She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
about
ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctionsThe composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAsArchitecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteinsAn exclusively nuclear RNA-binding protein affects asymmetric localization of ASH1 mRNA and Ash1p in yeastCis-acting determinants of asymmetric, cytoplasmic RNA transportFusion to GFP blocks intercellular trafficking of the sucrose transporter SUT1 leading to accumulation in companion cellsWidespread mRNA association with cytoskeletal motor proteins and identification and dynamics of myosin-associated mRNAs in S. cerevisiaeStructure of a myosinbulletadaptor complex and pairing by cargoProteome-wide search reveals unexpected RNA-binding proteins in Saccharomyces cerevisiaeWidespread cytoplasmic mRNA transport in yeast: identification of 22 bud-localized transcripts using DNA microarray analysis.Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.ASH1 mRNA localization in three acts.A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization.Association of the yeast RNA-binding protein She2p with the tubular endoplasmic reticulum depends on membrane curvature.The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast.Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of mitochondria in the budding yeastMyo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae.The SESA network links duplication of the yeast centrosome with the protein translation machinery.A cytoplasmic complex mediates specific mRNA recognition and localization in yeastCharacterization of rat BLOS2/Ceap, a putative yeast She3 homolog, as interaction partner of apoptosis antagonizing transcription factor/Che-1mRNA on the move: the road to its biological destiny.In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation.In the right place at the right time: visualizing and understanding mRNA localization.Identification of a conserved RNA motif essential for She2p recognition and mRNA localization to the yeast bud.Unbiased selection of localization elements reveals cis-acting determinants of mRNA bud localization in Saccharomyces cerevisiae.Discovery of a mRNA mitochondrial localization element in Saccharomyces cerevisiae by nonhomologous random recombination and in vivo selectionAn RNA transport system in Candida albicans regulates hyphal morphology and invasive growthCoupling of two non-processive myosin 5c dimers enables processive stepping along actin filaments.Multiple Myo4 motors enhance ASH1 mRNA transport in Saccharomyces cerevisiae.Single-mRNA counting using fluorescent in situ hybridization in budding yeastCo-transcriptional recruitment of Puf6 by She2 couples translational repression to mRNA localization.Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells.RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex.Walking to work: roles for class V myosins as cargo transporters.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Inducible control of subcellular RNA localization using a synthetic protein-RNA aptamer interaction.Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport.mRNA localization mechanisms in Trypanosoma cruziPolarized growth and organelle segregation in yeast: the tracks, motors, and receptors.Modular assembly of designer PUF proteins for specific post-transcriptional regulation of endogenous RNA
P2860
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P2860
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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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
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
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2000年学术文章
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2000年學術文章
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name
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@ast
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@en
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@nl
type
label
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@ast
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@en
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@nl
prefLabel
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@ast
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@en
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@nl
P2093
P2860
P356
P1433
P1476
She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.23.6592
P407
P577
2000-12-01T00:00:00Z