About: The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1

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rdf:type	Item
description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) наукова стаття, опублікована в жовтні 1996 (uk) 1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած (hyw) 1996 թվականի հոտեմբերին հրատարակված գիտական հոդված (hy) article scientifique publié en 1996 (fr) scientific journal article (en) im Oktober 1996 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 1996/10/14) (sk) مقالة علمية (نشرت في 14-10-1996) (ar) wetenschappelijk artikel (gepubliceerd op 1996/10/14) (nl) 1996 ഒക്ടോബര്‍ 14 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
publication date	wds:Q28504697-F022B32A-E9C4-406E-9F6B-65262EEEDBCC
publication date	1996-10-14 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28504697-7F317744-CEDD-4BD0-917F-AE2DAF49A619
language of work or name	English
cites work	wds:Q28504697-00C62BC0-3911-4FCD-BD3A-1138E1DBCAB4 wds:Q28504697-0620A1C7-8795-43E1-85FA-435250906958 wds:Q28504697-0F025D21-E052-4AB8-9695-F480C992ED5E wds:Q28504697-2AFEB9FC-6542-43F5-8C6D-0B7784BF59FC wds:Q28504697-2D0BC46A-DE82-48BB-BFDB-62052D90EB12 wds:Q28504697-367C7422-D08D-4956-9983-13A224665CBC wds:Q28504697-4A04272A-B590-49E7-8774-601B44B323A9 wds:Q28504697-C5003AAE-9F76-4EF5-9966-D8CE0ED663CA wds:Q28504697-C57C617C-D72F-4CC2-B077-ED91C6C47854 wds:Q28504697-E8A5E7AC-3976-497C-BA64-00CB9E58ECD7 wds:Q28504697-F7C6969F-5D91-4031-8C1B-9AFAED085278
cites work	Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 DNA sequencing with chain-terminating inhibitors Basic local alignment search tool Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning A channeled tRNA cycle during mammalian protein synthesis The cytoskeleton and mRNA localization Channeling of aminoacyl-tRNA for protein synthesis in vivo Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase Association of methionyl-tRNA synthetase with detergent-insoluble components of the rough endoplasmic reticulum Association of an aminoacyl-tRNA synthetase complex and of phenylalanyl-tRNA synthetase with the cytoskeletal framework fraction from mammalian cells
author name string	wds:Q28504697-4B010CAD-1919-454E-B10D-C06F69B95295 wds:Q28504697-F34F5BE8-95B9-4E73-B6DD-5FC9D92E81F9
author name string	M. Mirande S. Quevillon
rdfs:label	The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (en) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (nl) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (ast)
skos:prefLabel	The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (en) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (nl) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (ast)
name	The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (en) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (nl) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (ast)
title	wds:Q28504697-660AC90B-CF86-40E6-9DD5-101A1E26782A
title	The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1 (en)
page(s)	wds:Q28504697-F3310341-4262-4B76-8EF0-FA23C6B47DB9
page(s)	63–67
instance of	wds:Q28504697-49F1C84E-9E8C-418F-A576-C59B8B5DB610
instance of	scholarly article
main subject	wds:Q28504697-D0047B34-0887-4AE3-A971-D17DAC1B8988
main subject	Eukaryotic translation elongation factor 1 epsilon 1
PubMed ID	wds:Q28504697-AED9AF64-4DD9-4502-82F4-001BD23CA8F7
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8849690
PubMed ID	8849690
published in	wds:Q28504697-D3B6E96F-BBB8-48D0-9280-4B4B39177E23
published in	FEBS Letters
issue	wds:Q28504697-C847F8C2-3A96-459E-B42B-CE4DAEC826E9
volume	wds:Q28504697-CFC83A3D-1798-4F3F-AC79-CC5AD600809E
issue	1
volume	395
DOI	wds:Q28504697-BA892663-D0F9-4CB7-8B4F-EA1DD75B3DA7
DOI	http://dx.doi.org/10.1016/0014-5793(96)01005-8
DOI	10.1016/0014-5793(96)01005-8
ResearchGate publication ID	wds:Q28504697-62E208CA-EFD1-4CA7-ACBF-ADF0D668CB68
ResearchGate publication ID	14355113
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28504697
is cites work of	Ultrastructure of the eukaryotic aminoacyl-tRNA synthetase complex derived from two dimensional averaging and classification of negatively stained electron microscopic images. Immunoelectron microscopic localization of glutamyl-/ prolyl-tRNA synthetase within the eukaryotic multisynthetase complex An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase Functional Interaction of Mammalian Valyl-tRNA Synthetase with Elongation Factor EF-1α in the Complex with EF-1H Activation and regulation of ATM kinase activity in response to DNA double-strand breaks Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex. Aminoacyl tRNA synthetases and their connections to disease Mammalian aminoacyl-tRNA synthetases: cell signaling functions of the protein translation machinery p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed Building arks for tRNA: structure and function of the Arc1p family of non-catalytic tRNA-binding proteins Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43 Aminoacyl-tRNA synthetase complexes in evolution

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