Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification - Test2 - elhamkhani - TriplyDB

Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification

Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification

http://www.wikidata.org/entity/Q24650882

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Crystal structure of human eIF5A1: insight into functional similarity of human eIF5A1 and eIF5A2 Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent.eIF5A promotes translation elongation, polysome disassembly and stress granule assembly Functional significance of eIF5A and its hypusine modification in eukaryotes Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site.Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A.The hypusine-containing translation factor eIF5A.A tumour suppressor network relying on the polyamine-hypusine axis.Inactivation of eukaryotic initiation factor 5A (eIF5A) by specific acetylation of its hypusine residue by spermidine/spermine acetyltransferase 1 (SSAT1).Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.Hypusination of eukaryotic initiation factor 5A via cAMP-PKA-ERK1/2 pathway is required for ligand-induced downregulation of LH receptor mRNA expression in the ovary.The effect of hypusine modification on the intracellular localization of eIF5A.Unique modifications of translation elongation factors.eIF5A and EF-P: two unique translation factors are now traveling the same road.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis.Protein-protein-interaction network organization of the hypusine modification system.EF-P dependent pauses integrate proximal and distal signals during translation.Synthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeast.eIF5A is required for autophagy by mediating ATG3 translation

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P2860

Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification

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2008 nî lūn-bûn

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2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

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Mutational analyses of human e ...... vity and hypusine modification

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C Allen Henderson

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Geoung A Jeon

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Hans E Johansson

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Jong-Hwan Park

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Myung Hee Park

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Sandro R Valentini

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Veridiana S P Cano

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P2860

Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes

Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A

Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme.

Identification and characterization of eukaryotic initiation factor 5A-2

Identification of mRNA that binds to eukaryotic initiation factor 5A by affinity co-purification and differential display

Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 Rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification

Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5

Identification of the eukaryotic initiation factor 5A as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II

Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins

Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor

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