Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Fanny Bringolf"'
Autor:
Nadine Ader-Ebert, Mojtaba Khosravi, Michael Herren, Mislay Avila, Lisa Alves, Fanny Bringolf, Claes Örvell, Johannes P Langedijk, Andreas Zurbriggen, Richard K Plemper, Philippe Plattet
Publikováno v:
PLoS Pathogens, Vol 11, Iss 5, p e1004880 (2015)
Despite large vaccination campaigns, measles virus (MeV) and canine distemper virus (CDV) cause major morbidity and mortality in humans and animals, respectively. The MeV and CDV cell entry system relies on two interacting envelope glycoproteins: the
Externí odkaz:
https://doaj.org/article/f1faabedef24493dbf5bd10d593003e4
Autor:
Nadine Ader-Ebert, Mojtaba Khosravi, Fanny Bringolf, Andreas Zurbriggen, Philippe Plattet, Mislay Avila, Marc Vandevelde, Lisa Alves
Publikováno v:
Journal of virology
Measles and canine distemper viruses (MeV and CDV, respectively) first replicate in lymphatic and epithelial tissues by using SLAM and nectin-4 as entry receptors, respectively. The viruses may also invade the brain to establish persistent infections
Autor:
Nadine Ader-Ebert, Fanny Bringolf, Richard K. Plemper, Andreas Zurbriggen, Mislay Avila, Mojtaba Khosravi, Lisa Alves, Philippe Plattet
Publikováno v:
Journal of virology
Membrane fusion for morbillivirus cell entry relies on critical interactions between the viral fusion (F) and attachment (H) envelope glycoproteins. Through extensive mutagenesis of an F cavity recently proposed to contribute to F's interaction with
Autor:
Fanny Bringolf, Jürgen Schneider-Schaulies, Andreas Zurbriggen, Silvan Röthlisberger, Mojtaba Khosravi, Maria Bieringer, Francesco C. Origgi, Philippe Plattet
Publikováno v:
Journal of virology
Europe PubMed Central
Europe PubMed Central
Measles virus (MeV) and canine distemper virus (CDV) possess tetrameric attachment proteins (H) and trimeric fusion proteins, which cooperate with either SLAM or nectin 4 receptors to trigger membrane fusion for cell entry. While the MeV H-SLAM cocry
Dimerization Efficiency of Canine Distemper Virus Matrix Protein Regulates Membrane-Budding Activity
Autor:
Fanny Bringolf, Marianne Wyss, Michael Herren, Philippe Plattet, Beatriz Vidondo, Andreas Zurbriggen, Johannes P. M. Langedijk
Paramyxoviruses rely on the matrix (M) protein to orchestrate viral assembly and budding at the plasma membrane. Although the mechanistic details remain largely unknown, structural data suggested that M dimers and/or higher-order oligomers may facili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cf194dd340fa23734c8d677bf654570
https://europepmc.org/articles/PMC5533904/
https://europepmc.org/articles/PMC5533904/
Autor:
Richard K. Plemper, Fanny Bringolf, Nadine Ader-Ebert, Andreas Zurbriggen, Claes Örvell, Mojtaba Khosravi, Philippe Plattet, Michael Herren, Mislay Avila, Lisa Alves, Johannes P. M. Langedijk
Publikováno v:
PLoS pathogens
Ader-Ebert, Nadine; Khosravi, Mojtaba; Herren, Michael; Avila Sanchez, Mislay; Alves, Lisa; Bringolf, Fanny Anne; Örvell, Claes; Langedijk, Johannes P; Zurbriggen, Andreas; Plemper, Richard K; Plattet, Philippe (2015). Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process. PLoS pathogens, 11(5), e1004880. Public Library of Science 10.1371/journal.ppat.1004880
PLoS Pathogens
PLoS Pathogens, Vol 11, Iss 5, p e1004880 (2015)
Ader-Ebert, Nadine; Khosravi, Mojtaba; Herren, Michael; Avila Sanchez, Mislay; Alves, Lisa; Bringolf, Fanny Anne; Örvell, Claes; Langedijk, Johannes P; Zurbriggen, Andreas; Plemper, Richard K; Plattet, Philippe (2015). Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process. PLoS pathogens, 11(5), e1004880. Public Library of Science 10.1371/journal.ppat.1004880
PLoS Pathogens
PLoS Pathogens, Vol 11, Iss 5, p e1004880 (2015)
Despite large vaccination campaigns, measles virus (MeV) and canine distemper virus (CDV) cause major morbidity and mortality in humans and animals, respectively. The MeV and CDV cell entry system relies on two interacting envelope glycoproteins: the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::647ad5bdd5f46e3276d774382d446435
https://www.zora.uzh.ch/id/eprint/113662/
https://www.zora.uzh.ch/id/eprint/113662/