Results 41 to 50 of about 6,750 (198)

Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization [PDF]

open access: yesRetrovirology, 2009
Abstract Background The cellular cytidine deaminase APOBEC3G (A3G), when incorporated into the human immunodeficiency virus type 1 (HIV-1), renders viral particles non-infectious. We previously observed that mutation of a single cysteine residue of A3G (C100S) inhibited A3G packaging.
Walker Robert C   +5 more
openaire   +3 more sources

Association of APOBEC3G genotypes and CD4 decline in Thai and Cambodian HIV-infected children with moderate immune deficiency

open access: yesAIDS Research and Therapy, 2012
Introduction Human APOBEC3G is a host defense factor that potently inhibits HIV replication. We hypothesize that HIV-infected children with a genetic variant of APOBEC3G will have a more rapid disease progression.
Bunupuradah Torsak   +12 more
doaj   +1 more source

HIV-1 adaptation studies reveal a novel Env-mediated homeostasis mechanism for evading lethal hypermutation by APOBEC3G. [PDF]

open access: yesPLoS Pathogens, 2018
HIV-1 replication normally requires Vif-mediated neutralization of APOBEC3 antiviral enzymes. Viruses lacking Vif succumb to deamination-dependent and -independent restriction processes.
Terumasa Ikeda   +5 more
doaj   +1 more source

Structural basis of sequence-specific RNA recognition by the antiviral factor APOBEC3G

open access: yesNature Communications, 2022
Interaction between APOBEC3G and RNA is critical for its antiviral function. Here, the authors report four co-crystal structures of rhesus macaque APOBEC3G and RNA, demonstrating unpaired AA and GA dinucleotide motifs are preferentially recognized.
Hanjing Yang   +4 more
doaj   +1 more source

APOBEC3G levels predict rates of progression to AIDS [PDF]

open access: yesRetrovirology, 2007
APOBEC3G (hA3G) is a newly discovered cellular factor of innate immunity that inhibits HIV replication in vitro. Whether hA3G confers protection against HIV in vivo is not known. To investigate the possible anti-HIV activity of hA3G in vivo, we examined hA3G mRNA abundance in primary human cells isolated from either HIV-infected or HIV-uninfected ...
Wu Hulin, Jin Xia, Smith Harold
openaire   +3 more sources

Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.

open access: yesPLoS Pathogens, 2006
APOBEC3G is an antiviral host factor capable of inhibiting the replication of both exogenous and endogenous retroviruses as well as hepatitis B, a DNA virus that replicates through an RNA intermediate.
Michael J Wichroski   +2 more
doaj   +2 more sources

Dysregulated APOBEC3G causes DNA damage and promotes genomic instability in multiple myeloma

open access: yesBlood Cancer Journal, 2021
Multiple myeloma (MM) is a heterogeneous disease characterized by significant genomic instability. Recently, a causal role for the AID/APOBEC deaminases in inducing somatic mutations in myeloma has been reported.
Srikanth Talluri   +8 more
doaj   +1 more source

Restriction of retroviral replication by APOBEC3G/F and TRIM5α [PDF]

open access: yesTrends in Microbiology, 2008
Pathogenic viral infections have exerted selection pressure on their hosts to evolve cellular antiviral inhibitors referred to as restriction factors. Examples of such molecules are APOBEC3G, APOBEC3F and TRIM5alpha. APOBEC3G and APOBEC3F are cytidine deaminases that are able to strongly inhibit retroviral replication by at least two mechanisms.
Huthoff, Hendrik, Towers, Greg J.
openaire   +3 more sources

Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n. [PDF]

open access: yesPLoS Pathogens, 2012
The DNA deaminase APOBEC3G converts cytosines to uracils in retroviral cDNA, which are immortalized as genomic strand G-to-A hypermutations by reverse transcription.
Eric W Refsland   +2 more
doaj   +1 more source

Identification of an APOBEC3G Binding Site in Human Immunodeficiency Virus Type 1 Vif and Inhibitors of Vif-APOBEC3G Binding [PDF]

open access: yesJournal of Virology, 2007
ABSTRACT The APOBEC3 cytidine deaminases are potent antiviral factors that restrict replication of human immunodeficiency virus type 1 (HIV-1). HIV-1 Vif binds APOBEC3G and APOBEC3F and targets these proteins for ubiquitination by forming an E3 ubiquitin ligase with cullin 5 and elongins B and C.
Andrew, Mehle   +6 more
openaire   +2 more sources

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