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Publications

Chen J., Sathiaseelan V., Moore A.D., Tan S., Chilamakuri C.S., Roamio Franklin V.N., Shahsavari A., Jakwerth C.A., Hake S.B., Warren A.J., Mohorianu I., D’Santos C.S. and Ringshausen I. (2021). ZAP-70 constitutively regulates gene expression and protein synthesis in chronic lymphocytic leukemia. Blood, DOI: 10.1182/blood.2020009960

 

Procida T., Friedrich T., Jack A.P.M., Peritore M., Bönisch C., Eberl H.C., Daus N., Kletenkov K., Nist A., Stiewe T., Borggrefe T., Mann M., Bartkuhn M. and Hake S.B. (2021). JAZF1, a novel p400/TIP60/NuA4 complex member, regulates H2A.Z acetylation at regulatory regions. IJMS, 12(22): E678; DOI: 10.3390/ijms22020678

 

Zhang Z., Wang M., Zhang Y., Zhang Y., Bartkuhn M., Markmann M., Hossain H., Chakraborty T., Hake S.B., Jia Z., Meinhardt A. and Bhushan S. (2021). Uropathogenic Escherichia coli virulence factor a hemolysin reduces histone acetylation to inhibit expression of pro-inflammatory cytokine genes. J Infect Dis., DOI: 10.1093/infdis/jiab018

 

Low J.K.K., Silva A.P.G., Sharifi Tabar M., Torrado M., Webb S.R., Parker B.L., Sana M., Smits C., Schmidberger J.W., Brillault L.,     Jackman M.J., Wolliams D.C. Jr., Blobel G.A., Hake S.B., Shepherd N.E., Landsberg M.J., and Mackay J.P. (2020). The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture. Cell Reports, 33(9): 108450; DOI: 10.1016/j.celrep.2020.108450

 

Armache A., Yang S., Martinez de Paz A., Robbins L.E., Durmaz C., Cheong J.Q., Ravishankar A., Daman A.W., Ahimovic D.J., Klevorn T., Yue Y., Arslan T., Lin S., Panchenko T., Hrit J., Wang M., Thudium S., Garcia B.A., Korb E., Armache K.J., Rothbart S.B., Hake S.B., Allis C.D., Li H., and Josefowicz S.Z. (2020) Histone H3.3 phosphorylation amplifies stimulation-induced transcription. Nature, DOI: 10.1038/s41586-020-2533-0

 

Resnick R., Wong C.J., Hamm D.C., Bennett S.R., Skene P.J., Hake S.B., Henikoff S., van der Maarel S.M. and Tapscott S.J. (2019). DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression. Cell Reports, 29(7): 1812-1820

 

Riedlinger T., Bartkuhn M., Zimmermann T., Hake S.B., Nist A., Stiewe T., Kracht M. and Schmitz M.L. (2019). Chemotherapeutic drugs inhibiting Topoisomerase 1 activity impede cytokine-induced and NF-kB p65-regulated gene expression. Cancers, DOI: 10.3390/cancers11060883

 

Giaimo B.D., Ferrante F., Herchenröther A., Hake S.B. and Borggrefe T.. (2019). The histone variant H2A.Z in gene regulation. Epigenetics & Chromatin, DOI:10.1186/s13072-019-0274-9

 

Link S., Spitzer R.M.M., Sana M., Torrado M., Völker-Albert M.C., Keilhauer E.C., Burgold T., Pünzeler S., Low J.K.K., Lindström I., Nist A., Regnard C., Stiewe T., Hendrich B., Imhof A., Mann M., Mackay J.P., Bartkuhn M.* and Hake S.B.* (2018). PWWP2A binds distinct chromatin moieties and interacts with an MTA1-specific core NuRD complex. Nature Commun., DOI: 10.1038/s41467-018-06665-5

 

Link, S. and Hake S.B. (2017). PWWP2A: A novel mitosis link? Cell Cycle, 16(29): 1849-1850

 

Pünzeler S., Link S., Wagner G., Keilhauer E.C., Kronbeck N., Spitzer R.M.M., Leidescher S., Markaki Y., Menthele E., Regnard C., Schneider K., Takahashi D., Kusakabe M., Vardabasso C., Zink L.M., Straub T., Bernstein E., Harata M., Leonhardt H., Mann M., Rupp R. and Hake S.B. (2017) Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest differentiation. The EMBO Journal, 36(15): 2263-2279

 

Zink L.M., Delbarre E., Eberl H.C., Keilhauer E.C., Bönisch C., Pünzeler S., Bartkuhn, M., Collas P., Mann M. and Hake S.B. (2017). H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3-H4 binding and deposition. Nucleic Acids Research, 45(10): 5691-5706

 

Buschbeck M. and Hake S.B. (2017). Variants of core histones and their roles in cell fate decisions, development and cancer. Nature Rev Mol Cell Biol, 18(5): 299-314

 

Zink L.M. and Hake S.B. (2016). Histone variants: Nuclear function and disease. Curr Opin Genet Dev, 37: 82-89

 

Vardabasso C., Hake S.B. and Bernstein E. (2015). Histone variant H2A.Z.2: a novel driver of melanoma progression. Molecular & Cellular Oncology, 3(2): e1073417

 

Vardabasso C., Gaspar-Maia A., Hasson D., Pünzeler S., Valle-Garcia D., Straub T., Keilhauer E.C., Strub T., Panda T., Chung C.Y., Segura M.F., Fontanals-Cirera B., Verma A., Mann M., Hernando E., Hake S.B.* and Bernstein E.* (2015). Histone variant H2A.Z.2 mediates proliferation and drug sensitivity of malignant melanoma. Mol. Cell, 59(1): 75-88 (*: co-corresponding authors)

 

Abendroth C., Hofmeister A., Hake S.B., Kamweru P.K., Miess E., Dornblut C., Küffner I., Deng W., Leonhardt H., Orthaus S., Hoischen C. and Diekmann S. (2015). The CENP-T C-terminus is exclusively proximal to H3.1 and not to H3.2 or H3.3. Int. J. Mol. Sci., 16(3): 5839-5863

 

Leonhardt H. and Hake S.B. (2014). Histone glutamine methylation afFACTing rDNA transcription. Cell Res., 24(3): 261-262

 

Dindar G., Anger A.M., Mehlhorn C., Hake S.B. and Janzen C.J. (2014). Structure-guided mutational analysis reveals the functional requirements for product specificity of DOT1 enzymes. Nature Commun., DOI: 10.1038/ncomms6313

 

Jack A.P. and Hake S.B. (2014). Getting down to the core of histone modifications. Chromosoma, 124(4): 335-371

 

Sansoni V., Casas-Delucchi C.S., Rajan M., Schmidt A., Bönisch C., Thomae A.W., Staege M.S., Hake S.B., Cardoso M.C. and Imhof A. (2014). The histone variant H2A.Bbd is enriched at sites of DNA damage. Nucleic Acids Research, 42(19): 6405-6420

 

Garcia-Gimenez J.L., Olaso G., Hake S.B., Bönisch C., Wiedemann S.M., Markovic J., Dasi F., Gimeno A., Perez-Quilis C., Palacios O., Capdevila M., Vina J. and Pallardo F.V. (2013). Histone H3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure. Antioxid. Redox. Signal, 19(12): 1305-1320

 

Jack A.P., Bussemer S., Hahn M., Pünzeler S., Snyder M., Wells M., Csankovszki G., Solovei I., Schotta G., and Hake S.B. (2013). H3K56me3 is a novel, conserved heterochromatic mark that largely but not completely overlaps with H3K9me3 in both regulation and localization. PLoS ONE, 8(2): e51765

 

Talbert P.B., Ahmad K., Almouzni G., Ausio J., Berger F., Bhalla P.L., Bonner W.M., Cande W.Z., Chadwick B.P., Chan S.W.L., Cross G.A.M., Cui L., Dimitrov S.I., Doenecke D., Eirin-Lopez J.M., Gorovsky M.A., Hake S.B., Hamkalo B.A., Holec S., Jacobsen S.E., Khochbin S., Ladurner A.G., Landsman D., Latham J.A., Loppin B., Malik H.S., Marzluff W.F., Pehrson J.R., Postberg J., Singh M.B., Schneider R., Smith M.M., Thompson E., Torres-Padilla M.E., Tremethick D.J., Turner B.M., Waterborg J.H., Wollmann H., Yelagandula R., Zhu B. and Henikoff S. (2012). A unified phylogeny-based nomenclature for histone variants. Epigenetics & Chromatin, 5: 7

 

Pichler G., Jack A., Wolf P. and Hake S.B. (2012). Versatile Toolbox for High Throughput Biochemical and Functional Studies with Fluorescent Fusion Proteins. PLoS ONE, 7(5): e36967

 

Bönisch C. and Hake S.B. (2012). Histone H2A variants in nucleosomes and chromatin: more or less stable? Nucleic Acids Research, 40(21): 10719-10741

 

Bönisch C., Schneider K., Pünzeler S., Wiedemann S.M., Bielmeier C., Bocola M., Eberl H.C., Kügel W., Neumann, J., Kremmer E., Leonhardt H., Mann M., Michaelis J., Schermelleh L. and Hake S.B. (2012). H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilization. Nucleic Acids Research, 40(13): 5951-5964

 

Ratnakumar K., Duarte L.F., LeRoy G., Hasson, D., Smeets D., Vardabasso C., Bönisch C., Zheng T., Xiang, B., Zhang D.Y., Li H., Wang X., Hake S.B., Schermelleh L., Garcia B.A. and Bernstein E. (2012). ATRX-mediated chromatin association of histone variant macroH2A1 regulates alpha globin expression. Genes & Development, 26(5): 433-438

 

Torrente M.P., Zee B.M., Young N.L., Baliban R.C., Leroy G., Floudas C.A., Hake S.B. and Garcia B.A. 2011. Comprehensive proteomic interrogation of human chromatin. PLoS ONE, 6(9): e24747

 

Müller-Taubenberger A., Bönisch C., Fürbringer M, Wittek F. and Hake S.B. (2011). The histone methyltransferase Dot1 is required for DNA damage repair and proper development in Dictyostelium. Biochem. Biophys. Res. Commun., 404(4): 1016-1022

 

Wiedemann S.M., Mildner S.N., Bönisch C., Israel L., Maiser A., Matheisl S., Straub T., Merk R., Leonhardt H., Kremmer E., Schermelleh L., and Hake S.B. (2010). Identification and characterization of novel primate-specific histone H3 variants H3.X and H3.Y. Journal of Cell Biology, 190(5): 777-791 (Cover-Story mit Highlight Artikel)

 

Basu A., Rose K.L., Zhang J., Beavis R.C., Ueberheide B., Garcia B.A., Chait B., Zhao Y., Hunt D.F., Segal E., Allis C.D. and Hake S.B. (2009). Proteome-wide prediction of acetylation substrates. PNAS, 106(33): 13785-13790

 

Bönisch C., Nieratschker S.M., Orfanos N.K. and Hake S.B. (2008). Chromatin proteomics and epigenetic regulatory circuits. Expert Rev. Proteomics, 5(1): 105-119

 

Shechter D., Dormann H.L., Allis C.D. and Hake S.B. (2007). Extraction, purification and analysis of histones. Nature Prot., 2(6): 1445-1457

 

Mandava V., Fernandez J.P., Deng H., Janzen C.J., Hake S.B. and Cross G.A. (2007). Histone modifications in Trypanosoma brucei. Mol. Biochem. Parasitol., 156(1): 41-50

                                                                                                                                          

Garcia B.A.*, Hake S.B.*, Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra, N., Strahl B.D., Allis C.D. and Hunt D.F. (2007). Organismal differences in post-translational modifications in histones H3 and H4. J. Biol. Chem., 282(19): 7641-7655 (*: geteilte Erstautorenschaft)

 

Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D. and Strahl B.D. (2007). Identification of histone H3 lysine 36 acetylation as a highly conserved modification. J. Bio. Chem., 282(19): 7632-7640

 

Bernstein E. and Hake S.B. (2006). The nucleosome: a little variation goes a long way. Biochem. Cell Biol., 84(4): 495-507

 

Janzen C.J., Hake S.B., Lowell J.E. and Cross G.A.M. (2006). Selective di- or trimethylation of histone H3 lysine 76 by two DOT1 homologs is important for cell cycle regulation in Trypanosoma brucei. Mol. Cell, 23(4): 497-507

 

Janzen C.J., Fernandez J.P., Deng H., Diaz R., Hake S.B., and Cross G.A.M. (2006). Unusual histone modifications in Trypanosoma brucei. FEBS Lett., 580(9): 2306-2310

 

Hake S.B. and Allis C.D. (2006). Histone H3 variants and their potential role in indexing mammalian genomes: The “H3 barcode hypothesis”. PNAS, 103(17): 6428-6435 (Inaugural Artikel zu Ehren von C. David Allis’ Aufnahme in die National Academy of Science.)

 

Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G., Shabanowitz J., Bazett-Jones D.P., Allis C.D. and Hunt D.F. (2006). Expression patterns and post-translational modifications associated with mammalian histone H3 variants. J. Biol. Chem., 281(1): 559-568

 

Taverna S.D., Allis C.D. and Hake S.B. (2006). “Hunt”-ing for post-translational modifications that underlie the histone code. Int. J. Mass. Spec., 259(1-3): 40-45

 

Kim J., Hake S.B. and Roeder R.G. (2005). The human homologue of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions. Mol. Cell, 20(5): 759-770

 

Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A., Shabanowitz J., Moran R.G., Allis C.D. and Hunt D.F. (2005). Modifications of human histone H3 variants during mitosis. Biochemistry, 4(44): 13202-13213

 

Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F. and Allis C.D. (2005). Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes. PNAS, 102(18): 6344-6349

 

Hake S.B., Xiao A. and Allis C.D. (2004). Linking the epigenetic “language” of covalent histone modifications to cancer. Br. J. Cancer, 90(4): 761-769

 

Camacho-Carvajal M.M., Klinger S., Schnappauf F., Hake S.B. and Steimle V. (2004). Importance of class II transactivator leucine-rich repeats for dominant negative function and nucleo-cytoplasmic transport. Int. Immunology, 16(1): 65-75

 

Hake S.B., Tobin H.M., Steimle V. and Denzin L.K. (2003). Comparison of the transcriptional regulation of classical and non-classical MHC class II genes. Eur. J. Immunology, 33(9): 2361-2371

 

Schnappauf F., Hake S.B., Camacho-Carvajal M.M., Bontron S., Lisowska-Grospierre B. and Steimle V. (2003). N-terminal destruction signals lead to rapid degradation of the major histocompatibility complex class II transactivator CIITA. Eur. J. Immunology, 33(8): 2337-2347

 

Glazier K.S., Hake S.B., Tobin H.M., Chadburn A., Schattner E.J. and Denzin L.K. (2002). Germinal center B cells regulate their capability to present antigen by modulation of HLA-DO. J. Exp. Med., 195(8): 1063-1069

 

Hake S.B., Masternak K., Kammerbauer C., Janzen C., Reith W. and Steimle V. (2000). CIITA leucine rich repeats control nuclear localization and in vitro recruitment of the MHC class II enhanceosome. Mol. Cell. Biol., 20(20): 7716-7725

 

 

Books

 

Book chapter entitled “Chromatin modifications” in “Nutrition in Epigenetics”. Wiley-Blackwell, 2011.

 

Co-Editor together with Janzen C.J. of the book “Protein Acetylation” in the book series “Methods in Molecular Biology”. HUMANA Press, Springer, 2013