@book{BockGauchGiernatetal.2013,
  author    = {Bock, Stefanie and Gauch, Fabian and Giernat, Yannik and Hillebrand, Frank and Kozlova, Darja and Linck, Lisa and Moschall, Rebecca and Sauer, Markus and Schenk, Christian and Ulrich, Kristina and Bodem, Jochen},
  title     = {HIV-1 : Lehrbuch von Studenten f{\"u}r Studenten},
  organization    = {Bachelor- und Masterkurs Virologie 2013},
  isbn      = {978-3-923959-90-7},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-78980},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2013},
  abstract  = {Dies ist ein Lehrbuch {\"u}ber die HIV-1 Replikation, Pathogenese und Therapie. Es richtet sich an Studenten der Biologie und der Medizin, die etwas mehr {\"u}ber HIV erfahren wollen und stellt neben virologischen Themen auch die zellul{\"a}ren Grundlagen dar. Es umfasst den Viruseintritt, die reverse Transkription, Genom-Integration, Transkriptionsregualtion, die Kotrolle des Spleißens, der Polyadenylierung und des RNA-Exportes. Die Darstellung wird abgerundet mit Kapiteln zum intrazellul{\"a}rem Transport, zu Nef und zum Virusassembly. In zwei weiteren Kapitel wird die HIV-1 Pathogenese und die Therapie besprochen. Zur Lernkontrolle sind den Kapiteln Fragen und auch Klausurfragen angef{\"u}gt.},
  subject      = {HIV},
  language  = {de}
}
@article{HartlBodemJochheimetal.2011,
  author    = {Hartl, Maximilian J. and Bodem, Jochen and Jochheim, Fabian and Rethwilm, Axel and R{\"o}sch, Paul and W{\"o}hrl, Birgitta M.},
  title     = {Regulation of foamy virus protease activity by viral RNA},
  series = {Retrovirology},
  volume    = {8},
  journal   = {Retrovirology},
  number    = {Suppl. 1},
  doi       = {10.1186/1742-4690-8-S1-A228},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-142248},
  pages     = {A228},
  year      = {2011},
  abstract  = {No abstract available.},
  language  = {en}
}
@article{AvotaGassertSchneiderSchaulies2011,
  author    = {Avota, Elita and Gassert, Evelyn and Schneider-Schaulies, Sibylle},
  title     = {Cytoskeletal Dynamics: Concepts in Measles Virus Replication and Immunomodulation},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-69092},
  year      = {2011},
  abstract  = {In common with most viruses, measles virus (MV) relies on the integrity of the cytoskeleton of its host cells both with regard to efficient replication in these cells, but also retention of their motility which favors viral dissemination. It is, however, the surface interaction of the viral glycoprotein (gp) complex with receptors present on lymphocytes and dendritic cells (DCs), that signals effective initiation of host cell cytoskeletal dynamics. For DCs, these may act to regulate processes as diverse as viral uptake and sorting, but also the ability of these cells to successfully establish and maintain functional immune synapses (IS) with T cells. In T cells, MV signaling causes actin cytoskeletal paralysis associated with a loss of polarization, adhesion and motility, which has been linked to activation of sphingomyelinases and subsequent accumulation of membrane ceramides. MV modulation of both DC and T cell cytoskeletal dynamics may be important for the understanding of MV immunosuppression at the cellular level.},
  subject      = {Virologie},
  language  = {en}
}
@phdthesis{Lehmann2006,
  author    = {Lehmann, Christine},
  title     = {Die Bedeutung des Masernvirus Matrix-Proteins f{\"u}r die Virusfreisetzung und zelltypabh{\"a}ngige Unterschiede seines intrazellul{\"a}ren Transports},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-22107},
  school      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2006},
  abstract  = {Die Morphogenese von Viruspartikeln und deren Freisetzung aus infizierten Zellen sind sp{\"a}te Schritte im viralen Lebenszyklus. Matrix-Proteine (M) negativstr{\"a}ngiger RNA-Viren und Retroviren, bei denen es sich um periphere Membran-assoziierte Proteine handelt, spielen f{\"u}r diese Prozesse eine besonders wichtige Rolle. Im Verlauf der Masernvirus (MV)-Infektion interagiert das M-Protein mit dem viralen Nukleoproteinkomplex im Innern der Viruspartikel einerseits und mit den viralen Glykoproteinen auf der Oberfl{\"a}che andererseits. Die Bedeutung des MV M-Proteins f{\"u}r die Partikelproduktion und sein intrazellul{\"a}rer Transport wurden bislang wenig untersucht. In dieser Arbeit konnte gezeigt werden, dass das MV M-Protein in h{\"o}hermolekularen Komplexe oligomerisiert und transient mono-ubiquitiniert vorliegt. Beide biochemischen Eigenschaften des M-Proteins sind wahrscheinlich f{\"u}r die Partikelentstehung von Bedeutung, wie durch Studien an M-Protein-Orthologen anderer Viren bereits belegt wurde. Das MV M-Protein assoziierte mit Membranen und speziellen Membranmikrodom{\"a}nen, sogenannten Detergenz-resistenten Membranfraktionen (DRMs), und vermittelte nach transienter Expression in Fibroblasten die Produktion Virus-{\"a}hnlicher Partikel (virus-like particles, VLPs). Es ist beschrieben, dass umh{\"u}llte Viren pr{\"a}ferenziell aus DRMs freigesetzt werden. Die Koexpression des MV-Glykoproteins F erh{\"o}hte den Anteil mit DRM-assoziierten M-Proteins um ein Vierfaches, steigerte jedoch, wie auch das H-Protein, die Effizienz der VLP-Freisetzung nicht. {\"U}berraschenderweise waren beide jedoch selbst in der Lage VLPs zu induzieren. Die Effizienz der VLP-Produktion war gering und entsprach der der Viruspartikelfreisetzung. Dendritische Zellen (DCs) sind f{\"u}r MV semipermissiv. Obwohl alle viralen Proteine synthetisiert werden, wird kein infekti{\"o}ses Virus freigesetzt. In dieser Arbeit konnte gezeigt werden, dass die intrazellul{\"a}re Lokalisation der M-, H- und N-Proteine dramatisch von der in der produktiv infizierbaren Fibroblastenzelllinie HeLa abweicht. W{\"a}hrend in infizierten HeLa-Zellen das M-Protein mit Lamp-1-positiven sp{\"a}ten Endosomen kolokalisierte, akkumulierten in DCs alle untersuchten viralen Proteine in einem sp{\"a}t endosomalen Kompartiment, das das Tetraspanin CD81, aber nicht Lamp-1, enthielt und m{\"o}glicherweise an der MHC-Klasse-II-abh{\"a}ngigen Antigenpr{\"a}sentation beteiligt ist.},
  subject      = {Masernvirus},
  language  = {de}
}
@article{SegevRagerZismanIsakovetal.1994,
  author    = {Segev, Y. and Rager-Zisman, B. and Isakov, N. and Schneider-Schaulies, Sibylle and ter Meulen, V. and Udem, S. A. and Segal, S. and Wolfson, M.},
  title     = {Reversal of measles virus mediated increase of phosphorylating activity in persistently infected mouse neuroblastoma cells by anti measles antibodies},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62362},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Virologie},
  language  = {en}
}
@article{SchneiderSchauliesSchneiderSchauliesSchusteretal.1994,
  author    = {Schneider-Schaulies, Sibylle and Schneider-Schaulies, J{\"u}rgen and Schuster, A. and Bayer, M. and Pavlovic, J. and ter Meulen, V.},
  title     = {Cell type specific MxA-mediated inhibition of measles virus transcription in human brain cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62255},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Virologie},
  language  = {en}
}
@article{SiwkaSchwinnBaczkoetal.1994,
  author    = {Siwka, Wieslaw and Schwinn, Andreas and Baczko, Knut and Pardowitz, Iancu and Mhalu, Fred and Shao, John and Rethwilm, Axel and ter Meulen, Volker},
  title     = {vpu and env sequence variability of HIV-1 isolates from Tanzania},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61355},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Virologie},
  language  = {en}
}
@article{HahnBaunachBraeutigametal.1994,
  author    = {Hahn, Heidi and Baunach, Gerald and Br{\"a}utigam, Sandra and Mergia, Ayalew and Neumann-Haefelin, Dieter and Daniel, Muthiah D. and McClure, Myra O. and Rethwilm, Axel},
  title     = {Reactivity of primate sera to foamy virus Gag and Bet proteins},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61366},
  year      = {1994},
  abstract  = {In order to establish criteria for the Serodiagnosis of foamy virus infections we investigated the extent to which sera from iofected individuals of human and primate origin react with structural and non-structural virus proteins in immunoblot assays. Using lysates from infected cells as the source of virus antigen, antibodies were preferentially detected against the Gag proteins and the non-structural Bet protein. Both the Gag precursor molecules of 70 and 74K apparent M\(_r\) and the cytoplasmic 60K M\(_r\) Bet protein were found to be phosphorylated, the latter being synthesized in large amounts in infected cells. Rahbit antiserum raised against recombinant human foamy virus (HFV) Gag major capsid protein cross-reacted with foamy viruses of chimpanzee, gorilla, orang-utan, rhesus monkey and Mrican green monkey origin. This was reßected by a broad cross-reactivity of the respective monkey sera to the Gag proteins of the various foamy virus isolates. Cross-reactivity of antisera against the Bet protein was restricted to viruses from man and the great apes. Recombinant Gag and Bet proteins expressed in prokaryotes or in insect cells were readily recognized by foamy virus-positive primate sera. Screening serum samples from chimpanzees with HFV Gag and Bet proteins expressed by recombinant baculoviruses revealed that 18 out of 35 (52\%) were positive for Gag antibodies. Of these, 13 (72 o/o) showed antiborlies against the Bet protein, indicating that Bet antigen is of value in sero1ogical screening for foamy virus infections.},
  subject      = {Virologie},
  language  = {en}
}
@article{SchliephakeRethwilm1994,
  author    = {Schliephake, Andreas W. and Rethwilm, Axel},
  title     = {Nuclear Localization of Foamy Virus Gag Precursor Protein},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61371},
  year      = {1994},
  abstract  = {All foamy viruses give rise to a strong nuclear staining when infected cells are reacted with sera from infected hosts. This nuclear ftuorescence distinguishes foamy viruses from all other retroviruses. The experiments reported here indicate that the foamy virus Gag precursor protein is transiently located in the nuclei of infected cells and this is the likely reason for the typical foamy virus nuclear fluorescence. By using the vaccinia virus expression system, a conserved basic sequence motif in the nucleocapsid domain of foamy virus Cag proteins was identified to be responsible for the nuclear transport of the gag precursor molecule. Tbis motif was also found to be able to direct a heterologous protein, the Gag protein of human immunodeficiency virus, into the nucleus.},
  subject      = {Virologie},
  language  = {en}
}
@article{MuellerCzubRethwilmetal.1994,
  author    = {M{\"u}ller, J. G. and Czub, S. and Rethwilm, Axel and M{\"u}ller-Hermelink, H. K.},
  title     = {Korrelation von Organpathologie und Verteilung virusreplizierenderZellen, nachgewiesen mit der RNA in situ Hybridisierungw{\"a}hrend der SIVmac-Infektion von Macaca mulatta},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47331},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Virologie},
  language  = {de}
}