992). Histone acetyltransferases and histone deacetylases of Physarum polycephalum. Cell Biol. Int. Rep.16, 1103-1109.
77. López-Rodas, G., Brosch, G., Golderer, G., Lindner, H., Gröbner, P., and Loidl, P. (1992). Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum. FEBS Lett. 296 (1), 82-86.