Susceptibility to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and Bcl-xL protein levels
β Scribed by Tudor, G; Aguilera, A; Halverson, D O; Laing, N D; Sausville, E A
- Book ID
- 110016061
- Publisher
- Nature Publishing Group
- Year
- 2000
- Tongue
- English
- Weight
- 336 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1350-9047
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The expression and functionality of the Fas receptor (CD95/APO-1) play an important role for the maintenance of tissue homeostasis. Various types of tumor cells have been shown to escape immune recognition by constitutive resistance to CD95-mediated apoptosis. Furthermore, several apoptosis-related
## Abstract We have recently reported that the naturally occurring spliced variant of Hepatitis B virus protein, HBSP, displayed proapoptotic activity through its BH3 domain. To investigate whether the BH3 domain in HBSP interacted with Bclβ2 family of proteins, HBSP and Bclβ2 family of proteins we
## Abstract ## Background. The p53 protein, a wellβknown tumor suppressor that functions primarily as a transcription factor, initiates cell cycle arrest and apoptosis after genotoxic stress. The antiapoptotic regulator Bclβ2 is a downstream modulator of p53βinduced apoptosis. Loss of function of
It has been demonstrated that nitric oxide (NO) can promote apoptosis in human cancer cells. To test the protective effects of antioxidants (N-acetyl-L-cysteine (LNAC)) and free-radical spin traps (5,5-dimethyl-1-pyrroline N-oxide and 2,2,6,6,-tetramethyl-1-piperidinyloxy) against NO-induced apoptos