Related references
Note: Only part of the references are listed.Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA
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被撤回的出版物: Identification of a specific domain required for dimerization of activation-induced cytidine deaminase (Retracted Article. See vol 283, pg 660, 2008)
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APOBEC3G DNA deaminase acts processively 3′ → 5′ on single-stranded DNA
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Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus
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Complementary function of the two catalytic domains of APOBEC3G
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Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
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A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
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Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 Virions through interactions with viral and nonviral RNAs
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APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
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The interaction between HIV-1 Gag and APOBEC3G
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APOBEC3G incorporation into human immunodeficiency virus type 1 particles
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Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
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Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor
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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
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The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
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DNA determination mediates innate immunity to retroviral infection
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