Results 101 to 110 of about 6,750 (198)

Position and effect of random mutations in the Apobec3G N-terminal CDA domain bait on MAPPIT interaction with a Vif, Apobec3G or Gagpol prey.

, 2012
The residues of the head-to-head interface are directed towards the viewer. The effect of the mutation is indicated via a color scale from black to red, as indicated below the models.
Frank Peelman (137310), Delphine Lavens (137300), Isabel Uyttendaele (137298), Irma Lemmens (137306), Celia Bovijn (137308), Jan Tavernier (31436), Dominiek Catteeuw (137303)   +6 more
core   +1 more source

Species-Specific Exclusion of APOBEC3G from HIV-1 Virions by Vif [PDF]

, 2003
The HIV-1 accessory protein Vif (virion infectivity factor) is required for the production of infectious virions by CD4+ lymphocytes. Vif facilitates particle infectivity by blocking the inhibitory activity of APOBEC3G (CEM15), a virion-encapsidated ...
König, Renate, Münk, Carsten, Mariani, Roberto, Navarro, Francisco, Landau, Nathaniel R., Schröfelbauer, Bärbel, Chen, Darlene, Bollman, Brooke, Nymark-McMahon, Henrietta   +8 more
core   +1 more source

Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G.

PLoS Biology, 2004
Host genomes have adopted several strategies to curb the proliferation of transposable elements and viruses. A recently discovered novel primate defense against retroviral infection involves a single-stranded DNA-editing enzyme, APOBEC3G, that causes ...
Sara L Sawyer, Michael Emerman, Harmit S Malik   +2 more
doaj   +1 more source

APOBEC3G Cytoplasmic Bodies Are P-Bodies

, 2013
(A) Subcellular localization of APOBEC3G and LSM1 in T cells. Endogenous APOBEC3G and LSM1 were localized in peripheral blood CD4+ T cells (a) and H9 T lymphocytes (b) through indirect immunostaining using antibodies against APOBEC3G and LSM1 ...
Michael J Wichroski (72634), Tariq M Rana (63077), G. Brett Robb (72635)   +2 more
core   +1 more source

High level expression of the anti-retroviral protein APOBEC3G is induced by influenza A virus but does not confer antiviral activity

Retrovirology, 2009
Human APOBEC3G is an antiretroviral protein that was described to act via deamination of retroviral cDNA. However, it was suggested that APOBEC proteins might act with antiviral activity by yet other mechanisms and may also possess RNA deamination ...
Münk Carsten, Flory Egbert, Ehrhardt Christina, Hofmann Henning, Schmolke Mirco, Pauli Eva-K, Ludwig Stephan   +6 more
doaj   +1 more source

Effect of site-directed mutations in the N-terminal CDA domain of Apobec3G on the interactions with Gagpol and Gag.

, 2012
A: Effect of mutations on the Apobec3G-Gag interaction. Interactions between the Gag prey and the different mutant Apobec3G baits were determined via MAPPIT. The data are expressed as fold induction of luciferase activity after stimulation with Epo.
Frank Peelman (137310), Delphine Lavens (137300), Isabel Uyttendaele (137298), Irma Lemmens (137306), Celia Bovijn (137308), Jan Tavernier (31436), Dominiek Catteeuw (137303)   +6 more
core   +1 more source

APOBEC3G Variants and Protection against HIV-1 Infection in Burkina Faso.

PLoS ONE, 2016
Studies on host factors, particularly the APOBEC3G gene, have previously found an association with AIDS progression in some populations and against some HIV-1 strains but not others. Our study had two main objectives: firstly, to screen a population from
Tegwinde Rebeca Compaore, Serge Theophile Soubeiga, Abdoul Karim Ouattara, Dorcas Obiri-Yeboah, Damehan Tchelougou, Mamoudou Maiga, Maleki Assih, Cyrille Bisseye, Didier Bakouan, Issaka Pierre Compaore, Augustine Dembele, Jeremy Martinson, Jacques Simpore   +12 more
doaj   +1 more source

Importance of the N- and C-terminal domain of Apobec3G for the interaction with Apobec3G, Vif, Gag and Gagpol determined.

, 2012
A&B: Apobec3G, its N-terminal domain or its C-terminal domain were coupled to a V5-tagged MAPPIT bait receptor. Via MAPPIT, their interactions were determined with preys for full-length Apobec3G, Vif, Gagpol and Gag.
Frank Peelman (137310), Delphine Lavens (137300), Isabel Uyttendaele (137298), Irma Lemmens (137306), Celia Bovijn (137308), Jan Tavernier (31436), Dominiek Catteeuw (137303)   +6 more
core   +1 more source

A novel HIV-1 restriction factor that is biologically distinct from APOBEC3 cytidine deaminases in a human T cell line CEM.NKR

Retrovirology, 2009
Background Isolation of novel retroviral restriction factors will open new avenues for anti-HIV/AIDS treatment. Although HIV-1 replication is restricted by APOBEC3G/APOBEC3F, TRIM5α, and CD317, none defend HIV-1 infection under natural conditions ...
Zhou Tao, Han Yanxing, Dang Ying, Wang Xiaojun, Zheng Yong-Hui   +4 more
doaj   +1 more source

Suppression of APOBEC3-mediated restriction of HIV-1 by Vif

Frontiers in Microbiology, 2014
The APOBEC3 restriction factors are a family of deoxycytidine deaminases that are able to suppress replication of viruses with a single-stranded DNA intermediate by inducing mutagenesis and functional inactivation of the virus.
Yuqing eFeng, Tayyba T Baig, Robin P Love, Linda eChelico   +3 more
doaj   +1 more source