New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.

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New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

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New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

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New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

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New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

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New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

@en

New chemical tools for probing ...... nt lysine deacylase sirtuin 2.

@nl

P1476

New chemical tools for probing ...... ent lysine deacylase sirtuin 2

@en

P2093

Attila Lehotzky

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

Daria Monaldi

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Matthias Schiedel

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Sören Swyter

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Tobias Rumpf

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Wolfgang Sippl

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P2860

SIRT2 as a Therapeutic Target for Age-Related Disorders

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

SIRT2 induces the checkpoint kinase BubR1 to increase lifespan

A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection

Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling

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scholarly article

P356

10.1098/RSTB.2017.0083

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P407

English

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1748

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P478

373

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P50

Manfred Jung

Sándor Szunyogh

Judit Ovádi

P577

2018-06-01T00:00:00Z

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P698

29685963

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P932

5915722

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