Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kelly E. Du Pont"'
Publikováno v:
J Biol Chem
The unwinding of dsRNA intermediates is critical for the replication of flavivirus RNA genomes. This activity is provided by the C-terminal helicase domain of viral nonstructural protein 3 (NS3). As a member of the superfamily 2 (SF2) helicases, NS3
Publikováno v:
Wiley Interdiscip Rev RNA
Flaviviruses are a major health concern because over half of the world population is at risk of infection and there are very few antiviral therapeutics to treat diseases resulting from infection. Replication is an essential part of the flavivirus sur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b792c131bee280003e51658a07eaaf6
https://europepmc.org/articles/PMC8888775/
https://europepmc.org/articles/PMC8888775/
Publikováno v:
J Virol
The unwinding of double-stranded RNA intermediates is critical for replication and packaging of flavivirus RNA genomes. This unwinding activity is achieved by the ATP-dependent nonstructural protein 3 (NS3) helicase. In previous studies, we investiga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9a176f40f19b0bde68e6993a7ca252b
https://doi.org/10.1101/2020.05.26.117580
https://doi.org/10.1101/2020.05.26.117580
Autor:
Oleksandr Kokhan, Aidan M. McKenzie, Christopher E. Berndsen, Isaiah Sumner, Kelly E. Du Pont
Publikováno v:
Biochemistry. 55:940-947
Human BST-2/tetherin is a host factor that inhibits the release of enveloped viruses, including HIV-1, HIV-2, and SIV, from the cell surface by tethering viruses to the host cell membrane. BST-2 has an α-helical ectodomain that forms disulfide-linke
Autor:
Christopher E. Berndsen, Reuven Wiener, Emily A. Todd, Nardeen Baiady, Prasanth Padala, Einav Cohen-Kfir, Kelly E. Du Pont, Bayan Mashahreh
Publikováno v:
Journal of Biological Chemistry. 291:2033-2042
The deubiquitinating enzyme associated molecule with the SH3 domain of STAM (AMSH) is crucial for the removal of ubiquitin molecules during receptor-mediated endocytosis and lysosomal receptor sorting. AMSH interacts with signal transducing adapter m
Publikováno v:
Biophysical Journal. 114:233a
Publikováno v:
Biophysical Journal. 108(2)
Human BST-2/tetherin is a host factor that inhibits release of HIV-1, HIV-2, and SIV from the cell surface. Viruses can evade this inhibition through antagonistic viral protein interactions with BST-2. Structurally, full-length BST-2 consists of an N
Autor:
Klaus Strebel, Amy J. Andrew, Kelly E. Du Pont, Sarah Welbourn, Sandra Kao, Christopher E. Berndsen
BST-2/tetherin is a cellular host factor capable of restricting the release of a variety of enveloped viruses, including HIV-1. Structurally, BST-2 consists of an N-terminal cytoplasmic domain, a transmembrane domain, an ectodomain, and a C-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b51901ac066572eb1a42b19e7a75819c
https://europepmc.org/articles/PMC4319038/
https://europepmc.org/articles/PMC4319038/