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Volumn 15, Issue 5, 2007, Pages 625-636

Inhibition of Caspase-2 by a Designed Ankyrin Repeat Protein: Specificity, Structure, and Inhibition Mechanism

Author keywords

CELLCYCLE; CHEMBIOL

Indexed keywords

ANKYRIN; CASPASE 2; CASPASE INHIBITOR;

EID: 34247853389     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.03.014     Document Type: Article
Times cited : (120)

References (51)
  • 2
    • 0019617042 scopus 로고
    • The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors
    • Baici A. The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors. Eur. J. Biochem. 119 (1981) 9-14
    • (1981) Eur. J. Biochem. , vol.119 , pp. 9-14
    • Baici, A.1
  • 3
    • 0029817805 scopus 로고    scopus 로고
    • pH-dependent hysteretic behaviour of human myeloblastin (leucocyte proteinase 3)
    • Baici A., Szedlacsek S.E., Früh H., and Michel B.A. pH-dependent hysteretic behaviour of human myeloblastin (leucocyte proteinase 3). Biochem. J. 317 (1996) 901-905
    • (1996) Biochem. J. , vol.317 , pp. 901-905
    • Baici, A.1    Szedlacsek, S.E.2    Früh, H.3    Michel, B.A.4
  • 5
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz H.K., Stumpp M.T., Forrer P., Amstutz P., and Plückthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332 (2003) 489-503
    • (2003) J. Mol. Biol. , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 7
    • 0028883709 scopus 로고
    • Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria
    • Biocca S., Ruberti F., Tafani M., Pierandrei-Amaldi P., and Cattaneo A. Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria. Biotechnology (N. Y.) 13 (1995) 1110-1115
    • (1995) Biotechnology (N. Y.) , vol.13 , pp. 1110-1115
    • Biocca, S.1    Ruberti, F.2    Tafani, M.3    Pierandrei-Amaldi, P.4    Cattaneo, A.5
  • 10
    • 0028103275 scopus 로고
    • The CCP4 Suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 11
    • 0038576220 scopus 로고    scopus 로고
    • A key role for caspase-2 and caspase-3 in the apoptosis induced by 2-chloro-2′-deoxy-adenosine (cladribine) and 2-chloro-adenosine in human astrocytoma cells
    • Ceruti S., Beltrami E., Matarrese P., Mazzola A., Cattabeni F., Malorni W., and Abbracchio M.P. A key role for caspase-2 and caspase-3 in the apoptosis induced by 2-chloro-2′-deoxy-adenosine (cladribine) and 2-chloro-adenosine in human astrocytoma cells. Mol. Pharmacol. 63 (2003) 1437-1447
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1437-1447
    • Ceruti, S.1    Beltrami, E.2    Matarrese, P.3    Mazzola, A.4    Cattabeni, F.5    Malorni, W.6    Abbracchio, M.P.7
  • 12
    • 0036490942 scopus 로고    scopus 로고
    • Allosteric binding sites on cell-surface receptors: novel targets for drug discovery
    • Christopoulos A. Allosteric binding sites on cell-surface receptors: novel targets for drug discovery. Nat. Rev. Drug Discov. 1 (2002) 198-210
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 198-210
    • Christopoulos, A.1
  • 13
    • 1542426652 scopus 로고    scopus 로고
    • Apoptosis signaling triggered by the marine alkaloid ascididemin is routed via caspase-2 and JNK to mitochondria
    • Dirsch V.M., Kirschke S.O., Estermeier M., Steffan B., and Vollmar A.M. Apoptosis signaling triggered by the marine alkaloid ascididemin is routed via caspase-2 and JNK to mitochondria. Oncogene 23 (2004) 1586-1593
    • (2004) Oncogene , vol.23 , pp. 1586-1593
    • Dirsch, V.M.1    Kirschke, S.O.2    Estermeier, M.3    Steffan, B.4    Vollmar, A.M.5
  • 16
    • 4143110187 scopus 로고    scopus 로고
    • Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering
    • Ewert S., Honegger A., and Plückthun A. Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering. Methods 34 (2004) 184-199
    • (2004) Methods , vol.34 , pp. 184-199
    • Ewert, S.1    Honegger, A.2    Plückthun, A.3
  • 18
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 23
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., and Weinberg R.A. The hallmarks of cancer. Cell 100 (2000) 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 24
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., and Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. USA 94 (1997) 4937-4942
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 27
    • 0034671563 scopus 로고    scopus 로고
    • Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors
    • Jeffrey P.D., Tong L., and Pavletich N.P. Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors. Genes Dev. 14 (2000) 3115-3125
    • (2000) Genes Dev. , vol.14 , pp. 3115-3125
    • Jeffrey, P.D.1    Tong, L.2    Pavletich, N.P.3
  • 28
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21 (1988) 67-71
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 31
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P., Opitz-Araya X., and Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 297 (2002) 1352-1354
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 32
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 33
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50 (1994) 157-163
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 34
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: insights into drug design from structure
    • Noble M.E., Endicott J.A., and Johnson L.N. Protein kinase inhibitors: insights into drug design from structure. Science 303 (2004) 1800-1805
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 35
    • 0037119491 scopus 로고    scopus 로고
    • Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis
    • Robertson J.D., Enoksson M., Suomela M., Zhivotovsky B., and Orrenius S. Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J. Biol. Chem. 277 (2002) 29803-29809
    • (2002) J. Biol. Chem. , vol.277 , pp. 29803-29809
    • Robertson, J.D.1    Enoksson, M.2    Suomela, M.3    Zhivotovsky, B.4    Orrenius, S.5
  • 36
    • 4344663051 scopus 로고    scopus 로고
    • Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity
    • Robertson J.D., Gogvadze V., Kropotov A., Vakifahmetoglu H., Zhivotovsky B., and Orrenius S. Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity. EMBO Rep. 5 (2004) 643-648
    • (2004) EMBO Rep. , vol.5 , pp. 643-648
    • Robertson, J.D.1    Gogvadze, V.2    Kropotov, A.3    Vakifahmetoglu, H.4    Zhivotovsky, B.5    Orrenius, S.6
  • 37
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • Russo A.A., Tong L., Lee J.O., Jeffrey P.D., and Pavletich N.P. Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature 395 (1998) 237-243
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 38
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz P.J. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (N. Y.) 11 (1993) 1138-1143
    • (1993) Biotechnology (N. Y.) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 39
    • 0142242170 scopus 로고    scopus 로고
    • Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway
    • Schweizer A., Briand C., and Grütter M.G. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J. Biol. Chem. 278 (2003) 42441-42447
    • (2003) J. Biol. Chem. , vol.278 , pp. 42441-42447
    • Schweizer, A.1    Briand, C.2    Grütter, M.G.3
  • 42
    • 0037444152 scopus 로고    scopus 로고
    • Restoration of fragile histidine triad (FHIT) expression induces apoptosis and suppresses tumorigenicity in breast cancer cell lines
    • Sevignani C., Calin G.A., Cesari R., Sarti M., Ishii H., Yendamuri S., Vecchione A., Trapasso F., and Croce C.M. Restoration of fragile histidine triad (FHIT) expression induces apoptosis and suppresses tumorigenicity in breast cancer cell lines. Cancer Res. 63 (2003) 1183-1187
    • (2003) Cancer Res. , vol.63 , pp. 1183-1187
    • Sevignani, C.1    Calin, G.A.2    Cesari, R.3    Sarti, M.4    Ishii, H.5    Yendamuri, S.6    Vecchione, A.7    Trapasso, F.8    Croce, C.M.9
  • 43
    • 33645299092 scopus 로고    scopus 로고
    • Caspases at the crossroads of immune-cell life and death
    • Siegel R.M. Caspases at the crossroads of immune-cell life and death. Nat. Rev. Immunol. 6 (2006) 308-317
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 308-317
    • Siegel, R.M.1
  • 45
    • 0032847318 scopus 로고    scopus 로고
    • Caspases: preparation and characterization
    • Stennicke H.R., and Salvesen G.S. Caspases: preparation and characterization. Methods 17 (1999) 313-319
    • (1999) Methods , vol.17 , pp. 313-319
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 46
    • 0024288477 scopus 로고
    • A re-evaluation of the kinetic equations for hyperbolic tight-binding inhibition
    • Szedlacsek S.E., Ostafe V., Serban M., and Vlad M.O. A re-evaluation of the kinetic equations for hyperbolic tight-binding inhibition. Biochem. J. 254 (1988) 311-312
    • (1988) Biochem. J. , vol.254 , pp. 311-312
    • Szedlacsek, S.E.1    Ostafe, V.2    Serban, M.3    Vlad, M.O.4
  • 49
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A., and Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304 (2004) 843-846
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2


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