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]
This gene encodes tumor protein p53, which responds to diverse cellular stresses to regulate target genes that induce cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. p53 protein is expressed at low level in normal cells and at a high level in a variety of transformed cell lines, where it's believed to contribute to transformation and malignancy. p53 is a DNA-binding protein containing transcription activation, DNA-binding, and oligomerization domains. It is postulated to bind to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Alterations of this gene occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome. Multiple p53 variants due to alternative promoters and multiple alternative splicing have been found. These variants encode distinct isoforms, which can regulate p53 transcriptional activity. [provided by RefSeq].
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Western blot of rat brain nuclear fraction lysate showing specific immunolabeling of the ~53k p53 phosphorylated at Ser392 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: λ-Ptase). The blot is identical to the control except that it was incubated in λ-Ptase (1200 units for 30 min) before being exposed to the phospho Ser392 p53 antibody. The immunolabeling is completely eliminated by treatment with λ-Ptase.
Western blot of rat brain nuclear fraction lysate showing specific immunolabeling of the ~53k p53 phosphorylated at Ser392 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: λ-Ptase). The blot is identical to the control except that it was incubated in λ-Ptase (1200 units for 30 min) before being exposed to the phospho Ser392 p53 antibody. The immunolabeling is completely eliminated by treatment with λ-Ptase.
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