The C-terminal extension of Lsm4 interacts directly with the 3' end of the histone mRNP and is required for efficient histone mRNA degradation.
about
Surprises in the 3'-end: 'U' can decide too!Distinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body.Deep sequencing shows multiple oligouridylations are required for 3' to 5' degradation of histone mRNAs on polyribosomesStructure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.In vivo characterization of the Drosophila mRNA 3' end processing core cleavage complex.The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation.YB-1 regulates tiRNA-induced Stress Granule formation but not translational repressionUridylation and adenylation of RNAs.Degradation of oligouridylated histone mRNAs: see UUUUU and goodbye.TUT7 catalyzes the uridylation of the 3' end for rapid degradation of histone mRNA.Birth and Death of Histone mRNAs.Snipper, an Eri1 homologue, affects histone mRNA abundance and is crucial for normal Drosophila melanogaster development.
P2860
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P2860
The C-terminal extension of Lsm4 interacts directly with the 3' end of the histone mRNP and is required for efficient histone mRNA degradation.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
The C-terminal extension of Ls ...... ient histone mRNA degradation.
@en
type
label
The C-terminal extension of Ls ...... ient histone mRNA degradation.
@en
prefLabel
The C-terminal extension of Ls ...... ient histone mRNA degradation.
@en
P2093
P2860
P356
P1433
P1476
The C-terminal extension of Ls ...... cient histone mRNA degradation
@en
P2093
Andrew Y Guo
Christian Kambach
William F Marzluff
P2860
P304
P356
10.1261/RNA.042531.113
P407
P577
2013-11-19T00:00:00Z