Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
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HIV Genome-Wide Protein Associations: a Review of 30 Years of Research1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal StructureCrystal 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 regulationRedoxal, an inhibitor of de novo pyrimidine biosynthesis, augments APOBEC3G antiviral activity against human immunodeficiency virus type 1.APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain.Identification of the HIV-1 Vif and Human APOBEC3G Protein Interface.The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches.Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.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.The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme.APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular MechanismsA Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.Structural and functional assessment of APOBEC3G macromolecular complexes.The APOBEC Protein Family: United by Structure, Divergent in Function.Nanoscale Characterization of Interaction of APOBEC3G with RNA.CBFß and HIV Infection.Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.NMR-based method of small changes reveals how DNA mutator APOBEC3A interacts with its single-stranded DNA substrate.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Characterization of the Deamination Coupled with Sliding along DNA of Anti-HIV Factor APOBEC3G on the Basis of the pH-Dependence of Deamination Revealed by Real-Time NMR Monitoring.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.Hydrogen bonds are a primary driving force for de novo protein folding.Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway.Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands
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P2860
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
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2015 nî lūn-bûn
@nan
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
2015年论文
@zh
2015年论文
@zh-cn
name
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@ast
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@en
type
label
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@ast
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@en
prefLabel
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@ast
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@en
P2093
P2860
P356
P1476
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
@en
P2093
Celia A Schiffer
Elizabeth M Luengas
Hiroshi Matsuo
JingYing Zhang
Mayuko Hara
Megumi Shigematsu
Shivender M D Shandilya
Takahide Kouno
P2860
P2888
P304
P356
10.1038/NSMB.3033
P577
2015-05-18T00:00:00Z