The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation.
about
hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNAeIF4G is required for the pioneer round of translation in mammalian cellsIntegration of splicing, transport and translation to achieve mRNA quality control by the nonsense-mediated decay pathway.Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogramming of translation after hyperosmotic shock.Regulation of NAB2 mRNA 3'-end formation requires the core exosome and the Trf4p component of the TRAMP complex.Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast.The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae.mRNA stability in the nucleus.Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic degradation of both nonsense-containing mRNAs and wild-type mRNAs.A nuclear degradation pathway controls the abundance of normal mRNAs in Saccharomyces cerevisiae.Coupling of termination, 3' processing, and mRNA exportMutant LYS2 mRNAs retained and degraded in the nucleus of Saccharomyces cerevisiaeNonsense-mediated mRNA decay in Saccharomyces cerevisiae: a quality control mechanism that degrades transcripts harboring premature termination codons.Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae.Immunity of the Saccharomyces cerevisiae SSY5 mRNA to nonsense-mediated mRNA decay.Linking nuclear mRNP assembly and cytoplasmic destiny.Yeast cap binding complex impedes recruitment of cleavage factor IA to weak termination sites.The multiple lives of NMD factors: balancing roles in gene and genome regulationmRNA journey to the cytoplasm: attire required.Two cap-binding proteins CBP20 and CBP80 are involved in processing primary MicroRNAs.NMD: a multifaceted response to premature translational termination.The methylproteome and the intracellular methylation network.mRNA quality control pathways in Saccharomyces cerevisiae.Cap-binding complex (CBC).At the revolution with Fred ShermanThe cap binding complex influences H2B ubiquitination by facilitating splicing of the SUS1 pre-mRNAThe interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast.Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap.The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex.Mass spectrometric identification of proteins that interact through specific domains of the poly(A) binding protein.The yeast cap binding complex modulates transcription factor recruitment and establishes proper histone H3K36 trimethylation during active transcription.Nuclear mRNA degradation tunes the gain of the unfolded protein response in Saccharomyces cerevisiae.eIF4G-an integrator of mRNA metabolism?DRN and TRAMP degrade specific and overlapping aberrant mRNAs formed at various stages of mRNP biogenesis in Saccharomyces cerevisiae.Functional genomics of lipid metabolism in the oleaginous yeast Rhodosporidium toruloides.
P2860
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P2860
The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
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2000年學術文章
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2000年學術文章
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name
The role of nuclear cap bindin ...... A termination and degradation.
@en
The role of nuclear cap bindin ...... A termination and degradation.
@nl
type
label
The role of nuclear cap bindin ...... A termination and degradation.
@en
The role of nuclear cap bindin ...... A termination and degradation.
@nl
prefLabel
The role of nuclear cap bindin ...... A termination and degradation.
@en
The role of nuclear cap bindin ...... A termination and degradation.
@nl
P2093
P2860
P1476
The role of nuclear cap bindin ...... A termination and degradation.
@en
P2093
P2860
P304
P356
10.1128/MCB.20.8.2827-2838.2000
P407
P577
2000-04-01T00:00:00Z