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Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

http://www.wikidata.org/entity/Q30496858

about

Hallmarks of cancer and AU-rich elements DSCR1 interacts with FMRP and is required for spine morphogenesis and local protein synthesis RNA binding protein CUGBP2/CELF2 mediates curcumin-induced mitotic catastrophe of pancreatic cancer cells.Alternative RISC assembly: binding and repression of microRNA-mRNA duplexes by human Ago proteins.Probing nucleic acid interactions and pre-mRNA splicing by Förster Resonance Energy Transfer (FRET) microscopy Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction RNAs as chaperones.mRNA stability as a function of striated muscle oxidative capacity.In Vitro Synthesis, Delivery, and Bioavailability of Exogenous mRNA in Gene Transfer Mediated by PiggyBac Transposition.

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P2860

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

http://www.wikidata.org/entity/Q30496858

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@ast

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

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type

label

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@ast

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@en

prefLabel

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@ast

Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@en

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1471-2121-11-69

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BMC Cell Biology

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Intracellular localization and interaction of mRNA binding proteins as detected by FRET.

@en

P2093

J David Port

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

Molly A Taylor

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

Pamela S David Gerecht

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

P2860

The RNA-binding protein KSRP promotes decay of beta-catenin mRNA and is inactivated by PI3K-AKT signaling

Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA.

AU binding proteins recruit the exosome to degrade ARE-containing mRNAs

Phosphorylation of HuR by Chk2 regulates SIRT1 expression

Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping

14-3-3sigma is a p37 AUF1-binding protein that facilitates AUF1 transport and AU-rich mRNA decay

Caveolin-1 and -2 in airway epithelium: expression and in situ association as detected by FRET-CLSM

beta-Dystroglycan modulates the interplay between actin and microtubules in human-adhered platelets

Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA

Functional cloning of BRF1, a regulator of ARE-dependent mRNA turnover.

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1471-2121-11-69

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69

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scholarly article

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10.1186/1471-2121-11-69

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11

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2010-09-15T00:00:00Z

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