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]
Prion diseases are transmissible neurodegenerative disorders which affect a range of mammalian species. In humans they can be inherited and sporadic as well as acquired by exposure to human prions. Prions appear to be composed principally of a conformational isomer of host-encoded prion protein and propagate by recruitment of cellular prion protein (1). The function of the cellular prion protein (PrP) is still poorly understood. It has been proposed that one unprecedented role for PrP is against Bax-mediated neuronal apoptosis. It has been shown that PrP potently inhibits Bax-induced cell death in human primary neurons (2). An impaired synaptic inhibition may be involved in the epileptiform activity seen in Creutzfeldt-Jakob and other neurodegenerative diseases and it is believed that loss of function of PrP may contribute to the early synaptic loss and neuronal degeneration seen in these diseases (3).
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