Multimerization of Staufen1 in live cells. - sprookjes - yvandenbroek - TriplyDB

Multimerization of Staufen1 in live cells.

Multimerization of Staufen1 in live cells.

http://www.wikidata.org/entity/Q39751807

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Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay Transient CPEB dimerization and translational control The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing 'Black sheep' that don't leave the double-stranded RNA-binding domain fold Multiple Myo4 motors enhance ASH1 mRNA transport in Saccharomyces cerevisiae.HERV-K(HML-2), a seemingly silent subtenant - but still waters run deep.Selective ligand activity at Nur/retinoid X receptor complexes revealed by dimer-specific bioluminescence resonance energy transfer-based sensors Staufen1 Regulates Multiple Alternative Splicing Events either Positively or Negatively in DM1 Indicating Its Role as a Disease Modifier mRNP granules. Assembly, function, and connections with disease.Characterization of staufen1 ribonucleoproteins by mass spectrometry and biochemical analyses reveal the presence of diverse host proteins associated with human immunodeficiency virus type 1.Specificity of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR for double-stranded RNA: insights from thermodynamics and small-angle X-ray scattering.Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity.Hyper conserved elements in vertebrate mRNA 3'-UTRs reveal a translational network of RNA-binding proteins controlled by HuR.Control of myogenesis by rodent SINE-containing lncRNAs STAU1 binding 3' UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdown mRNA-mRNA duplexes that autoelicit Staufen1-mediated mRNA decay.Staufen-mediated mRNA decay.Synaptic control of local translation: the plot thickens with new characters.RNA Localization in the Vertebrate Oocyte: Establishment of Oocyte Polarity and Localized mRNA Assemblages.The downregulation of the RNA-binding protein Staufen2 in response to DNA damage promotes apoptosis.The M-phase specific hyperphosphorylation of Staufen2 involved the cyclin-dependent kinase CDK1.Cell cycle-dependent regulation of the RNA-binding protein Staufen1.Multiplexing of multicolor bioluminescence resonance energy transfer.Staufen1 senses overall transcript secondary structure to regulate translation The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity

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Multimerization of Staufen1 in live cells.

http://www.wikidata.org/entity/Q39751807

description

2010 nî lūn-bûn

@nan

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

2010年學術文章

@zh

2010年學術文章

@zh-hant

name

Multimerization of Staufen1 in live cells.

@en

Multimerization of Staufen1 in live cells.

@nl

type

label

Multimerization of Staufen1 in live cells.

@en

Multimerization of Staufen1 in live cells.

@nl

prefLabel

Multimerization of Staufen1 in live cells.

@en

Multimerization of Staufen1 in live cells.

@nl

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Multimerization of Staufen1 in live cells.

@en

P2093

Billy Breton

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

Catherine Martel

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

Gabriel Lapointe

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Karine Boulay

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

Luc Desgroseillers

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

Samuel Dugré-Brisson

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Sylvain Armando

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

Thomas Duchaîne

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

Véronique Trépanier

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P2860

Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum

Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay

Characterization of Staufen 1 ribonucleoprotein complexes

The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus

The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs

Molecular mapping of the determinants involved in human Staufen-ribosome association

Modular structure of PACT: distinct domains for binding and activating PKR

A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum

Identification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particles

A genome-wide approach identifies distinct but overlapping subsets of cellular mRNAs associated with Staufen1- and Staufen2-containing ribonucleoprotein complexes

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585-597

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scholarly article

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10.1261/RNA.1664210

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3

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16

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2010-01-14T00:00:00Z

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41028196

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20075165

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