ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
about
A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)Identification and characterization of the human ARD1-NATH protein acetyltransferase complexHuman Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activityCharacterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferaseArrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinaseThe chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregationCharacterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptidesN-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule PathwayN-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effectsMolecular basis for N-terminal acetylation by the heterodimeric NatA complexImplications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal orthologTEL2, an essential gene required for telomere length regulation and telomere position effect in Saccharomyces cerevisiaeProtein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.Cloning, characterization, and expression analysis of the novel acetyltransferase retrogene Ard1b in the mouseDe novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and femalesExpression of human NAA11 (ARD1B) gene is tissue-specific and is regulated by DNA methylationBiochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defectsExpression, crystallization and preliminary X-ray crystallographic analyses of two N-terminal acetyltransferase-related proteins from Thermoplasma acidophilumEffects of histone deacetylase inhibitors on HIF-1Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alphaDrosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complexThe NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotypeA Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutantProteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferaseCrystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific AcetylationThe biological functions of Naa10 - From amino-terminal acetylation to human diseaseAcetylation of androgen receptor by ARD1 promotes dissociation from HSP90 complex and prostate tumorigenesis.Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion.Functional genomics reveals relationships between the retrovirus-like Ty1 element and its host Saccharomyces cerevisiae.Protein N-terminal acetylation: NAT 2007-2008 Symposia.A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substratesArrest-defective-1 protein (ARD1): tumor suppressor or oncoprotein?Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndromeN-terminal acetylation of cellular proteins creates specific degradation signalsThe N-end rule pathway and regulation by proteolysis"Sleeping beauty": quiescence in Saccharomyces cerevisiae.Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha.Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing.Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae
P2860
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P2860
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@ast
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@en
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@nl
type
label
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@ast
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@en
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@nl
altLabel
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity
@en
prefLabel
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@ast
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@en
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@nl
P2860
P1433
P1476
ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity.
@en
P2093
P2860
P304
P407
P577
1992-06-01T00:00:00Z