SUMO-1 controls the protein stability and the biological function of phosducin - Wikidata - wikimedia - TriplyDB

SUMO-1 controls the protein stability and the biological function of phosducin

SUMO-1 controls the protein stability and the biological function of phosducin

http://www.wikidata.org/entity/Q28292447

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SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function Control of Rad52 recombination activity by double-strand break-induced SUMO modification.Enhanced retinal insulin receptor-activated neuroprotective survival signal in mice lacking the protein-tyrosine phosphatase-1B gene.Pias3 is necessary for dorso-ventral patterning and visual response of retinal cones but is not required for rod photoreceptor differentiation.Sumoylation of influenza A virus nucleoprotein is essential for intracellular trafficking and virus growth.SUMO-SIM interactions regulate the activity of RGSZ2 proteins.Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation.Modification of nonstructural protein 1 of influenza A virus by SUMO1.Small ubiquitin-like modifier modification of arrestin-3 regulates receptor trafficking.Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding Aberrant sumoylation signaling evoked by reactive oxygen species impairs protective function of Prdx6 by destabilization and repression of its transcription.SUMOylation Confers Posttranslational Stability on NPM-ALK Oncogenic Protein.Phosducin regulates the expression of transducin betagamma subunits in rod photoreceptors and does not contribute to phototransduction adaptation Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding.SUMOylation of pancreatic glucokinase regulates its cellular stability and activity Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication.Phosducin influences sympathetic activity and prevents stress-induced hypertension in humans and mice Targets and consequences of protein SUMOylation in neurons.The physiological roles of phosducin: from retinal function to stress-dependent hypertension.The ubiquitin-proteasome system in retinal health and disease.The role of ubiquitin and ubiquitin-like modification systems in papillomavirus biology.Methionine adenosyltransferase α2 sumoylation positively regulate Bcl-2 expression in human colon and liver cancer cells.Functional swapping between transmembrane proteins TMEM16A and TMEM16F.The Latency-Associated Nuclear Antigen of Kaposi's Sarcoma-Associated Herpesvirus Inhibits Expression of SUMO/Sentrin-Specific Peptidase 6 To Facilitate Establishment of Latency.Nuclear translocation of IGF-1R via p150(Glued) and an importin-β/RanBP2-dependent pathway in cancer cells.Agonist-regulated cleavage of the extracellular domain of parathyroid hormone receptor type 1.Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation.Pias3-dependent SUMOylation directs rod photoreceptor development.SUMO E3 ligases are expressed in the retina and regulate SUMOylation of the metabotropic glutamate receptor 8b.SUMOylation regulates cytochrome P450 2E1 expression and activity in alcoholic liver disease.Introduction to Sumoylation.SUMO expression shortens the lag phase of Saccharomyces cerevisiae yeast growth caused by complex interactive effects of major mixed fermentation inhibitors found in hot-compressed water-treated lignocellulosic hydrolysate.SUMO-1 promotes degradation of the polyglutamine disease protein ataxin-3

P2860

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P2860

SUMO-1 controls the protein stability and the biological function of phosducin

http://www.wikidata.org/entity/Q28292447

description

2006 nî lūn-bûn

@nan

2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

SUMO-1 controls the protein stability and the biological function of phosducin

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SUMO-1 controls the protein stability and the biological function of phosducin

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SUMO-1 controls the protein stability and the biological function of phosducin

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type

label

SUMO-1 controls the protein stability and the biological function of phosducin

@ast

SUMO-1 controls the protein stability and the biological function of phosducin

@en

SUMO-1 controls the protein stability and the biological function of phosducin

@nl

prefLabel

SUMO-1 controls the protein stability and the biological function of phosducin

@ast

SUMO-1 controls the protein stability and the biological function of phosducin

@en

SUMO-1 controls the protein stability and the biological function of phosducin

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

SUMO-1 controls the protein stability and the biological function of phosducin

@en

P2093

Christoph Klenk

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

Jan Humrich

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

Martin J Lohse

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

Ursula Quitterer

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P2860

Cloning and characterization of the rat and human phosducin-like protein genes: structure, expression and chromosomal localization

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1

Differential regulation of sentrinized proteins by a novel sentrin-specific protease

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly

Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex

Phosducin-like protein: an ethanol-responsive potential modulator of guanine nucleotide-binding protein function

PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies

Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p.

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8357-64

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scholarly article

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10.1074/JBC.M513703200

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P433

13

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281

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2006-03-31T00:00:00Z

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7351713

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P698

16421094

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