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A prevalent cancer susceptibility APOBEC3A hybrid allele bearing APOBEC3B 3′UTR enhances chromosomal DNA damage
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Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions
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Identification of novel alternative splice variants of APOBEC-1 complementation factor with different capacities to support apolipoprotein B mRNA editing
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JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
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APOBEC3G incorporation into human immunodeficiency virus type 1 particles
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Involvement of a chaperone regulator, Bcl2-associated athanogene-4, in apolipoprotein B mRNA editing
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JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay
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JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
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GENOMICS (2002)
C -> U editing of neurofibromatosis 1 mRNA occurs in tumors that express both the type II transcript and apobec-1, the catalytic subunit of the apolipoprotein B mRNA-editing enzyme
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A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing
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JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Intracellular trafficking determinants in APOBEC-1, the catalytic subunit for cytidine to uridine editing of apolipoprotein B mRNA
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EXPERIMENTAL CELL RESEARCH (2001)
(O)over-cap | identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing
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JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Patterns of variant polyadenylation signal usage in human genes
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GENOME RESEARCH (2000)
Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex
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JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
An AU-rich sequence element (UUUN[A/U]U) downstream of the edited C in apolipoprotein B mRNA is a high-affinity binding site for Apobec-1:: Binding of Apobec-1 to this motif in the 3′ untranslated region of c-myc increases mRNA stability
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MOLECULAR AND CELLULAR BIOLOGY (2000)
Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme
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CELL (2000)
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