Complementary function of the two catalytic domains of APOBEC3G. - Wikidata - awgldk - TriplyDB

Complementary function of the two catalytic domains of APOBEC3G.

Complementary function of the two catalytic domains of APOBEC3G.

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Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies Model structure of human APOBEC3G Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1 Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity The localization of APOBEC3H variants in HIV-1 virions determines their antiviral activity Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factors Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model HIV-1 Vif, APOBEC, and intrinsic immunity Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G Human cytidine deaminase APOBEC3H restricts HIV-1 replication Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1 Inhibition of tRNA₃(Lys)-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration APOBEC3G targets human T-cell leukemia virus type 1.APOBEC3G & HTLV-1: inhibition without deamination Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all Suppression of APOBEC3-mediated restriction of HIV-1 by Vif NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1 Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components A DNA sequence recognition loop on APOBEC3A controls substrate specificity Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms APOBEC3G: an intracellular centurion HIV/AIDS epidemiology, pathogenesis, prevention, and treatment Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Cellular inhibitors of long interspersed element 1 and Alu retrotransposition.Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.AID and Apobec3G haphazard deamination and mutational diversity

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P2860

Complementary function of the two catalytic domains of APOBEC3G.

http://www.wikidata.org/entity/Q45274484

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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name

Complementary function of the two catalytic domains of APOBEC3G.

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Complementary function of the two catalytic domains of APOBEC3G.

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type

label

Complementary function of the two catalytic domains of APOBEC3G.

@en

Complementary function of the two catalytic domains of APOBEC3G.

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prefLabel

Complementary function of the two catalytic domains of APOBEC3G.

@en

Complementary function of the two catalytic domains of APOBEC3G.

@nl

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J.VIROL.2005.01.011

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Complementary function of the two catalytic domains of APOBEC3G.

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Brooke Bollman

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Francisco Navarro

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Hui Chen

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Kristopher Chiles

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Nathaniel R Landau

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Qin Yu

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Renate König

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374-386

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10.1016/J.VIROL.2005.01.011

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