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]
A phospho specific peptide corresponding to residues surrounding serine 889 of human NMDAR1 was used as an immunogen. This antibody detects NMDAR1 phosphorylated at serine 889.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
The NMDA (N-methyl D-aspartate) receptors in the brain play a critical role in synaptic plasticity, synaptogenesis and excitotoxicity. Molecular cloning has demonstrated that NMDA receptors consist of several homologous subunits (NMDAR1). A variety of studies have suggested that protein phosphorylation of NMDA receptors may regulate their function and play a role in many forms of synaptic plasticity such as long-term potentiation. PKC phosphorylation occurs on several distinct sites on the NR1 subunit. Most of these sites are contained within a single alternatively spliced exon in the C-terminal domain, which has previously been proposed to be on the extracellular side of the membrane (1). A role for NMDAR1 in the molecular pathology underlying Huntington disease (HD) has been proposed on the basis of neurochemical studies in HD and the ability of the NMDAR1 to mediate neuronal cell death (2). Also, studies reveal a unrecognized role of the NMDAR1 in dynamically maintaining the long-term synaptic stability of memory storage circuits in the brain (3).
Related Pathway
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