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Akademický článek

Hepatitis C Virus NS2 Is a Protease Stimulated by Cofactor Domains in NS3

Autor: Schregel, V., Jacobi, S., Penin, F., Tautz, N., Rice,, Charles M.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 2009 Mar . 106(13), 5342-5347.

Externí odkaz: https://www.jstor.org/stable/40455197

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Nonstructural protein 3-4A: the Swiss army knife of hepatitis C virus

Autor: Morikawa, K., Lange, C. M., Gouttenoire, J., Meylan, E., Brass, V., Penin, F., Moradpour, D.

Publikováno v: Journal of viral hepatitis

Hepatitis C virus (HCV) nonstructural protein 3-4A (NS3-4A) is a complex composed of NS3 and its cofactor NS4A. It harbours serine protease as well as NTPase/RNA helicase activities and is essential for viral polyprotein processing, RNA replication a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::d1ce7c3c4b3e6943194ab67739bab93d

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Structural determinants that target the hepatitis C virus core protein to lipid droplets

Autor: Boulant, S., Montserret, R., Hope, Rg, Ratinier, M., Targett-Adams, P., Lavergne, Jp, Penin, F., Mclauchlan, J.

Hepatitis C virus core protein is targeted to lipid droplets, which serve as intracellular storage organelles, by its C-terminal domain, termed D2. From circular dichroism and nuclear magnetic resonance analyses, we demonstrate that the major structu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::ae97b7134921237c7be7b87fd1c14f89
https://hal.archives-ouvertes.fr/hal-00313671

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Akademický článek

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Assembly of functional hepatitis C virus glycoproteins on infectious pseudoparticles occurs intracellularly and requires concomitant incorporation of E1 and E2 glycoproteins

Autor: Sandrin, V., Boulanger, P., Penin, F., Granier, C., François-Loïc, Cosset, Bartosch, B.

Publikováno v: J Gen Virol
J Gen Virol, 2005, 86, pp.3189-3199

International audience; Hepatitis C virus (HCV) E1 and E2 envelope glycoproteins (GPs) displayed on retroviral cores (HCVpp) are a powerful and highly versatile model system to investigate wild-type HCV entry. To further characterize this model syste

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::fecb7c0c4f0bd9b4186cfa3d6b05b337
https://hal.archives-ouvertes.fr/hal-00313677

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Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex

Autor: Moradpour, D., Gosert, R., Egger, D., Penin, F., Blum, He, Bienz, K.

Hepatitis C virus (HCV) replicates its genome in a membrane-associated complex composed of viral proteins, replicating RNA, and altered cellular membranes. Determinants for membrane association of the HCV nonstructural proteins involved in genome rep

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::9d16f5ddefe50b1ee66c54df0b0146a3
https://hal.archives-ouvertes.fr/hal-00313694

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Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh

Autor: Anja Böckmann, Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., Heise, H., Montserret, R., Penin, F., Baldus, M.

Publikováno v: J Biomol NMR
J Biomol NMR, 2003, 27, pp.323-339
HAL

International audience; Solid state NMR sample preparation and resonance assignments of the U-[13C,15N] 2x10.4 kDa dimeric form of the regulatory protein Crh in microcrystalline, PEG precipitated form are presented. Intra- and interresidue correlatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::1cb0583e39c4a0e3b20e2e138dc74142
https://hal.archives-ouvertes.fr/hal-00313695

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An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A

Autor: Brass, V., Bieck, E., Montserret, R., Wolk, B., Hellings, Ja, Blum, He, Penin, F., Moradpour, D.

Hepatitis C virus (HCV) nonstructural protein 5A (NS5A), a phosphoprotein of unknown function, is believed to be a component of a membrane-associated viral replication complex. The determinants for membrane association of NS5A, however, have not been

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::a4c43b391155cb6bef734dfc1e163ac3
https://hal.archives-ouvertes.fr/hal-00313705

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