A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum
about
PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activatorsCharacterization of Staufen 1 ribonucleoprotein complexesThe host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminusMammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granulesThe composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAsThe double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: evidence for a role in genomic RNA encapsidationMolecular mapping of the determinants involved in human Staufen-ribosome associationIdentification of two RNA-binding proteins associated with human telomerase RNAInteraction of Staufen1 with the 5' end of mRNA facilitates translation of these RNAsScp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner.Assignment of protein function and discovery of novel nucleolar proteins based on automatic analysis of MEDLINEThe interactomes of influenza virus NS1 and NS2 proteins identify new host factors and provide insights for ADAR1 playing a supportive role in virus replicationH19 RNA binds four molecules of insulin-like growth factor II mRNA-binding proteinIRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L proteinThe RNA-binding protein Staufen from rat brain interacts with protein phosphatase-1Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motorStaufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytesTwo rat brain staufen isoforms differentially bind RNAThe zinc-finger protein ZFR is critical for Staufen 2 isoform specific nucleocytoplasmic shuttling in neuronsHuD distribution changes in response to heat shock but not neurotrophic stimulationlncRNAs transactivate STAU1-mediated mRNA decay by duplexing with 3' UTRs via Alu elementsThe RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicingTwo distinct Staufen isoforms in Xenopus are vegetally localized during oogenesis.Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neuronsGenetic analysis of influenza virus NS1 gene: a temperature-sensitive mutant shows defective formation of virus particles.A yEGFP-based reporter system for high-throughput yeast two-hybrid assay by flow cytometry.Analysis of the interaction of influenza virus polymerase complex with human cell factors.Genomic characterization of Wilms' tumor suppressor 1 targets in nephron progenitor cells during kidney development.Protein synthesis shut-off induced by influenza virus infection is independent of PKR activityA novel murine Staufen isoform modulates the RNA content of Staufen complexes.Protein synthesis in the dendrite.Distinct roles of two conserved Staufen domains in oskar mRNA localization and translationInsights into mRNA transport in neurons.Isolation and characterization of Staufen-containing ribonucleoprotein particles from rat brain.HIV-1 transcripts use IRES-initiation under conditions where Cap-dependent translation is restricted by poliovirus 2A proteasehiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1.Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent manner to recruit UPF1 for rapid mRNA degradation.Neuronal activity induces synaptic delivery of hnRNP A2/B1 by a BDNF-dependent mechanism in cultured hippocampal neurons.Human Staufen1 associates to miRNAs involved in neuronal cell differentiation and is required for correct dendritic formationRNA-binding proteins in early development.
P2860
Q24291569-32412910-F1E5-4635-B6F8-21FD18DC14AAQ24300881-D4C213A6-FFA9-4A38-BDE9-0463342C3626Q24315925-D74F0EDB-8CA2-49A6-91EF-505941A739BDQ24338191-C7512890-CD17-4C05-B446-4A21FEDFBE28Q24338478-FBEEED03-53A0-4658-9829-19ADA1AE0FE5Q24525207-509C6518-B522-4247-AEA0-3F7B73D7D5D2Q24534331-2577C350-A5DB-4593-8977-CFC54CC28297Q24548517-22EAB254-4FE0-4B61-8D6B-50D2ACE6F88FQ24816776-954CFB96-3930-4A49-A5BB-965EEF447865Q27932288-17CBC928-F312-4F84-89EE-1D59D90CC088Q27967929-0D910D9D-6B2A-4E74-9645-35D0E0B79463Q28115759-8E59D99F-15AA-4A35-8667-E31350A8442FQ28139674-B594D8A7-38B5-438C-8C5B-9F37A8768629Q28140837-34418B37-9F96-4FC5-B397-9C4C699BCEBDQ28204595-1CEF78E6-A77E-4364-9C08-AFBC59E30B18Q28216333-543A56F9-7009-473A-9F69-AF121011411FQ28572768-BEF700B5-64E1-43FE-AA3E-7866C0694D7FQ28573755-95C33AD8-1BCA-407A-ABCF-3E9BEBA0CF60Q28577459-69D9DEAD-2BDA-4AD3-B766-74EAEF9DCABCQ28577653-31152B6E-2F27-477F-A8EA-82DE6BE94BA9Q29617832-6249FB5E-EBE9-490C-BA36-9B43B07EC11CQ30424920-7F6183AF-7010-44AC-BD8E-2E721AF63921Q30447063-48C7B283-ED4A-4083-99CC-9B4A73841599Q30483753-F9775622-FB28-4AA8-A877-5F9884556706Q33227755-0ECDFE4D-962E-41D3-AF69-CDDB797D1ACEQ33321653-F32DE59E-6729-4FC5-9E8B-0D1F112064A3Q33336123-9C3632D7-A2BD-4629-B199-250CBD4013FBQ33714250-35200883-72E0-488B-B6E4-C7379D7E016AQ33874625-39823F3E-24EC-4747-9671-490D17024D17Q33964811-541B6A18-3426-4954-A036-B4DD70187BB2Q34655817-D0EEDA89-E894-4B5E-99CD-44B12659F1BBQ34668374-5C475F6C-758D-442F-AFF3-5B9E9C72E670Q34760294-9D6D0365-A497-4D7B-91FA-4D3702947B33Q34763540-42DFBC4C-22F5-4732-B01E-9EF307306AC4Q35092875-C7EC5241-B4D8-41E6-97C3-D4A738253F2EQ35224643-29AB42BF-B87E-45D6-B89D-5CB1586D4862Q35280346-0F3BFAD9-2CB4-4BB0-B1E8-E1C96867FA51Q35305075-8AB48885-54CA-4101-BAD2-BFF338B7287DQ35448741-BAC33604-F557-4DED-A57E-28D35258AE60Q36086066-80C7CF4A-64CC-4760-BEE4-3FFF07E741D9
P2860
A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
A human sequence homologue of ...... he rough endoplasmic reticulum
@ast
A human sequence homologue of ...... he rough endoplasmic reticulum
@en
A human sequence homologue of ...... he rough endoplasmic reticulum
@nl
type
label
A human sequence homologue of ...... he rough endoplasmic reticulum
@ast
A human sequence homologue of ...... he rough endoplasmic reticulum
@en
A human sequence homologue of ...... he rough endoplasmic reticulum
@nl
prefLabel
A human sequence homologue of ...... he rough endoplasmic reticulum
@ast
A human sequence homologue of ...... he rough endoplasmic reticulum
@en
A human sequence homologue of ...... he rough endoplasmic reticulum
@nl
P2093
P2860
P3181
P356
P1476
A human sequence homologue of ...... he rough endoplasmic reticulum
@en
P2093
P2860
P304
P3181
P356
10.1128/MCB.19.3.2212
P407
P577
1999-03-01T00:00:00Z