Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis
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Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent.Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiaeThe importance of conserved features of yeast actin-binding protein 1 (Abp1p): the conditional nature of essentialityThe role of eIF5A in epidermal growth factor-induced proliferation of corneal epithelial cell association with PI3-k/Akt activation.Characterization of a eukaryotic translation initiation factor 5A homolog from Tamarix androssowii involved in plant abiotic stress tolerance.eIF5A promotes translation elongation, polysome disassembly and stress granule assemblyFunctional significance of eIF5A and its hypusine modification in eukaryotesEvidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site.The hypusine-containing translation factor eIF5A.Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity.eIF5A interacts functionally with eEF2.Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the RibosomeMammalian polyamine metabolism and functioneIF5A and EF-P: two unique translation factors are now traveling the same road.Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis.EF-P dependent pauses integrate proximal and distal signals during translation.eIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer.Eukaryotic initiation factor 5A dephosphorylation is required for translational arrest in stationary phase cells.eIF5A has a function in the cotranslational translocation of proteins into the ER.Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A)
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P2860
Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 March 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Structural modeling and mutati ...... volvement in protein synthesis
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Structural modeling and mutati ...... olvement in protein synthesis.
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type
label
Structural modeling and mutati ...... volvement in protein synthesis
@en
Structural modeling and mutati ...... olvement in protein synthesis.
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Structural modeling and mutati ...... volvement in protein synthesis
@en
Structural modeling and mutati ...... olvement in protein synthesis.
@nl
P2093
P2860
P1433
P1476
Structural modeling and mutati ...... volvement in protein synthesis
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P2093
Camila A O Dias
Cleslei F Zanelli
Luciano H Apponi
Mariana C Frigieri
Myung H Park
Richard C Garratt
Suzana M Rangel
Veridiana S P Cano
Wanius Garcia
P2860
P304
P356
10.1111/J.1742-4658.2008.06345.X
P407
P577
2008-03-13T00:00:00Z