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HIV Genome-Wide Protein Associations: a Review of 30 Years of Research1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal StructureCytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulationVif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C.Evolutionary Paradigms from Ancient and Ongoing Conflicts between the Lentiviral Vif Protein and Mammalian APOBEC3 Enzymes.Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.Crystal structures of APOBEC3G N-domain alone and its complex with DNA.Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B.A Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.Feline Immunodeficiency Virus Vif N-Terminal Residues Selectively Counteract Feline APOBEC3s.Reassessing APOBEC3G Inhibition by HIV-1 Vif-Derived Peptides.The APOBEC Protein Family: United by Structure, Divergent in Function.The Structural Interface between HIV-1 Vif and Human APOBEC3H.CBFß and HIV Infection.The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and Deamination.Influence of the DNA sequence/length and pH on deaminase activity, as well as the roles of the amino acid residues around the catalytic center of APOBEC3F.APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA.APOBEC Enzymes as Targets for Virus and Cancer Therapy.Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.Fab-based inhibitors reveal ubiquitin independent functions for HIV Vif neutralization of APOBEC3 restriction factors.SIVmac239 Vif and Human APOBEC3B Interactions Resemble Those Between HIV-1 Vif and Human APOBEC3G.Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.
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description
2015 nî lūn-bûn
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2015 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@ast
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@en
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@nl
type
label
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@ast
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@en
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@nl
prefLabel
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@ast
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@en
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural Insights into HIV-1 Vif-APOBEC3F Interaction
@en
P2093
Atsuko Hachiya
Hiroaki Awazu
Hirotaka Ode
Kazuhiro Matsuoka
Masaaki Nakashima
Michiko Nemoto
Nobuhisa Watanabe
Shingo Kitamura
Shinya Tsuzuki
Takashi Kawamura
P2860
P304
P3181
P356
10.1128/JVI.02369-15
P577
2015-11-04T00:00:00Z