Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
Eukaryotic elongation factor-2 kinase (eEF-2k) previously known as Ca2+/calmodulin-dependent protein kinase III, is an abundant cytoplasmic protein highly specific for elongation factor-2 (eEf-2) (1). Phosphorylation of eEF-2 by eEF-2 kinase on specific threonine residues results in the inactivation of eEF-2 and in termination of mRNA translation (2). The activity of eEF2 kinase is not only dependent upon Ca2+ ions, calmodulin (CaM) and insulin, but is also regulated both negatively and positively via phosphorylation by different protein kinases (AMPK, S6K1, p90 RSK) (3-4). There is also evidence that eEF-2 phosphorylation is involved in the regulation of cell cycle progression, cellular differentiation, oogensis and malignant tumors (5-6).
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