Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression.
about
Nuclear import of the stem-loop binding protein and localization during the cell cycle.U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesisCombined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA bindingInteraction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline IsomerizationMolecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitinationMetabolism and regulation of canonical histone mRNAs: life without a poly(A) tailDistinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body.The stem-loop binding protein stimulates histone translation at an early step in the initiation pathway.Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.Ultrasensitive proteome analysis using paramagnetic bead technology.Structural basis for regulation of RNA-binding proteins by phosphorylation.Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Drosophila Symplekin localizes dynamically to the histone locus body and tricellular junctionsNickel and cadmium-induced SLBP depletion: A potential pathway to metal mediated cellular transformation.Histone storage and deposition in the early Drosophila embryo.FEM1 proteins are ancient regulators of SLBP degradation.Cyclin F-Mediated Degradation of SLBP Limits H2A.X Accumulation and Apoptosis upon Genotoxic Stress in G2FLASH, a proapoptotic protein involved in activation of caspase-8, is essential for 3' end processing of histone pre-mRNAs.Live-imaging of single stem cells within their niche reveals that a U3snoRNP component segregates asymmetrically and is required for self-renewal in Drosophila.
P2860
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P2860
Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
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2004年论文
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name
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@ast
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@en
type
label
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@ast
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@en
prefLabel
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@ast
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@en
P2093
P2860
P356
P1476
Drosophila stem-loop binding p ...... lated histone mRNA expression.
@en
P2093
David J Lanzotti
Jeremy M Kupsco
Robert J Duronio
William F Marzluff
Xiao-Cui Yang
Zbigniew Dominski
P2860
P304
P356
10.1091/MBC.E03-09-0649
P577
2004-03-01T00:00:00Z