Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex (Q24306092)

N(alpha)-acetyltransferase 50, NatE catalytic subunit

GOA release 2020-03-11

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GOA release 2020-03-11

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Thomas Arnesen

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Jan Erik Varhaug

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object named as

Jan Erik Varhaug

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Johan R. Lillehaug

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object named as

Johan R Lillehaug

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Janniche Torsvik

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object named as

Janniche Torsvik

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author name string

Dave Anderson

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Helene B Halseth

Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.

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language of work or name

English

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publication date

26 April 2006

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published in

Gene

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volume

371

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issue

2

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page(s)

291-5

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cites work

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An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

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Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila

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Composition and function of the eukaryotic N-terminal acetyltransferase subunits

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N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins

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Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily

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Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase

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Identification and characterization of the human ARD1-NATH protein acetyltransferase complex

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SMART, a simple modular architecture research tool: identification of signaling domains

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NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p

1 reference

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7 January 2021

Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin

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Expression of N-acetyl transferase human and human Arrest defective 1 proteins in thyroid neoplasms

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Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

16507339

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Consolidated OpenCitations Corpus – April 2017