A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase
about
Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymesAutoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activityZ-DNA-binding proteins can act as potent effectors of gene expression in vivo.A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domainsComplex regulation of the human gene for the Z-DNA binding protein DLM-1.The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domainsThe Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequencesThe human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling proteinADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian cellsEvidence that vaccinia virulence factor E3L binds to Z-DNA in vivo: Implications for development of a therapy for poxvirus infectionThe solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNAHuman RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducibleA left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1RNA editing by adenosine deaminases that act on RNAA role for Z-DNA binding in vaccinia virus pathogenesisA-to-I editing of coding and non-coding RNAs by ADARsNew Insights into the Biological Role of Mammalian ADARs; the RNA Editing ProteinsThe ADAR protein familyProtein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon responseThe structures of non-CG-repeat Z-DNAs co-crystallized with the Z-DNA-binding domain, hZ ADAR1The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNACrystal Structure of a Poxvirus-Like Zalpha Domain from Cyprinid Herpesvirus 3Structural and functional studies of a large winged Z-DNA-binding domain of Danio rerio protein kinase PKZRequirement of dimerization for RNA editing activity of adenosine deaminases acting on RNALiver disintegration in the mouse embryo caused by deficiency in the RNA-editing enzyme ADAR1Enhancement of replication of RNA viruses by ADAR1 via RNA editing and inhibition of RNA-activated protein kinaseRNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKRFunctions and regulation of RNA editing by ADAR deaminasesMutations in ADAR1 cause Aicardi-Goutières syndrome associated with a type I interferon signatureAdenosine deaminases acting on RNA (ADARs) are both antiviral and proviralADAR1 is essential for the maintenance of hematopoiesis and suppression of interferon signalingIntracellular localization of differentially regulated RNA-specific adenosine deaminase isoforms in inflammationMouse models for Aicardi-Goutières syndrome provide clues to the molecular pathogenesis of systemic autoimmunityZBP1 subcellular localization and association with stress granules is controlled by its Z-DNA binding domains.Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.An RNA editor, adenosine deaminase acting on double-stranded RNA (ADAR1).A PKR-like eukaryotic initiation factor 2alpha kinase from zebrafish contains Z-DNA binding domains instead of dsRNA binding domainsStructure-function analysis of the Z-DNA-binding domain Zalpha of dsRNA adenosine deaminase type I reveals similarity to the (alpha + beta) family of helix-turn-helix proteinsBiological function of the vaccinia virus Z-DNA-binding protein E3L: gene transactivation and antiapoptotic activity in HeLa cells.CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain.
P2860
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P2860
A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@ast
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@en
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@nl
type
label
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@ast
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@en
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@nl
prefLabel
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@ast
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@en
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@nl
P2093
P2860
P3181
P356
P1476
A Z-DNA binding domain present ...... randed RNA adenosine deaminase
@en
P2093
P2860
P304
P3181
P356
10.1073/PNAS.94.16.8421
P407
P577
1997-08-05T00:00:00Z