Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
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Model structure of human APOBEC3GDeaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminaseMolecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA.Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editingThe apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decayMutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificitiesThe neurofibromatosis type I messenger RNA undergoes base-modification RNA editingThe structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1An auxiliary factor containing a 240-kDa protein complex is involved in apolipoprotein B RNA editingApolipoprotein B RNA editing enzyme-deficient mice are viable despite alterations in lipoprotein metabolismTranscriptome-wide sequencing reveals numerous APOBEC1 mRNA-editing targets in transcript 3' UTRsAPOBEC1-mediated editing and attenuation of herpes simplex virus 1 DNA indicate that neurons have an antiviral role during herpes simplex encephalitisIdentification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editaseRNA Editing-Systemic Relevance and Clue to Disease Mechanisms?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 editingIntracellular localization of human cytidine deaminase. Identification of a functional nuclear localization signalMutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activityNovel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factorARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editingInhibition of the apolipoprotein B mRNA editing enzyme-complex by hnRNP C1 protein and 40S hnRNP complexesSecondary structure for the apolipoprotein B mRNA editing site. Au-binding proteins interact with a stem loopRetroviral restriction by APOBEC proteinsEvolution of RNA-protein interactions: non-specific binding led to RNA splicing activity of fungal mitochondrial tyrosyl-tRNA synthetasesMultiple protein domains determine the cell type-specific nuclear distribution of the catalytic subunit required for apolipoprotein B mRNA editingTargeted disruption of the mouse apobec-1 gene abolishes apolipoprotein B mRNA editing and eliminates apolipoprotein B48The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.Maize haplotype with a helitron-amplified cytidine deaminase gene copy.A prokaryotic-type cytidine deaminase from Arabidopsis thaliana gene expression and functional characterization.Functions and regulation of the APOBEC family of proteinsAn 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.Evolution of RNA editing in trypanosome mitochondriaNMR structure of the apoB mRNA stem-loop and its interaction with the C to U editing APOBEC1 complementary factor.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.LINE-1 retroelements complexed and inhibited by activation induced cytidine deaminase.Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: development of a chloroplast in vitro RNA editing system.Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.Apolipoprotein B RNA sequence 3' of the mooring sequence and cellular sources of auxiliary factors determine the location and extent of promiscuous editing.A site-specific factor interacts directly with its cognate RNA editing site in chloroplast transcripts.Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.AID mediates hypermutation by deaminating single stranded DNA.
P2860
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P2860
Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Evolutionary origins of apoB m ...... nding motif at its active site
@ast
Evolutionary origins of apoB m ...... nding motif at its active site
@en
Evolutionary origins of apoB m ...... nding motif at its active site
@en-gb
Evolutionary origins of apoB m ...... nding motif at its active site
@nl
type
label
Evolutionary origins of apoB m ...... nding motif at its active site
@ast
Evolutionary origins of apoB m ...... nding motif at its active site
@en
Evolutionary origins of apoB m ...... nding motif at its active site
@en-gb
Evolutionary origins of apoB m ...... nding motif at its active site
@nl
prefLabel
Evolutionary origins of apoB m ...... nding motif at its active site
@ast
Evolutionary origins of apoB m ...... nding motif at its active site
@en
Evolutionary origins of apoB m ...... nding motif at its active site
@en-gb
Evolutionary origins of apoB m ...... nding motif at its active site
@nl
P2093
P1433
P1476
Evolutionary origins of apoB m ...... nding motif at its active site
@en
P2093
P304
P356
10.1016/0092-8674(95)90328-3
P407
P577
1995-04-21T00:00:00Z