Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Elena Sokolskaja"'
Publikováno v:
PLoS Pathogens, Vol 7, Iss 8, p e1002194 (2011)
The HIV/AIDS pandemic is a major global health threat and understanding the detailed molecular mechanisms of HIV replication is critical for the development of novel therapeutics. To replicate, HIV-1 must access the nucleus of infected cells and inte
Externí odkaz:
https://doaj.org/article/f9114f3b0cf94e9abe5cf249eb3eb68a
Vif Counteracts a Cyclophilin A-Imposed Inhibition of Simian Immunodeficiency Viruses in Human Cells
Autor:
Sandra Kao, Mohammad Ahmed Khan, Ritu Goila-Gaur, Thomas Pertel, Eri Miyagi, Hiroaki Takeuchi, Jeremy Luban, Elena Sokolskaja, Sandrine Opi, Alicia Buckler-White, Klaus Strebel
Publikováno v:
Journal of Virology. 81:8080-8090
Vif is a primate lentiviral accessory protein that is crucial for viral infectivity. Vif counteracts the antiviral activity of host deaminases such as APOBEC3G and APOBEC3F. We now report a novel function of African green monkey simian immunodeficien
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1263d0609d8ca7e5e318a4b1abcaabfe
https://doi.org/10.1128/jvi.02727-06
https://doi.org/10.1128/jvi.02727-06
Publikováno v:
Journal of Virology. 80:2051-2054
Arsenic trioxide (As 2 O 3 ) increased human immunodeficiency virus type 1 (HIV-1) infectivity when particular Homo sapiens and Cercopithecus aethiops cell lines were used as targets. Knockdown of human TRIM5α by RNA interference eliminated the As 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::338344c2fb53f6691ee2050ba42666aa
https://doi.org/10.1128/jvi.80.4.2051-2054.2006
https://doi.org/10.1128/jvi.80.4.2051-2054.2006
Autor:
Youngnam Lee, Bin Yu, Amy H. Andreotti, Elena Sokolskaja, Jeremy Luban, John D. Colgan, Martha R. Neagu, Mohammed Asmal, Jason Schneidkraut
Publikováno v:
Immunity. 21(2):189-201
Cyclophilin A (CypA/Ppia) is a peptidyl-prolyl isomerase (PPIase) that binds the immunosuppressive drug cyclosporine. The resulting complex blocks T cell function by inhibiting the calcium-dependent phosphatase calcineurin. To identify the native fun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae2f5cf1f0c3540358f52f93dd473a24
Autor:
Massimo Pizzato, Elena Sokolskaja, Caterina Strambio-De-Castillia, Jeremy Luban, Silvia Olivari, Madeleine Zufferey
Publikováno v:
Journal of Virology, Vol. 84, No 9 (2010) pp. 4851-4855
Journal of virology
Journal of Virology; Vol 84
Journal of virology
Journal of Virology; Vol 84
Cyclosporine (CsA) decreases HIV-1 infectivity by blocking HIV-1 capsid (CA) interaction with target cell cyclophilin A (CypA). Yet, HIV-1 virions produced in the presence of CsA also exhibit decreased infectivity that was previously shown to be inde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7506fc655e1242621a55fe9fddb8953b
https://archive-ouverte.unige.ch/unige:21321
https://archive-ouverte.unige.ch/unige:21321
Autor:
Elena Sokolskaja, Jeremy Luban
Publikováno v:
Current opinion in microbiology. 9(4)
The peptidyl-prolyl isomerase cyclophilin A (CypA) binds a proline-rich loop on the surface of HIV-1 capsid (CA). This interaction increases HIV-1 infectivity in humans but promotes an anti-HIV-1 restriction activity in non-human primates. Efforts to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b71992e727cc2174044612c8f26b4e2b
https://pubmed.ncbi.nlm.nih.gov/16815734
https://pubmed.ncbi.nlm.nih.gov/16815734
Publikováno v:
Journal of virology. 80(6)
Cyclophilin A (CypA), a cytoplasmic, human immunodeficiency virus type 1 (HIV-1) CA-binding protein, acts after virion membrane fusion with human cells to increase HIV-1 infectivity. HIV-1 CA is similarly greeted by CypA soon after entry into rhesus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e96687f40451337d2ec9e83a79be8a35
https://pubmed.ncbi.nlm.nih.gov/16501094
https://pubmed.ncbi.nlm.nih.gov/16501094
The peptidyl-prolyl isomerase cyclophilin A (CypA) embraces an exposed, proline-rich loop on HIV-1 capsid (CA) and renders reverse transcription complexes resistant to an antiviral activity in human cells. A CypA fusion with TRIM5 that is unique to N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d21dad70507e865ced1f121cb3a3e3a4
https://europepmc.org/articles/PMC1239943/
https://europepmc.org/articles/PMC1239943/
Publikováno v:
Journal of virology. 78(23)
The peptidyl-prolyl isomerase cyclophilin A (CypA) increases the kinetics by which human immunodeficiency virus type 1 (HIV-1) spreads in tissue culture. This was conclusively demonstrated by gene targeting in human CD4 + T cells, but the role of Cyp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::408f984a030a51956e8f9f04d0bb11eb
https://pubmed.ncbi.nlm.nih.gov/15542632
https://pubmed.ncbi.nlm.nih.gov/15542632
Publikováno v:
Nature. 430(6999)
In Old World primates, TRIM5-alpha confers a potent block to human immunodeficiency virus type 1 (HIV-1) infection that acts after virus entry into cells. Cyclophilin A (CypA) binding to viral capsid protects HIV-1 from a similar activity in human ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a9b0adf7d812570ce9f6be3163afec9
https://pubmed.ncbi.nlm.nih.gov/15243629
https://pubmed.ncbi.nlm.nih.gov/15243629