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]
Accumulation of the amyloid-beta (alphabeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. alphabeta peptide is generated by proteolytic cleavage of the β-amyloid protein precursor (APP) at beta- and gamma-sites by proteases. The long-sought β-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2) (1-4). BACE/Asp2 is a novel transmembrane aspartic protease and co-localizes with APP. A BACE homolog was recently cloned and designated BACE2, Asp1, DRAP (for Down region aspartic protease), and memapsin 1 (4-9). BACE2 also cleaves APP at b-site and at a different site within alphabeta (8). BACE2 locates on chromosome 21q22.3, the so-called ‘Down critical region’, suggesting that BACE2 and alphabeta may also contribute to the pathogenesis of Down syndrome (6,7)
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