Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals
about
A single homozygous point mutation in a 3'untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathyThe redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation functionCellular and molecular basis of deiodinase-regulated thyroid hormone signalingSECIS elements in the coding regions of selenoprotein transcripts are functional in higher eukaryotesThe selenocysteine-specific elongation factor contains a novel and multi-functional domainThreading the needle: getting selenocysteine into proteinsHypermethylated-capped selenoprotein mRNAs in mammals.Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression.Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.The L7Ae RNA binding motif is a multifunctional domain required for the ribosome-dependent Sec incorporation activity of Sec insertion sequence binding protein 2.Size matters: a view of selenocysteine incorporation from the ribosome.Selenoprotein N in skeletal muscle: from diseases to function.Altered RNA binding activity underlies abnormal thyroid hormone metabolism linked to a mutation in selenocysteine insertion sequence-binding protein 2.Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation.A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpinsFunctional analysis of the interplay between translation termination, selenocysteine codon context, and selenocysteine insertion sequence-binding protein 2.A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.In Vitro Translation Assays for Selenocysteine Insertion.On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.
P2860
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P2860
Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Characterization of the SECIS ...... n of selenocysteine in mammals
@ast
Characterization of the SECIS ...... n of selenocysteine in mammals
@en
Characterization of the SECIS ...... n of selenocysteine in mammals
@nl
type
label
Characterization of the SECIS ...... n of selenocysteine in mammals
@ast
Characterization of the SECIS ...... n of selenocysteine in mammals
@en
Characterization of the SECIS ...... n of selenocysteine in mammals
@nl
prefLabel
Characterization of the SECIS ...... n of selenocysteine in mammals
@ast
Characterization of the SECIS ...... n of selenocysteine in mammals
@en
Characterization of the SECIS ...... n of selenocysteine in mammals
@nl
P2860
P356
P1476
Characterization of the SECIS ...... n of selenocysteine in mammals
@en
P2093
Kelvin Caban
Scott A Kinzy
P2860
P304
P356
10.1093/NAR/GKI826
P407
P577
2005-09-09T00:00:00Z