Name
Abstract | ||
|---|---|---|
A family of cystein-dependent aspartate-directed proteases, called caspases, is responsible for the proteolytic cleavage of cellular proteins leading to the characteristic apoptotic features, e.g. cleavage of caspase-activated DNase resulting in inter nucleosomal DNA fragmentation. Currently, two pathways for activating caspases have been studied in detail. One starts with ligation of a death ligand to its transmembrane death receptor, followed by recruitment and activation of caspases in the death-inducing signaling complex. The second pathway involves the participation of mitochondria, which release caspase-activating proteins into the cytosol, thereby forming the apoptosome where caspases will bind and become activated. In addition, two other apoptotic pathways are emerging: endoplasmic reticulum stress-induced apoptosis and caspase-independent apoptosis. The model for cell death has been implemented using Fuzzy and CMOS logic using SPICE taking three input signals: Tumor necrosis factor-α (TNF), Epidermal growth factor (EGF) and Insulin. |
Year | DOI | Venue |
|---|---|---|
2010 | 10.1145/1741906.1742082 | ICWET |
Keywords | Field | DocType |
proteolytic cleavage,cell death,death ligand,system model,endoplasmic reticulum stress-induced apoptosis,epidermal growth factor,transmembrane death receptor,characteristic apoptotic feature,apoptotic pathway,caspase-independent apoptosis,activating caspases,dna fragmentation,death inducing signaling complex,apoptosis,caspase,insulin,system modeling,tumor necrosis factor,activator protein | Apoptosome,Computer science,Computer network,Cell biology,DNA fragmentation,Endoplasmic reticulum,Epidermal growth factor,Intrinsic apoptosis,Caspase,Programmed cell death,Apoptosis | Conference |
Citations | PageRank | References |
0 | 0.34 | 0 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| S. Jain | 1 | 0 | 1.35 |
| P. K. Naik | 2 | 0 | 1.01 |
| Sunil Bhooshan | 3 | 1 | 2.73 |