Search Results - "Lischka, P."

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  1. 1

    Antiviral strategies to combat cytomegalovirus infections in transplant recipients by Lischka, Peter, Zimmermann, Holger

    Published in Current opinion in pharmacology (01-10-2008)
    “…Human cytomegalovirus remains an important pathogen for transplant recipients. To date, a limited number of drugs have been licensed for the treatment of HCMV…”
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  2. 2

    First Report of Successful Treatment of Multidrug‐Resistant Cytomegalovirus Disease with the Novel Anti‐CMV Compound AIC246 by Kaul, D. R., Stoelben, S., Cober, E., Ojo, T., Sandusky, E., Lischka, P., Zimmermann, H., Rubsamen‐Schaeff, H.

    Published in American journal of transplantation (01-05-2011)
    “…We report the first case of cytomegalovirus (CMV) disease treated with AIC246, a novel anti‐CMV compound which targets the viral terminase complex and remains…”
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    Cellular p32 Recruits Cytomegalovirus Kinase pUL97 to Redistribute the Nuclear Lamina by Marschall, Manfred, Marzi, Andrea, Siepen, Patricia aus dem, Jochmann, Ramona, Kalmer, Martina, Auerochs, Sabrina, Lischka, Peter, Leis, Martina, Stamminger, Thomas

    Published in The Journal of biological chemistry (30-09-2005)
    “…Replication of human cytomegalovirus is limited at the level of nucleocytoplasmic transport of viral capsids, a process that requires the disassembly of the…”
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  6. 6

    The UL69 Transactivator Protein of Human Cytomegalovirus Interacts with DEXD/H-Box RNA Helicase UAP56 To Promote Cytoplasmic Accumulation of Unspliced RNA by Lischka, Peter, Toth, Zsolt, Thomas, Marco, Mueller, Regina, Stamminger, Thomas

    Published in Molecular and Cellular Biology (01-03-2006)
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  7. 7

    RNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA by Toth, Zsolt, Lischka, Peter, Stamminger, Thomas

    Published in Nucleic acids research (01-01-2006)
    “…The human cytomegalovirus protein pUL69 belongs to a family of regulatory factors that is conserved within the Herpesviridae and includes the proteins ICP27 of…”
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    A novel transferable nuclear export signal mediates CRM1‐independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69 by Lischka, Peter, Rosorius, Olaf, Trommer, Erik, Stamminger, Thomas

    Published in The EMBO journal (17-12-2001)
    “…The best studied nuclear export processes are mediated by classical leucine‐rich nuclear export signals that specify recognition by the CRM1 export receptor…”
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  10. 10

    Sox10 Is an Active Nucleocytoplasmic Shuttle Protein, and Shuttling Is Crucial for Sox10-Mediated Transactivation by Rehberg, Stephan, Lischka, Peter, Glaser, Gabi, Stamminger, Thomas, Wegner, Michael, Rosorius, Olaf

    Published in Molecular and Cellular Biology (01-08-2002)
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  11. 11

    HIV-1 Nef Mimics an Integrin Receptor Signal that Recruits the Polycomb Group Protein Eed to the Plasma Membrane by Witte, Vanessa, Laffert, Bernd, Rosorius, Olaf, Lischka, Peter, Blume, Katja, Galler, Gunther, Stilper, Andrea, Willbold, Dieter, D'Aloja, Paola, Sixt, Michael, Kolanus, Johanna, Ott, Melanie, Kolanus, Waldemar, Schuler, Gerold, Baur, Andreas S.

    Published in Molecular cell (30-01-2004)
    “…The Nef protein of human and simian immunodeficiency virus (HIV/SIV) is believed to interfere with T cell activation signals by forming a signaling complex at…”
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  12. 12

    A Nonconventional Nuclear Localization Signal within the UL84 Protein of Human Cytomegalovirus Mediates Nuclear Import via the Importin α/β Pathway by Lischka, Peter, Sorg, Gabriele, Kann, Michael, Winkler, Michael, Stamminger, Thomas

    Published in Journal of Virology (01-03-2003)
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  13. 13

    Structural requirements for nuclear localization of GCMa/Gcm-1 by Hashemolhosseini, Said, Kilian, Karin, Kardash, Elena, Lischka, Peter, Stamminger, Thomas, Wegner, Michael

    Published in FEBS letters (23-10-2003)
    “…GCM proteins constitute a small transcription factor family. Nuclear localization of Drosophila GCM is mediated by a typical bipartite nuclear localization…”
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