Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Hanno Scheffczik"'
Autor:
Mildred Ugozzoli, Simona Tavarini, Sandra Nuti, Manmohan Singh, Emanuele Montomoli, Barbara Baudner, Hanno Scheffczik, Jina Kazzaz, Rino Rappuoli, Andreas Wack, Ilaria Manini, Derek T. O'Hagan, Giuseppe Del Giudice, Anne Katrin Hilbert
Publikováno v:
Vaccine. 26:552-561
Influenza is controlled by protective titres of neutralizing antibodies, induced with the help of CD4 T-cells, and by antiviral T-cell effector function. Adjuvants are essential for the efficient vaccination of a naïve population against avian influ
Autor:
Hanno Scheffczik, Wolfgang Garten, Simone Kiermayer, Markus Eickmann, Jürgen A. Richt, Ina Kraus, Manuela Fluess
Publikováno v:
Journal of Virology. 75:12098-12104
The open reading frame III of Borna disease virus (BDV) codes for a protein with a mass of 16 kDa, named p16 or BDV-M. p16 was described as an N-glycosylated protein in several previous publications and therefore was termed gp18, although the amino a
Autor:
Markus Eickmann, Milton T. Stubbs, Simone Kiermayer, Hanno Scheffczik, Wolfgang Garten, Ina Kraus
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:1371-1373
The matrix protein M of Borna disease virus (BDV) is associated with the inner viral membrane and is thought to be a mediator between the nucleocapsid and the lipid-containing envelope in stabilizing the virus shape. The full-length BDV-M gene encodi
Publikováno v:
Nucleic acids research. 30(7)
Herpesvirus DNA packaging involves binding and cleavage of DNA containing the specific DNA-packaging motifs. Here we report a first characterization of the terminase subunits pUL56 and pUL89 of human cytomegalovirus (HCMV). Both gene products were sh
Autor:
Elke Bogner, Markus Eickmann, Ina Kraus, Simone Kiermayer, Hanno Scheffczik, Wolfgang Garten, Andreas Holzenburg
Publikováno v:
FEBS letters. 506(2)
In the present study the coding sequence of the cytoplasmic tail of the human cytomegalovirus glycoprotein B (gB) was expressed. The secondary structure of the purified recombinant protein was analyzed by circular dichroism, and the quaternary struct