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]
S100-ß is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100-ß are mediated via its interaction with target proteins (1). S100-ß protein is a low molecular weight, EF-hand, Ca2(+)-binding protein widely distributed and conserved in the central nervous system of vertebrates (2). Measurements of Ca2+ binding to human brain S100-ß (beta beta) protein revealed six Ca2+-binding sites and zinc-binding studies on human S100b protein showed that the protein bound two zinc ions per beta monomer. These results indicate that the Ca2+- and Zn2+-binding sites on S100-ß protein are different and suggest that Zn2+ may regulate Ca2+ binding by increasing the affinity of the protein for calcium (3).
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