PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner.

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Multifactorial Regulation of G Protein-Coupled Receptor Endocytosis.Ubiquitin-Related Roles of β-Arrestins in Endocytic Trafficking and Signal Transduction.

P2860

Q37551913-544400E1-B6C7-4FCD-B42D-3C0E96D7D9EA Q38704567-0C185BBD-2657-4969-8AA4-56D7A1FE9F7D

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PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner.

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http://www.wikidata.org/entity/Q54235583

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@en

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@nl

type

Item

label

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@en

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@nl

prefLabel

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@en

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@nl

P1476

PKCβII inhibits the ubiquitina ...... sphorylation-dependent manner.

@en

P2093

Hyun Jin Choi

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

Kyeong-Man Kim

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

Mei Zheng

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

Moo-Yeol Lee

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

Shuohan Guo

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

Xiaohan Zhang

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

Xiaowei Zhang

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

P2860

A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription

Roles of protein kinase C and actin-binding protein 280 in the regulation of intracellular trafficking of dopamine D3 receptor

A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum.

Heterologous activation of protein kinase C stimulates phosphorylation of delta-opioid receptor at serine 344, resulting in beta-arrestin- and clathrin-mediated receptor internalization

Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase, cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanisms

Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin

Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus

Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2

Degradation of CFTR by the ubiquitin-proteasome pathway

Regulation of C3a receptor signaling in human mast cells by G protein coupled receptor kinases.

P304

3929-3937

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

P31

scholarly article

P356

10.1016/J.FEBSLET.2015.10.031

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

P407

English

P433

24 Pt B

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

P478

589

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

P577

2015-11-03T00:00:00Z

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

P698

26545496

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

P921

protein ubiquitination

PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner.

about

P2860

P2860

PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921