Chapter PDF
Keywords
- Epidermal Growth Factor Receptor
- Caspase Family
- Methyl Ketone
- Actinobacillus Actinomycetemcomitans
- Viral Nucleocapsid Protein
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Strausberg R.L.; Feingold E.A.; Grouse L.H.; Derge J.G., et al.: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. USA, 99, 16899–16903 (2002)
Nakajima, K.; Takahashi, A.; Yaoita, Y.: Structure, expression, and function of the Xenopus laevis caspase family. J. Biol. Chem., 275, 10484–10491 (2000)
Garcia-Calvo, M.; Peterson, E.P.; Leiting, B.; Ruel, R.; Nicholson, D.W.; Thornberry, N.A.: Inhibition of human caspases by peptide-based and macromolecular inhibitors. J. Biol. Chem., 273, 32608–32613 (1998)
Garcia-Calvo, M.; Peterson, E.P.; Rasper, D.M.; Vaillancourt, J.P.; Zamboni, R.; Nicholson, D.W.; Thornberry, N.A.: Purification and catalytic properties of human caspase family members. Cell Death Differ., 6, 362–369 (1999)
Chang, H.Y.; Yang, X.: Proteases from cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev., 64, 821–846 (2000)
Thornberry, N.A.; Rano, T.A.; Peterson, E.P.; et al.: A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem., 272, 17907–17911 (1997)
Fernandes-Alnemri, T.; Armstrong, R.C.; Krebs, J.F.; Srinivasula, S.M.; Wang, L.; Bullrich, F.; Fritz, L.C.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri, E.S.: In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl. Acad. Sci. USA, 93, 7464–7469 (1996)
van de Craen, M.; Vandenabeele, P.; Declercq, W.; van den Brande, I.; van Loo, G.; Molemans, F.; Schotte, P.; van Criekinge, W.; Beyaert, R.; Fiers, W.: Characterization of seven murine caspase family members. FEBS Lett., 403, 61–69 (1997)
Eleouet, J.F.; Slee, E.A.; Saurini, F.; Castagne, N.; Poncet, D.; Garrido, C.; Solary, E.; Martin, S.J.: The viral nucleocapsid protein of transmissible gastroenteritis coronavirus (TGEV) is cleaved by caspase-6 and-7 during TGEV-induced apoptosis. J. Virol., 74, 3975–3983 (2000)
Talanian, R.V.; Quinlan, C.; Trautz, S.; Hackett, M.C.; Mankovich, J.A.; Banach, D.; Ghayur, T.; Brady, K.D.; Wong, W.W.: Substrate specificities of caspase family proteases. J. Biol. Chem., 272, 9677–9682 (1997)
Margolin, N.; Raybuck, S.A.; Wilson, K.P.; Chen, W.; Fox, T.; Gu, Y.; Livingston, D.J.: Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases. J. Biol. Chem., 272, 7223–7228 (1997)
Bae, S.S.; Choi, J.H.; Oh, Y.S.; Perry, D.K.; Ryu, S.H.; Suh, P.G.: Proteolytic cleavage of epidermal growth factor receptor by caspases. FEBS Lett., 491, 16–20 (2001)
Kisselev, A.F.; Garcia-Calvo, M.; Overkleeft, H.S.; Peterson, E.; Pennington, M.W.; Ploegh, H.L.; Thornberry, N.A.; Goldberg, A.L.: The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites. J. Biol. Chem., 278, 35869–35877 (2003)
Lippke, J.A.; Gu, Y.; Sarnecki, C.; Caron, P.R.; Su, M.S.-S.: Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. J. Biol. Chem., 271, 1825–1828 (1996)
Fernandes-Alnemri, T.; Takahashi, A.; Armstrong, R.C.; Krebs, J.; Fritz, L.C.; Tomaselli, K.J.; Wang, L.; Yu, Z.; Croce, C.M.; Salveson, G.; Earnshaw, W.C.; Litwack, G.; Alnemri, E.S.: Mch3, a novel human apoptotic cysteine protease highly related to CPP32. Cancer Res., 55, 6045–6052 (1995)
Juan, T.S.-C.; McNiece, I.K.; Argento, J.M.; Jenkins, N.A.; Gilbert, D.J.; Copeland, N.G.; Fletcher, F.A.: Identification and mapping of Casp7, a cysteine protease resembling CPP32 β, interleukin-1 β converting enzyme, and CED-3. Genomics, 40, 86–93 (1997)
Pai J.-T., Brown M.S., Goldstein J.L.: Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins. Proc. Natl. Acad. Sci. USA, 93, 5437–5442 (1996)
Machleidt, T.; Geller, P.; Schwandner, R.; Scherer, G.; Kronke, M.: Caspase 7-induced cleavage of kinectin in apoptotic cells. FEBS Lett., 436, 51–54 (1998)
Ethell, D.W.; Bossy-Wetzel, E.; Bredesen, D.E.: Caspase 7 can cleave tumor necrosis factor receptor-I (p60) at a non-consensus motif, in vitro. Biochim. Biophys. Acta, 1541, 231–238 (2001)
Riedl, S.J.; Fuentes-Prior, P.; Renatus, M.; Kairies, N.; Krapp, S.; Huber, R.; Salvesen, G.S.; Bode, W.: Structural basis for the activation of human procaspase-7. Proc. Natl. Acad. Sci. USA, 98, 14790–14795 (2001)
Yaoita, Y.: Inhibition of nuclear transport of caspase-7 by its prodomain. Biochem. Biophys. Res. Commun., 291, 79–84 (2002)
Behrensdorf, H.A.; van de Craen, M.; Knies, U.E.; Vandenabeele, P.; Clauss, M.: The endothelial monocyte-activating polypeptide II (EMAP II) is a substrate for caspase-7. FEBS Lett., 466, 143–147 (2000)
Denault, J.B.; Salvesen, G.S.: Human caspase-7 activity and regulation by its N-terminal peptide. J. Biol. Chem., 278, 34042–34050 (2003)
Duan, H.; Chinnaiyan, A.M.; Hudson, P.L.; Wing, J.P.; He, W.-W.; Dixit, V.M.: ICE-LAP-3, a novel mammalian homologue at the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas-and tumor necrosis factor-induced apoptosis. J. Biol. Chem., 271, 1621–1625 (1996)
Chiu, C.C.; Lin, C.H.; Fang, K.: Etoposide (VP-16) sensitizes p53-deficient human non-small cell lung cancer cells to caspase-7-mediated apoptosis. Apoptosis, 10, 643–650 (2005)
Yacobi, K.; Wojtowicz, A.; Tsafriri, A.; Gross, A.: Gonadotropins enhance caspase-3 and-7 activity and apoptosis in the theca-interstitial cells of rat preovulatory follicles in culture. Endocrinology, 145, 1943–1951 (2004)
Ohara, M.; Hayashi, T.; Kusunoki, Y.; Miyauchi, M.; Takata, T.; Sugai, M.: Caspase-2 and caspase-7 are involved in cytolethal distending toxin-induced apoptosis in Jurkat and MOLT-4 T-cell lines. Infect. Immun., 72, 871–879 (2004)
Sironi, J.J.; Ouchi, T.: STAT1-induced apoptosis is mediated by caspases 2, 3, and 7. J. Biol. Chem., 279, 4066–4074 (2004)
Clarke, C.A.; Bennett, L.N.; Clarke, P.R.: Cleavage of claspin by caspase-7 during apoptosis inhibits the Chk1 pathway. J. Biol. Chem., 280, 35337–35345 (2005)
Twiddy, D.; Cohen, G.M.; Macfarlane, M.; Cain, K.: Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex. J. Biol. Chem., 281, 3876–3888 (2006)
Fang, B.; Boross, P.I.; Tozser, J.; Weber, I.T.: Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition. J. Mol. Biol., 360, 654–666 (2006)
Houde, C.; Banks, K.G.; Coulombe, N.; Rasper, D.; Grimm, E.; Roy, S.; Simpson, E.M.; Nicholson, D.W.: Caspase-7 expanded function and intrinsic expression level underlies strain-specific brain phenotype of caspase-3-null mice. J. Neurosci., 24, 9977–9984 (2004)
Hayashi, N.; Shirakura, H.; Uehara, T.; Nomura, Y.: Relationship between SUMO-1 modification of caspase-7 and its nuclear localization in human neuronal cells. Neurosci. Lett., 397, 5–9 (2006)
Goode, D.R.; Sharma, A.K.; Hergenrother, P.J.: Using peptidic inhibitors to systematically probe the S1 site of caspase-3 and caspase-7. Org. Lett., 7, 3529–3532 (2005)
Chen, D.; Texada, D.E.; Duggan, C.; Deng, Y.; Redens, T.B.; Langford, M.P.: Caspase-3 and-7 mediate apoptosis of human Chang’s conjunctival cells induced by enterovirus 70. Virology, 347, 307–322 (2006)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2009). Caspase-7. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_14
Download citation
DOI: https://doi.org/10.1007/978-3-540-85705-1_14
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-85704-4
Online ISBN: 978-3-540-85705-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)