A split active site couples cap recognition by Dcp2 to activation.
about
7-methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly bound by decapping scavenger (DcpS) enzymes and potently inhibits their activityNew insights into decapping enzymes and selective mRNA decayThe structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complexActive Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformationStructure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activatorStructural basis of mRNA-cap recognition by Dcp1-Dcp2Changes 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 LocalizationDcp1 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 preadipocytesMaternally 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 domainSynthesis 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 cerevisaeStructural 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.
P2860
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P2860
A split active site couples cap recognition by Dcp2 to activation.
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
P2093
P2860
P356
P1476
A split active site couples cap recognition by Dcp2 to activation.
@en
P2093
Brittnee N Jones
Gail A Hernandez
John D Gross
Stephen N Floor
P2860
P2888
P304
P356
10.1038/NSMB.1879
P577
2010-08-15T00:00:00Z
P5875
P6179
1052685241