Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

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Probing the interaction between NatA and the ribosome for co-translational protein acetylation.FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α

P2860

Q42706640-B64C7BB8-981C-47F8-AC4D-900A70209DEC Q58758683-0AE4802C-0EF7-4F74-A577-BD930AE8C2CF

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Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

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2017年論文

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2017年论文

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Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

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Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

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Item

label

Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

@en

Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

@nl

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Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

@en

Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

@nl

P1476

Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

@en

P2093

Andrea Gumiero

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

Felix Alexander Weyer

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

Irmgard Sinning

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

Jürgen Kopp

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

Karine Lapouge

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

P2860

A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)

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

The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex

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

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

Electrostatics of nanosystems: application to microtubules and the ribosome

The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation

MolProbity: all-atom structure validation for macromolecular crystallography

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

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ncomms15726

P304

15726

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P31

scholarly article

P356

10.1038/NCOMMS15726

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English

P478

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Gert Bange

P577

2017-06-06T00:00:00Z

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P6179

1085883920

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P698

28585574

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P932

5467210

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Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

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P2860

P2860

Structural basis of HypK regulating N-terminal acetylation by the NatA complex.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P6179

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P6179

P698

P932