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PubMed:14709557 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-164 Sentence denotes Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398.
T2 165-307 Sentence denotes Protein synthesis consumes a high proportion of the metabolic energy of mammalian cells, and most of this is used by peptide chain elongation.
T3 308-422 Sentence denotes An important regulator of energy supply and demand in eukaryotic cells is the AMP-activated protein kinase (AMPK).
T4 423-668 Sentence denotes The rate of peptide chain elongation can be modulated through the phosphorylation of eukaryotic elongation factor (eEF) 2, which inhibits its activity and is catalyzed by a specific calcium/calmodulin-dependent protein kinase termed eEF2 kinase.
T5 669-828 Sentence denotes Here we show that AMPK directly phosphorylates eEF2 kinase, and we identify the major site of phosphorylation as Ser-398 in a regulatory domain of eEF2 kinase.
T6 829-915 Sentence denotes AMPK also phosphorylates two other sites (Ser-78 and Ser-366) in eEF2 kinase in vitro.
T7 916-1136 Sentence denotes We develop appropriate phosphospecific antisera and show that phosphorylation of Ser-398 in eEF2 kinase is enhanced in intact cells under a range of conditions that activate AMPK and increase the phosphorylation of eEF2.
T8 1137-1212 Sentence denotes Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells.
T9 1213-1379 Sentence denotes Although cardiomyocytes appear to contain a distinct isoform of eEF2 kinase, it also contains a site corresponding to Ser-398 that is phosphorylated by AMPK in vitro.
T10 1380-1491 Sentence denotes Stimuli that activate AMPK and increase eEF2 phosphorylation within cells increase the activity of eEF2 kinase.
T11 1492-1651 Sentence denotes Thus, AMPK and eEF2 kinase may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy.