نتایج جستجو برای: 1 vif

تعداد نتایج: 2762395  

2015
Allison M. Land Jiayi Wang Emily K. Law Ryan Aberle Andrea Kirmaier Annabel Krupp Welkin E. Johnson Reuben S. Harris

APOBEC3B is a newly identified source of mutation in many cancers, including breast, head/neck, lung, bladder, cervical, and ovarian. APOBEC3B is a member of the APOBEC3 family of enzymes that deaminate DNA cytosine to produce the pro-mutagenic lesion, uracil. Several APOBEC3 family members function to restrict virus replication. For instance, APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H combine ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
M J Potash G Bentsman T Muir C Krachmarov P Sova D J Volsky

We recently reported that HIV-1 Vif (virion infectivity factor) inhibits HIV-1 protease in vitro and in bacteria, suggesting that it may serve as the basis for the design of new protease inhibitors and treatment for HIV-1 infection. To evaluate this possibility, we synthesized peptide derivatives from the region of Vif, which inhibits protease, and tested their activity on protease. In an assay...

2010
Julien R. C. Bergeron Hendrik Huthoff Dennis A. Veselkov Rebecca L. Beavil Peter J. Simpson Stephen J. Matthews Michael H. Malim Mark R. Sanderson

The HIV-1 viral infectivity factor (Vif) protein recruits an E3 ubiquitin ligase complex, comprising the cellular proteins elongin B and C (EloBC), cullin 5 (Cul5) and RING-box 2 (Rbx2), to the anti-viral proteins APOBEC3G (A3G) and APOBEC3F (A3F) and induces their polyubiquitination and proteasomal degradation. In this study, we used purified proteins and direct in vitro binding assays, isothe...

2017
Congjie Zhai Ling Ma Zhixin Zhang Jiwei Ding Jing Wang Yongxin Zhang Xiaoyu Li Fei Guo Liyan Yu Jinming Zhou Shan Cen

Human APOBEC3G (hA3G) is a cytidine deaminase which inhibits HIV-1 replication. The HIV-1 accessory protein viral infectivity factor (Vif) counteracts with hA3G by targeting it for proteasomal degradation. In this work, we constructed and optimized molecular models of the hA3G dimer and the hA3G-Vif complex. The molecular modeling study revealed that the loop7 motif of hA3G appears on the inter...

Journal: :Journal of virology 1996
R A Fouchier J H Simon A B Jaffe M H Malim

The Vif protein of human immunodeficiency virus type 1 is required for productive replication in peripheral blood lymphocytes and a limited number of immortalized T-lymphoid lines (nonpermissive cells). In contrast, Vif is fully dispensable for virus replication in other T-cell lines (permissive cells). Because the infection phenotype of released virions is determined by producer cells and by t...

Journal: :Journal of virology 2010
John S Albin Guylaine Haché Judd F Hultquist William L Brown Reuben S Harris

Tandem stop mutations K26X and H27X in human immunodeficiency virus type 1 (HIV-1) vif compromise virus replication in human T-cell lines that stably express APOBEC3F (A3F) or APOBEC3G (A3G). We previously reported that partial resistance to A3G could develop in these Vif-deficient viruses through a nucleotide A200-to-T/C transversion and a vpr null mutation, but these isolates were still susce...

Journal: :The EMBO journal 2004
Heather L Wiegand Brian P Doehle Hal P Bogerd Bryan R Cullen

The HIV-1 Vif protein suppresses the inhibition of viral replication caused by the human antiretroviral factor APOBEC3G. As a result, HIV-1 mutants that do not express the Vif protein are replication incompetent in 'nonpermissive' cells, such as primary T cells and the T-cell line CEM, that express APOBEC3G. In contrast, Vif-defective HIV-1 replicates effectively in 'permissive' cell lines, suc...

Journal: :The Journal of general virology 1998
I Huvent S S Hong C Fournier B Gay J Tournier C Carrière M Courcoul R Vigne B Spire P Boulanger

Human immunodeficiency virus type 1 (HIV-1) wild-type (WT) virion infectivity factor (Vif) protein (Vifwt) and full-length Gag precursor (Pr55Gag) were found to be co-encapsidated into extracellular, membrane-enveloped virus-like particles released by budding from Sf9 cells co-expressing the two recombinant proteins in trans, with an average copy number of 3.5+/-0.6 Vifwt per 100 Pr55Gag molecu...

2010
Iris Cadima-Couto Joao Goncalves

APOBEC proteins appeared in the cellular battle against HIV-1 as part of intrinsic cellular immunity. The antiretroviral activity of some of these proteins is overtaken by the action of HIV-1 Viral Infectivity Factor (Vif) protein. Since the discovery of APOBEC3G (A3G) as an antiviral factor, many advances have been made to understand its mechanism of action in the cell and how Vif acts in orde...

2012
Stefanie Jäger Dong Young Kim Judd F. Hultquist Keisuke Shindo Rebecca S. LaRue Eunju Kwon Ming Li Brett D. Anderson Linda Yen David Stanley Cathal Mahon Joshua Kane Kathy Franks-Skiba Peter Cimermancic Alma Burlingame Andrej Sali Charles S. Craik Reuben S. Harris John D. Gross Nevan J. Krogan

Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication. TheAIDSvirus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host’s antiviral defence by hijacking a ubiquitin ligase complex, containing CUL5, ELOC, ELOB and a RING-box protein, and targeting APOB...

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