eEF1A is a novel component of the mammalian nuclear protein export machinery - Test2 - elhamkhani - TriplyDB

eEF1A is a novel component of the mammalian nuclear protein export machinery

eEF1A is a novel component of the mammalian nuclear protein export machinery

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The translation elongation factor eEF1A1 couples transcription to translation during heat shock response Nuclear relocalisation of cytoplasmic poly(A)-binding proteins PABP1 and PABP4 in response to UV irradiation reveals mRNA-dependent export of metazoan PABPs The eEF1A Proteins: At the Crossroads of Oncogenesis, Apoptosis, and Viral Infections Regulation of tRNA bidirectional nuclear-cytoplasmic trafficking in Saccharomyces cerevisiae.Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutations Elevated copper remodels hepatic RNA processing machinery in the mouse model of Wilson's disease A structural domain mediates attachment of ethanolamine phosphoglycerol to eukaryotic elongation factor 1A in Trypanosoma brucei Eukaryotic translation elongation factor 1-alpha 1 inhibits p53 and p73 dependent apoptosis and chemotherapy sensitivity Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation.C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2 eEF1A: thinking outside the ribosome Proteins modified by the lipid peroxidation aldehyde 9,12-dioxo-10(E)-dodecenoic acid in MCF7 breast cancer cells.Multiple Orientia tsutsugamushi ankyrin repeat proteins interact with SCF1 ubiquitin ligase complex and eukaryotic elongation factor 1 α.The eukaryotic elongation factor eEF1A1 interacts with SAMHD1.Uncovering the salt response of soybean by unraveling its wild and cultivated functional genomes using tag sequencing.Consecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm.The eukaryotic elongation factor 1A is critical for genome replication of the paramyxovirus respiratory syncytial virus.Ethanolamine phosphoglycerol attachment to eEF1A is not essential for normal growth of Trypanosoma brucei The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities.Characterization of VHL missense mutations in sporadic clear cell renal cell carcinoma: hotspots, affected binding domains, functional impact on pVHL and therapeutic relevance The regulation of AβPP expression by RNA-binding proteins The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis Nuclear relocalization of polyadenylate binding protein during rift valley fever virus infection involves expression of the NSs gene Subcellular dynamics of the VHL tumor suppressor: on the move for HIF degradation.VHL missense mutations in the p53 binding domain show different effects on p53 signaling and HIFα degradation in clear cell renal cell carcinoma.Unique modifications of translation elongation factors.Effector glycosyltransferases in legionella.From global phosphoproteomics to individual proteins: the case of translation elongation factor eEF1A.Cutaneous human papillomavirus type 38 E7 regulates actin cytoskeleton structure for increasing cell proliferation through CK2 and the eukaryotic elongation factor 1A.Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.Visualizing protein interactions involved in the formation of the 42S RNP storage particle of Xenopus oocytes.Isolation and characterization of three cassava elongation factor 1 alpha (MeEF1A) promoters.An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins Identification of proteins from prunus persica that interact with peach latent mosaic viroid.Adding structural information to the von Hippel-Lindau (VHL) tumor suppressor interaction network.Regulation of the transcriptional activation of the androgen receptor by the UXT-binding protein VHL.Role of the Y-located putative gonadoblastoma gene in human spermatogenesis.TIMAP, the versatile protein phosphatase 1 regulator in endothelial cells.Expanded polyalanine tracts function as nuclear export signals and promote protein mislocalization via eEF1A1 factor.Structural rationale for the cross-resistance of tumor cells bearing the A399V variant of elongation factor eEF1A1 to the structurally unrelated didemnin B, ternatin, nannocystin A and ansatrienin B.

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P2860

eEF1A is a novel component of the mammalian nuclear protein export machinery

http://www.wikidata.org/entity/Q24651660

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

eEF1A is a novel component of the mammalian nuclear protein export machinery

@ast

eEF1A is a novel component of the mammalian nuclear protein export machinery

@en

eEF1A is a novel component of the mammalian nuclear protein export machinery

@nl

type

label

eEF1A is a novel component of the mammalian nuclear protein export machinery

@ast

eEF1A is a novel component of the mammalian nuclear protein export machinery

@en

eEF1A is a novel component of the mammalian nuclear protein export machinery

@nl

prefLabel

eEF1A is a novel component of the mammalian nuclear protein export machinery

@ast

eEF1A is a novel component of the mammalian nuclear protein export machinery

@en

eEF1A is a novel component of the mammalian nuclear protein export machinery

@nl

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MBC.E08-06-0562

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Molecular Biology of the Cell

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eEF1A is a novel component of the mammalian nuclear protein export machinery

@en

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Arnim Pause

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Karine Pilon-Larose

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Stephen Lee

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P2860

Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p

T RANSPORT B ETWEEN THE C ELL N UCLEUS AND THE C YTOPLASM

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins

The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm

Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport

Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1

Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor protein

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5296-5308

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scholarly article

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4055357

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10.1091/MBC.E08-06-0562

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12

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19

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Mireille Khacho

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2008-09-17T00:00:00Z

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18799616

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2592675

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