Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Edith C. Wolff"'
Autor:
Myung Hee Park, Edith C. Wolff
Publikováno v:
Journal of Biological Chemistry. 293:18710-18718
The natural amino acid hypusine (N(ϵ)-4-amino-2-hydroxybutyl(lysine)) is derived from the polyamine spermidine, and occurs only in a single family of cellular proteins, eukaryotic translation factor 5A (eIF5A) isoforms. Hypusine is formed by conjuga
Publikováno v:
Amino Acids. 49:1793-1804
Deoxyhypusine synthase (DHS) catalyzes the post-translational modification of eukaryotic translation factor 5A (eIF5A) by the polyamine, spermidine, that converts one specific lysine residue to deoxyhypusine [N e -4-aminobutyl(lysine)], which is subs
Publikováno v:
Journal of Biological Chemistry. 282:8300-8308
Deoxyhypusine hydroxylase (DOHH) is a novel metalloenzyme that catalyzes the final step of the post-translational synthesis of hypusine (Nepsilon-(4-amino-2-hydroxybutyl)lysine) in the eukaryotic translation initiation factor 5A (eIF5A). Hypusine syn
Publikováno v:
Journal of Biological Chemistry. 279:28697-28705
Deoxyhypusine synthase catalyzes the first step in the two-step post-translational synthesis of hypusine, which is uniquely present in eukaryotic initiation factor 5A (eIF5A). Deoxyhypusine synthase and eIF5A are conserved throughout the eukaryotic k
Autor:
Myung Hee Park, Zeljka Smit-McBride, C. Allen Henderson, Edith C. Wolff, John W.B. Hershey, Paul M. J. Clement, Hans E. Johansson, Zandra A. Jenkins
Publikováno v:
European Journal of Biochemistry. 270:4254-4263
The phylogenetically conserved eukaryotic translation initiation factor 5A (eIF5A) is the only known cellular protein to contain the post-translationally derived amino acid hypusine [Ne-(4-amino-2-hydroxybutyl)lysine]. Both eIF5A and its hypusine mod
Autor:
Edith C. Wolff, Myung Hee Park
Publikováno v:
Polyamines ISBN: 9784431552116
Although polyamines exert various effects on nucleic acids and macromolecular synthesis as polycations, spermidine is covalently incorporated into a single protein, eukaryotic initiation factor 5A (eIF5A), through a unique posttranslational modificat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ebdc575aa258de18e0ac7101fe827fa2
https://doi.org/10.1007/978-4-431-55212-3_10
https://doi.org/10.1007/978-4-431-55212-3_10
Publikováno v:
Translation and Its Regulation in Cancer Biology and Medicine ISBN: 9789401790772
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::907f012341616ee4b05940256e5091c5
https://doi.org/10.1007/978-94-017-9078-9_10
https://doi.org/10.1007/978-94-017-9078-9_10
Publikováno v:
Journal of Biological Chemistry. 275:9170-9177
Deoxyhypusine is a modified lysine residue. It is formed posttranslationally in the precursor of eukaryotic initiation factor 5A (eIF5A) by deoxyhypusine synthase, employing spermidine as a butylamine donor. In the initial step of this reaction, deox
Publikováno v:
Biochemical Journal. 340:273-281
Deoxyhypusine synthase catalyses the first step in the post-translational synthesis of hypusine [Nϵ-(4-amino-2-hydroxybutyl) lysine] in a single cellular protein, the precursor of eukaryotic initiation factor 5A (eIF5A). Deoxyhypusine synthase exist
Autor:
Edith C. Wolff, Myung Hee Park
Publikováno v:
Yeast. 15:43-50
The posttranslational formation of deoxyhypusine in the precursor of eukaryotic initiation factor 5A (eIF5A) is catalysed by deoxyhypusine synthase. This NAD-dependent reaction involves transfer of the 4-aminobutyl moiety of spermidine to a single ly