A monoclonal antibody to a multiphosphorylated, conformational epitope at the carboxy-terminus of p53
Laszlo Otvos,Ralf Hoffmann,Zhi Quan Xiang,Insug O,Hongying Deng,Maria Wysocka,Anne Marie Pease,Mark E. Rogers,Magdalena Blaszczyk-Thurin,Hildegund C.J. Ertl +9 more
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TL;DR: Antibody p53-18 appears to be a highly useful biochemical marker to detect low levels of p53 protein in different tissues, and to beA key tool to characterize the phosphorylation status of the C-terminus of p 53 protein originated from various sources.
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About: This article is published in Biochimica et Biophysica Acta. The article was published on 16 Sep 1998. and is currently open access. The article focuses on the topics: Epitope & Peptide sequence.
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Citations
A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element-binding protein.
Henri H. Versteeg,E. Nijhuis,G. R. van den Brink,Maaike W.A Evertzen,G. N. Pynaert,S. J. H. Van Deventer,P. J. Coffer,Maikel P. Peppelenbosch +7 more
TL;DR: Using phosphospecific antibodies, ELISA techniques enabling non-radioactive semi-quantitative assessment of the activation state of p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK,protein kinase B and the transcription factor cAMP-response-element-binding protein (CREB) in 96-well plates are developed.
Growth inhibition and apoptosis induction in ovarian cancer cells
TL;DR: A sensitivity profile for each ovarian carcinoma seems to be highly recommended before starting treatment, as both cell lines were rather resistant against gamma-irradiation and treatment with cisplatin and irinotecan whereas paclitaxel and gemcitabine resulted in a considerable reduction of the viability of the cancer cells.
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TL;DR: The major subunits of a class of PHFs are A68 proteins and the excessive or inappropriate phosphorylation of normal tau may change its apparent Mr, thus transforming tau into A68.
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TL;DR: Data indicate that, in addition to the transcriptional activation domain, the p53 proline-rich domain plays a critical role in the transmission of antiproliferative signals down-stream of the p 53 protein and may link p53 to a direct signal transduction pathway.
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