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Mutational analyses of human eIF5A-1-identification of amino acid residues critical for eIF5A activity and hypusine modification
(Blackwell Publishing, 2008-01-01)
The eukaryotic translation initiation factor 5A (eIF5A) is the only protein that contains hypusine [N-epsilon-(4-amino-2-hydroxybutyl)lysine], which is required for its activity. Hypusine is formed by post-translational ...
Akt/PKB: one kinase, many modifications
(Portland Press, 2015-06)
Akt/PKB, a serine/threonine kinase member of the AGC family of proteins, is involved in the regulation of a plethora of cellular processes triggered by a wide diversity of extracellular signals and is thus considered a key ...
Biophysical and Structural Characterization of the Recombinant Human eIF3L
(Bentham Science Publ Ltd, 2014-01-01)
The eukaryotic translation initiation factor 3, subunit L (eIF3L) is one of the subunits of the eIF3 complex, an accessory protein of the Polymerase I enzyme and may have an important role in the Flavivirus replication by ...
Biophysical and structural characterization of the recombinant human eIF3L
(2014-01-01)
The eukaryotic translation initiation factor 3, subunit L (eIF3L) is one of the subunits of the eIF3 complex, an accessory protein of the Polymerase I enzyme and may have an important role in the Flavivirus replication by ...
Modification of Akt by SUMO conjugation regulates alternative splicing and cell cycle
(Landes Bioscience, 2013-08)
Akt/PKB is a key signaling molecule in higher eukaryotes and a crucial protein kinase in human health and disease. Phosphorylation, acetylation, and ubiquitylation have been reported as important regulatory post-translational ...
Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193
(Elsevier Science Inc., 2019-09)
Peroxiredoxins (Prx) are enzymes that efficiently reduce hydroperoxides through active participation of cysteine residues (CP, CR). The first step in catalysis, the reduction of peroxide substrate, is fast, 107 - 108 M−1s−1 ...
Biophysical and Structural Characterization of the Recombinant Human eIF3L
(Bentham Science Publ Ltd, 2014)