tailieunhanh - Báo cáo y học: "System in biology leading to cell pathology: stable proteinprotein interactions after covalent modifications by small molecules or in transgenic cells"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: System in biology leading to cell pathology: stable proteinprotein interactions after covalent modifications by small molecules or in transgenic cells | JOURNAL OF BIOMEDICAL SCIENCE System in biology leading to cell pathology stable proteinprotein interactions after covalent modifications by small molecules or in transgenic cells Malina Malina Journal of Biomedical Science 2011 18 7 http content 18 V7 19 January 2011 2 BioMed Central Malina Journal of Biomedical Science 2011 18 7 http content 18 1 7 The cost of publication in Journal of Biomedical Science Is borne by the National Science Council Taiwan JOURNAL OF BIOMEDICAL SCIENCE RESEARCH Open Access System in biology leading to cell pathology stable protein-protein interactions after covalent modifications by small molecules or in transgenic cells Halina Z Malina Abstract Background The physiological processes in the cell are regulated by reversible electrostatic protein-protein interactions. Apoptosis is such a regulated process which is critically important in tissue homeostasis and development and leads to complete disintegration of the cell. Pathological apoptosis a process similar to apoptosis is associated with aging and infection. The current study shows that pathological apoptosis is a process caused by the covalent interactions between the signaling proteins and a characteristic of this pathological network is the covalent binding of calmodulin to regulatory sequences. Results Small molecules able to bind covalently to the amino group of lysine histidine arginine or glutamine modify the regulatory sequences of the proteins. The present study analyzed the interaction of calmodulin with the BH3 sequence of Bax and the calmodulin-binding sequence of myristoylated alanine-rich C-kinase substrate in the presence of xanthurenic acid in primary retinal epithelium cell cultures and murine epithelial fibroblast cell lines transformed with SV40 wild type WT Bid knockout Bid- - and Bax- - Bak- - double knockout DKO . Cell death was observed to be associated with the covalent binding of calmodulin in parallel to the .

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