Acetylation modulates prolactin receptor dimerization. - Wikidata - awgldk - TriplyDB

Acetylation modulates prolactin receptor dimerization.

Acetylation modulates prolactin receptor dimerization.

http://www.wikidata.org/entity/Q34320685

about

Molecular mechanisms of prolactin and its receptor Sirtuins in epigenetic regulation The natural chemopreventive agent sulforaphane inhibits STAT5 activity Blocking the class I histone deacetylase ameliorates renal fibrosis and inhibits renal fibroblast activation via modulating TGF-beta and EGFR signaling The synthetic α-bromo-2',3,4,4'-tetramethoxychalcone (α-Br-TMC) inhibits the JAK/STAT signaling pathway.Histone/protein deacetylases control Foxp3 expression and the heat shock response of T-regulatory cells.SUMO-specific protease 1 is critical for early lymphoid development through regulation of STAT5 activation.Regulation of STAT signaling by acetylation.Sirtuin biology and relevance to diabetes treatment.Histone deacetylases 6 and 9 and sirtuin-1 control Foxp3+ regulatory T cell function through shared and isoform-specific mechanisms.Prolactin protects retinal pigment epithelium by inhibiting sirtuin 2-dependent cell death PRLR regulates hepatic insulin sensitivity in mice via STAT5.SIRT1 regulates adaptive response of the growth hormone--insulin-like growth factor-I axis under fasting conditions in liver Histone deacetylases: a saga of perturbed acetylation homeostasis in cancer.Nanoscale membrane organization: where biochemistry meets advanced microscopy.STAT5 acetylation: Mechanisms and consequences for immunological control and leukemogenesis.Acetylation Modulates IL-2 Receptor Signaling in T Cells.HDAC6 Deacetylates HMGN2 to Regulate Stat5a Activity and Breast Cancer Growth.Deacetylase inhibitors repress STAT5-mediated transcription by interfering with bromodomain and extra-terminal (BET) protein function.Pancreatic β-cell prosurvival effects of the incretin hormones involve post-translational modification of Kv2.1 delayed rectifier channels.Acetylation and sumoylation control STAT5 activation antagonistically.Role of influenza A virus NP acetylation on viral growth and replication.Pharmacologic inhibition of STAT5 in acute myeloid leukemia.Regulation of T-Cell Signaling by Post-Translational Modifications in Autoimmune Disease.Implications of STAT3 and STAT5 signaling on gene regulation and chromatin remodeling in hematopoietic cancer STAT3 is constitutively acetylated on lysine 685 residues in chronic lymphocytic leukemia cells

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P2860

Acetylation modulates prolactin receptor dimerization.

http://www.wikidata.org/entity/Q34320685

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Acetylation modulates prolactin receptor dimerization.

@ast

Acetylation modulates prolactin receptor dimerization.

@en

Acetylation modulates prolactin receptor dimerization.

@nl

type

label

Acetylation modulates prolactin receptor dimerization.

@ast

Acetylation modulates prolactin receptor dimerization.

@en

Acetylation modulates prolactin receptor dimerization.

@nl

prefLabel

Acetylation modulates prolactin receptor dimerization.

@ast

Acetylation modulates prolactin receptor dimerization.

@en

Acetylation modulates prolactin receptor dimerization.

@nl

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PNAS.1010253107

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Acetylation modulates prolactin receptor dimerization.

@en

P2093

Hao Zhang

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

Jin-song Gao

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

Li Ma

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

Li Xu

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

Marina K Ayrapetov

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

Minsoo Kim

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

Shougang Zhuang

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

Xiaoyan Shi

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

Y Eugene Chin

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

Yingjie Guan

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

P2860

Structure and ligand of a histone acetyltransferase bromodomain

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Acetylation-dependent signal transduction for type I interferon receptor

Structural bases of unphosphorylated STAT1 association and receptor binding

Three-dimensional structure of the Stat3beta homodimer bound to DNA

Structure of the unphosphorylated STAT5a dimer.

The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif.

Stat3 dimerization regulated by reversible acetylation of a single lysine residue.

Hedgehog regulates smoothened activity by inducing a conformational switch.

Choose your partners: dimerization in eukaryotic transcription factors.

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107

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