LC-MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes.

about

LC-MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes.

Item

http://www.wikidata.org/entity/Q50106782

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@en

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@nl

type

Item

label

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@en

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@nl

prefLabel

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@en

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@nl

P1476

LC-MS/MS-based quantitative st ...... tuins to acylated nucleosomes.

@en

P2093

Daiki Kato

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

Jiaan Liu

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

Kana Tanabe

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

Shigehiro A Kawashima

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

P2860

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis

The first identification of lysine malonylation substrates and its regulatory enzyme

SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Sirtuins in epigenetic regulation

Sirtuin-dependent epigenetic regulation in the maintenance of genome integrity

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

P2888

s41598-018-21060-2

P304

2656

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

P31

scholarly article

P356

10.1038/S41598-018-21060-2

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

P407

English

P433

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

P478

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

P50

Hitoshi Kurumizaka

Motomu Kanai

Kenzo Yamatsugu

P577

2018-02-08T00:00:00Z

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

P6179

1100796104

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

P698

29422688

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

P932

5805777

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