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注意：仅列出部分参考文献，下载原文获取全部文献信息。Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA
Sukhdev S. Brar et al.
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The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction
April J. Schumacher et al.
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Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
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Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1
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JOURNAL OF VIROLOGY (2007)
Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G
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APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G
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The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA
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Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration
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JOURNAL OF VIROLOGY (2007)
Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
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JOURNAL OF VIROLOGY (2007)
DNA deaminases AID and APOBEC3G act processively on single-stranded DNA
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Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H
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The APOBEC-2 crystal structure and functional implications for the deaminase AID
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NATURE (2007)
Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits
Joseph E. Wedekind et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
High-molecular-mass APOBEC3G complexes restrict alu retrotransposition
Ya-Lin Chiu et al.
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Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication
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Biochemical activities of highly purified, catalytically active human APOBEC3G: Correlation with antiviral effect
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Monomeric APOBEC3G is catalytically active and has antiviral activity
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APOBEC3G DNA deaminase acts processively 3′ → 5′ on single-stranded DNA
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NATURE STRUCTURAL & MOLECULAR BIOLOGY (2006)
AFM studies on the role of the protein RdgC in bacterial DNA recombination
I Tessmer et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
被撤回的出版物: Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells (Retracted Article. See vol 466, pg 276, 2010)
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The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
G Haché et al.
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Complementary function of the two catalytic domains of APOBEC3G
F Navarro et al.
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DNA polymerase V and RecA protein, a minimal mutasome
K Schlacher et al.
MOLECULAR CELL (2005)
Biochemical analysis of hypermutational targeting by wild type and mutant activation-induced cytidine deaminase
R Bransteitter et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
How do site-specific DNA-binding proteins find their targets?
SE Halford et al.
NUCLEIC ACIDS RESEARCH (2004)
The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1
KF Xie et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome
Q Yu et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2004)
Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
B Mangeat et al.
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The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
H Zhang et al.
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Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy
Y Yang et al.
METHODS (2003)
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JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
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The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands
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A minimal exonuclease domain of WRN forms a hexamer on DNA and possesses both 3′-5′ exonuclease and 5′-protruding strand endonuclease activities
Y Xue et al.
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A novel single-molecule study to determine protein-protein association constants
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JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2001)
One- and three-dimensional pathways for proteins to reach specific DNA sites
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Sequence dependent rigidity of single stranded DNA
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PHYSICAL REVIEW LETTERS (2000)
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