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A split active site couples cap recognition by Dcp2 to activation.

A split active site couples cap recognition by Dcp2 to activation.

http://www.wikidata.org/entity/Q34103699

about

7-methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly bound by decapping scavenger (DcpS) enzymes and potently inhibits their activity New insights into decapping enzymes and selective mRNA decay The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex Active Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2 Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator Structural basis of mRNA-cap recognition by Dcp1-Dcp2 Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.Phosphorylation of mRNA decapping protein Dcp1a by the ERK signaling pathway during early differentiation of 3T3-L1 preadipocytes Maternally recruited DCP1A and DCP2 contribute to messenger RNA degradation during oocyte maturation and genome activation in mouse.Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex.Control of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domain Synthesis and evaluation of fluorescent cap analogues for mRNA labelling.Cap analogs modified with 1,2-dithiodiphosphate moiety protect mRNA from decapping and enhance its translational potential.RNA degradation in Saccharomyces cerevisae Structural and functional control of the eukaryotic mRNA decapping machinery.The role of disordered protein regions in the assembly of decapping complexes and RNP granules.The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.The decapping activator Edc3 and the Q/N-rich domain of Lsm4 function together to enhance mRNA stability and alter mRNA decay pathway dependence in Saccharomyces cerevisiae.mRNA decapping in 3D.Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis.

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A split active site couples cap recognition by Dcp2 to activation.

http://www.wikidata.org/entity/Q34103699

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին 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

A split active site couples cap recognition by Dcp2 to activation.

@ast

A split active site couples cap recognition by Dcp2 to activation.

@en

A split active site couples cap recognition by Dcp2 to activation.

@nl

type

label

A split active site couples cap recognition by Dcp2 to activation.

@ast

A split active site couples cap recognition by Dcp2 to activation.

@en

A split active site couples cap recognition by Dcp2 to activation.

@nl

prefLabel

A split active site couples cap recognition by Dcp2 to activation.

@ast

A split active site couples cap recognition by Dcp2 to activation.

@en

A split active site couples cap recognition by Dcp2 to activation.

@nl

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Nature Structural & Molecular Biology

P1476

A split active site couples cap recognition by Dcp2 to activation.

@en

P2093

Brittnee N Jones

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

Gail A Hernandez

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

John D Gross

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

Stephen N Floor

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Helicase structure and mechanism

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

TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation

The hDcp2 protein is a mammalian mRNA decapping enzyme

Functional characterization of the mammalian mRNA decapping enzyme hDcp2

mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes

MUSCLE: multiple sequence alignment with high accuracy and high throughput

Jalview Version 2--a multiple sequence alignment editor and analysis workbench

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions

The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family

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1096-1101

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10.1038/NSMB.1879

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9

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17

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2010-08-15T00:00:00Z

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45651096

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1052685241

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20711189

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2933276

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