The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
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Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodiesDeaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminaseThe dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3GMutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificitiesTargeting APOBEC3A to the viral nucleoprotein complex confers antiviral activityDifferential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypesHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsHuman LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activityAPOBEC1-mediated editing and attenuation of herpes simplex virus 1 DNA indicate that neurons have an antiviral role during herpes simplex encephalitisAn extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme modelHIV-1 Vif, APOBEC, and intrinsic immunityStructure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3GHuman APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integrationAPOBEC3G targets human T-cell leukemia virus type 1.APOBEC3G & HTLV-1: inhibition without deaminationMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allMultiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.T cells contain an RNase-insensitive inhibitor of APOBEC3G deaminase activity.Quantitative effect of suboptimal codon usage on translational efficiency of mRNA encoding HIV-1 gag in intact T cells.Differences in APOBEC3G expression in CD4+ T helper lymphocyte subtypes modulate HIV-1 infectivity.Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics.5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition.APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms.Small molecules that inhibit Vif-induced degradation of APOBEC3G.HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinantsThe level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals.Remarkable lethal G-to-A mutations in vif-proficient HIV-1 provirus by individual APOBEC3 proteins in humanized miceThe HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F.Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Monomeric APOBEC3G is catalytically active and has antiviral activity.Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.The role of BST2/tetherin in feline retrovirus infectionAPOBEC3 inhibits DEAD-END function to regulate microRNA activityAPOBEC3G: a double agent in defenseInteractions of HIV and drugs of abuse: the importance of glia, neural progenitors, and host genetic factors.Severe restriction of xenotropic murine leukemia virus-related virus replication and spread in cultured human peripheral blood mononuclear cells.Identification of a novel HIV-1 inhibitor targeting Vif-dependent degradation of human APOBEC3G protein.Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.
P2860
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P2860
The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@ast
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@en
type
label
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@ast
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@en
prefLabel
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@ast
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@en
P2093
P2860
P356
P1476
The enzymatic activity of CEM1 ...... ant of its antiviral activity.
@en
P2093
Aierken Abudu
Akifumi Takaori-Kondo
Keiko Fukunaga
Masayuki Kobayashi
Takashi Uchiyama
P2860
P304
44412-44416
P356
10.1074/JBC.C300376200
P407
P577
2003-09-11T00:00:00Z