Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases.

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Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization.

P2860

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P2860

Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases.

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http://www.wikidata.org/entity/Q41333839

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-hans

2016年学术文章

@zh-my

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2016年學術文章

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2016年學術文章

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name

Microscopy-based Saccharomyces ...... N-terminal acetyltransferases.

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type

Item

label

Microscopy-based Saccharomyces ...... N-terminal acetyltransferases.

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Microscopy-based Saccharomyces ...... N-terminal acetyltransferases.

@en

P1476

Microscopy-based Saccharomyces ...... N-terminal acetyltransferases.

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P2093

Camilla Osberg

http://www.w3.org/2001/XMLSchema#string

Michaël Marie

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Sandra Ninzima

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P2860

NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation

The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4

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

Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity

Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization

N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects

Structure of a Ternary Naa50p (NAT5/SAN) N-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

A generic protein purification method for protein complex characterization and proteome exploration

An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.

P2888

srep31627

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31627

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scholarly article

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10.1038/SREP31627

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English

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Henriette Aksnes

Thomas Arnesen

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2016-08-24T00:00:00Z

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1043333205

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27555049

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4995432

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Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases.

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P2860

P2860

Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases.

description

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type

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P1433

P1476

P2093

P2860

P2888

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P31

P356

P407

P478

P50

P577

P6179

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

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P6179

P698

P932