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Article

ARD1 and NAT1 proteins form a complex that has N‐terminal acetyltransferase activity.

1 Jun 1992

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 1600941
DOI: 10.1002/j.1460-2075.1992.tb05267.x

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Related research

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Click a neighbor to travelStep 1 · 12 closest

ARD1 and NAT1 proteins form a complex that has N‐terminal acetyltransferase activity.PMID 1600941Read ↗

Biological Function and Mechanism of NAT10 in CancerSemantic proximity Read ↗

Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex.Semantic proximity Read ↗

[Cloning and analysis of a novel gene encoding N-terminal acetyltransferase subunit].Semantic proximity Read ↗

NATs at a glanceSemantic proximity Read ↗

A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)Semantic proximity Read ↗

Cellular effects of NAT-mediated histone N-terminal acetylationSemantic proximity Read ↗

N-Terminal Acetyltransferases Are Cancer-Essential Genes Prevalently Upregulated in TumoursSemantic proximity Read ↗

The biological functions of Naa10 – from amino-terminal acetylation to human diseaseSemantic proximity Read ↗

Mutation of an Arabidopsis NatB N-alpha-terminal acetylation complex component causes pleiotropic developmental defects.Semantic proximity Read ↗

Identification of the human N(alpha)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression.Semantic proximity Read ↗

Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.Semantic proximity Read ↗

The biological functions of Naa10 — From amino-terminal acetylation to human diseaseSemantic proximity Read ↗

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