Modeling the Critical Activation of Chaperone Machinery in Protein Folding
| Autor: | Georgia Theocharopoulou, Panayiotis Vlamos |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Programmed cell death
ER stress response biology Chemistry Cell Protein Homeostasis Cell biology 03 medical and health sciences 0302 clinical medicine medicine.anatomical_structure Chaperone (protein) biology.protein Unfolded protein response medicine Protein biosynthesis Protein folding 030212 general & internal medicine |
| Zdroj: | Advances in Experimental Medicine and Biology ISBN: 9783030326210 |
| DOI: | 10.1007/978-3-030-32622-7_33 |
| Popis: | Protein homeostasis is a dynamic network that plays a pivotal role in systems' maintenance within a cell. This quality control system involves a number of mechanisms regarding the process of protein folding. Chaperones play a critical role in the folding, refolding, and unfolding of proteins. Aggregation of misfolded proteins is a common characteristic of neurodegenerative diseases. Chaperones act in a variety of pathways in this critical interplay between protein homeostasis network and misfolded protein's load. Moreover, ER stress-induced cell death mechanisms (such as the unfolded protein response) are activated as a response. Therefore, there is a critical balance in the accumulation of misfolded proteins and ER stress response mechanisms which can lead to cell death. Our focus is in understanding the different mechanisms that govern ER stress signaling in health and disease in order to represent the regulation of protein homeostasis and balance of protein synthesis and degradation in the ER. Our proposed model describes, using hybrid modeling, the function of chaperones' machinery for protein folding. |
| Databáze: | OpenAIRE |
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