**Acknowledgement**

We are sincerely grateful to the Chair of the Petrozavodsk State University Molecular Biology Department (Russia), DSc, Professor N. N. Nemova for her invaluable help in the preparation of the manuscript. Special thanks are due also to Professor V. P. Andreev of the St. Petersburg State University Organic Chemistry Department (Russia) for the chemical compounds he has provided.

Cellular Caspases: New Targets for the Action of Pharmacological Agents 201

[11] Wang L, Miura M, Bergeron L, Zhu H, Yuan J (1994) Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell. 78 (5):

[12] Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86 (1): 147-57. [13] Chang HY, Yang X (2000) Proteases for cell suicide: functions and regulation of

[14] Haunstetter A, Izumo S (1998) Apoptosis: basic mechanisms and implications for

[15] Wang Y, Zhao Y, Liu Y, Tian L, Jin D (2011) Chamaejasmine inactivates Akt to trigger apoptosis in human HEp-2 larynx carcinoma cells. Molecules. 16 (10): 8152-64. [16] Chandra J, Samali A, Orrenius S (2000) Triggering and modulation of apoptosis by

[17] Slomiany BL, Slomiany A (2010) Constitutive nitric oxide synthase-mediated caspase-3 S-nitrosylation in ghrelin protection against Porphyromonas gingivalis-induced

[18] Schmitz I, Kirchhoff S, Krammer PH (2000) Regulation of death receptor-mediated

[19] Ferrao R, Wu H (2012) Helical assembly in the death domain (DD) superfamily. Curr

[20] Esposito D, Sankar A, Morgner N, Robinson CV, Rittinger K, Driscoll PC (2010) Solution NMR investigation of the CD95/FADD homotypic death domain complex

[22] Pennarun B, Meijer A, de Vries EG, Kleibeuker JH, Kruyt F, de Jong S (2010) Playing the DISC: turning on TRAIL death receptor-mediated apoptosis in cancer. Biochim Biophys

[23] Shang YC, Chong ZZ, Hou J, Maiese K (2009) FoxO3a governs early microglial proliferation and employs mitochondrial depolarization with caspase 3, 8, and 9

[25] Yuan S, Yu X, Topf M, Ludtke SJ, Wang X, Akey CW (2010) Structure of an

[26] Kowaltowski AJ, Castilho RF, Vercesi AE (2001) Mitochondrial permeability transition

[27] Hu Y, Benedict MA, Ding L, Núñez G (1999) Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 18 (13):

apoptosome-procaspase-9 CARD complex. Structure. 18 (5): 571-83.

cleavage during oxidant induced apoptosis. Curr Neurovasc Res. 6 (4): 223-38. [24] Twiddy D, Brown DG, Adrain C, Jukes R, Martin SJ, Cohen GM, MacFarlane M, Cain K (2004) Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/caspase-9 apoptosome

suggests lack of engagement of the CD95 C terminus. Structure. 18 (10): 1378-90. [21] Lavrik IN, Krammer PH (2012) Regulation of CD95/Fas signaling at the DISC. Cell

salivary gland acinar cell apoptosis. Inflammopharmacology. 18 (3): 119-25.

apoptosis pathways. Int J Biochem Cell Biol. 32 (11-12): 1123-36.

caspases. Microbiol Mol Biol Rev. 64 (4): 821-46.

cardiovascular disease. Circ Res. 82 (11): 1111-29.

oxidative stress. Free Radic Biol Med. 29 (3-4): 323-33.

Opin Struct Biol. 22 (2): 241-7.

Death Differ. 19 (1): 36-41.

complex. J Biol Chem. 279 (19): 19665-82.

and oxidative stress. FEBS Lett. 495 (1-2): 12-5

Acta. 1805 (2): 123-40.

3586-95.

739-50.

The study was supported by the Government of the Russian Federation grant № 11.G34.31.0052 (Ordinance 220), and RF Presidential grant for leading scientific schools № 1642.2012.4.
