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Rauen T Benedyk K Juang YT Kerkhoff C Kyttaris VC Roth J Tsokos GC Tenbrock K 《The Journal of biological chemistry》2011,286(37):32366-32372
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Transcription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cells.
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Okot Nyormoi Zhi Wang Dao Doan Maribelis Ruiz David McConkey Menashe Bar-Eli 《Molecular and cellular biology》2001,21(15):4856-4867
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Eugenia Mata-Greenwood Wu-xiang Liao Wen Wang Jing Zheng Dong-bao Chen 《The Journal of biological chemistry》2010,285(23):17348-17358
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Fabbi M Marimpietri D Martini S Brancolini C Amoresano A Scaloni A Bargellesi A Cosulich E 《Cell death and differentiation》1999,6(10):992-1001
Tissue transglutaminase (tTG) is a Ca2+-dependent cross-linking enzyme that participates in the apoptotic machinery by irreversibly assembling a protein scaffold that prevents the leakage of intracellular components. In the present study a single-chain antibody fragment (scFv) detecting tTG is described. We demonstrate that TG/F8 scFv, selected from a phase display library of human V-gene segments by binding to guinea-pig liver tTG, can react with human tTG both in Western blot and in immunohistochemistry. The specific detection of tTG by TG/F8 in human thymocytes is verified by mass spectrometric analysis of the purified protein. Furthermore, we demonstrate that in lymphoid cells tTG is cleaved by caspase 3 during the late phase of apoptotic death, concomitant to DNA fragmentation, and that such cleavage causes loss of cross-linking function. We propose tTG cleavage as a valuable biochemical marker of caspase 3 activation during the late execution phase of apoptosis. 相似文献
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