APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.
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The APOBEC3 family of retroelement restriction factorsSuppression of APOBEC3-mediated restriction of HIV-1 by VifInteraction of APOBEC3A with DNA assessed by atomic force microscopyCytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulationSequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Characterization of the Catalytic Domain of Human APOBEC3B and the Critical Structural Role for a Conserved Methionine.A Single Nucleotide Polymorphism in Human APOBEC3C Enhances Restriction of LentivirusesAPOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain.A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.The ssDNA Mutator APOBEC3A Is Regulated by Cooperative DimerizationNuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.APOBECs and virus restriction.Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancer.The APOBEC Protein Family: United by Structure, Divergent in Function.Functions and Malfunctions of Mammalian DNA-Cytosine DeaminasesNanoscale Characterization of Interaction of APOBEC3G with RNA.Family-Wide Comparative Analysis of Cytidine and Methylcytidine Deamination by Eleven Human APOBEC Proteins.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Biochemical Characterization of APOBEC3H Variants: Implications for Their HIV-1 Restriction Activity and mC Modification.APOBEC3H polymorphisms associated with the susceptibility to HIV-1 infection and AIDS progression in Japanese.APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA.Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism.Multiple Inhibitory Factors Act in the Late Phase of HIV-1 Replication: a Systematic Review of the Literature.Scanning number and brightness yields absolute protein concentrations in live cells: a crucial parameter controlling functional bio-molecular interaction networks.Understanding the Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H.Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands
P2860
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P2860
APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
APOBEC3 multimerization correl ...... tion activity in living cells.
@en
type
label
APOBEC3 multimerization correl ...... tion activity in living cells.
@en
prefLabel
APOBEC3 multimerization correl ...... tion activity in living cells.
@en
P2093
P2860
P50
P1476
APOBEC3 multimerization correl ...... ction activity in living cells
@en
P2093
Elizabeth M Luengas
Patrick J Macdonald
Rebecca M McDougle
P2860
P304
P356
10.1016/J.JMB.2013.12.014
P407
P577
2013-12-17T00:00:00Z