Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.
about
Suppression of APOBEC3-mediated restriction of HIV-1 by VifStructural Insights into HIV-1 Vif-APOBEC3F InteractionAPOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription.Antiretroviral restriction factors in mice.Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Redoxal, an inhibitor of de novo pyrimidine biosynthesis, augments APOBEC3G antiviral activity against human immunodeficiency virus type 1.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activityStructure-based design of novel naproxen derivatives targeting monomeric nucleoprotein of Influenza A virus.A ruthenium dimer complex with a flexible linker slowly threads between DNA bases in two distinct steps.APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.DNA intercalation optimized by two-step molecular lock mechanismL1 retrotransposition requires rapid ORF1p oligomerization, a novel coiled coil-dependent property conserved despite extensive remodelingInhibition of APOBEC3G activity impedes double-stranded DNA repairNuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular MechanismsStructural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Biochemical and biological studies of mouse APOBEC3.Single-Stranded Nucleic Acids Bind to the Tetramer Interface of SAMHD1 and Prevent Formation of the Catalytic Homotetramer.APOBECs and virus restriction.Extracting physical chemistry from mechanics: a new approach to investigate DNA interactions with drugs and proteins in single molecule experiments.Reassessing APOBEC3G Inhibition by HIV-1 Vif-Derived Peptides.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.Nanoscale Characterization of Interaction of APOBEC3G with RNA.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.Deep sequencing of HIV-1 reverse transcripts reveals the multifaceted antiviral functions of APOBEC3G.Single Molecule FRET Analysis of DNA Binding Proteins.
P2860
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P2860
Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年學術文章
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name
Oligomerization transforms hum ...... nucleic acid-binding protein.
@en
Oligomerization transforms hum ...... nucleic acid-binding protein.
@nl
type
label
Oligomerization transforms hum ...... nucleic acid-binding protein.
@en
Oligomerization transforms hum ...... nucleic acid-binding protein.
@nl
prefLabel
Oligomerization transforms hum ...... nucleic acid-binding protein.
@en
Oligomerization transforms hum ...... nucleic acid-binding protein.
@nl
P2093
P2860
P356
P1433
P1476
Oligomerization transforms hum ...... g nucleic acid-binding protein
@en
P2093
Amber Hertz
Denise S B Chan
Dominic F Qualley
Hylkje Geertsema
Ioulia Rouzina
Judith G Levin
Karin Musier-Forsyth
Kathy R Chaurasiya
Micah J McCauley
Shingo Kitamura
P2860
P2888
P356
10.1038/NCHEM.1795
P577
2013-11-24T00:00:00Z