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HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsAn extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3GMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allMulti-scale modeling of HIV infection in vitro and APOBEC3G-based anti-retroviral therapyRationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulationsRandom mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.The cellular source for APOBEC3G's incorporation into HIV-1.Integrating computational modeling and functional assays to decipher the structure-function relationship of influenza virus PB1 protein.The roles of APOBEC3G complexes in the incorporation of APOBEC3G into HIV-1.Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.APOBEC2 is a monomer in solution: implications for APOBEC3G modelsAPOBEC3G subunits self-associate via the C-terminal deaminase domain.Functional domain organization of human APOBEC3G.APOBEC proteins and intrinsic resistance to HIV-1 infectionIntracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3GAPOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotranspositionHIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerizationFunctional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition.Biochemical basis of immunological and retroviral responses to DNA-targeted cytosine deamination by activation-induced cytidine deaminase and APOBEC3G.Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast.A Comparison of Two Single-Stranded DNA Binding Models by Mutational Analysis of APOBEC3G.Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases.Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007 թուականին հրատարակուած գիտական յօդուած
@hyw
2007 թվականին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Model structure of human APOBEC3G
@ast
Model structure of human APOBEC3G
@en
Model structure of human APOBEC3G
@en-gb
Model structure of human APOBEC3G
@nl
type
label
Model structure of human APOBEC3G
@ast
Model structure of human APOBEC3G
@en
Model structure of human APOBEC3G
@en-gb
Model structure of human APOBEC3G
@nl
altLabel
Model Structure of Human APOBEC3G
@en
prefLabel
Model structure of human APOBEC3G
@ast
Model structure of human APOBEC3G
@en
Model structure of human APOBEC3G
@en-gb
Model structure of human APOBEC3G
@nl
P2093
P2860
P1433
P1476
Model structure of human APOBEC3G
@en
P2093
Bastien Mangeat
Didier Trono
Kun-Lin Zhang
Millan Ortiz
Olivier Michielin
Vincent Zoete
P2860
P356
10.1371/JOURNAL.PONE.0000378
P407
P577
2007-01-01T00:00:00Z