메뉴 건너뛰기




Volumn 18, Issue 20, 1999, Pages 5453-5462

Crystal structure of gingipain R: An Arg-specific bacterial cysteine proteinase with a caspase-like fold

Author keywords

Caspases; Crystal structure; Cysteine proteinase; Periodontitis; Porphyromonas gingivalis

Indexed keywords

BACTERIAL ENZYME; CASPASE; CYSTEINE PROTEINASE; ENZYME INHIBITOR; GINGIPAIN R;

EID: 0033570275     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.20.5453     Document Type: Article
Times cited : (157)

References (54)
  • 2
    • 0031863621 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone
    • Banbula, A., Potempa, J., Travis, J., Bode, W. and Medrano, F.-J. (1998) Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone. Protein Sci., 7, 1259-1261.
    • (1998) Protein Sci. , vol.7 , pp. 1259-1261
    • Banbula, A.1    Potempa, J.2    Travis, J.3    Bode, W.4    Medrano, F.-J.5
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 4
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System - A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography & NMR System - a new software suite for macromolecular structure determination. Acta Crystallogr. D, 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 5
    • 0032549590 scopus 로고    scopus 로고
    • Inactivation of tumor necrosis factor-α by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis
    • Calkins, C.C., Platt, K., Potempa, J. and Travis, J. (1998) Inactivation of tumor necrosis factor-α by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. J. Biol. Chem., 273, 6611-6614.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6611-6614
    • Calkins, C.C.1    Platt, K.2    Potempa, J.3    Travis, J.4
  • 6
    • 0026517239 scopus 로고
    • Molecular cloning of the interleukin-1β converting enzyme
    • Cerretti, D.P. et al. (1992) Molecular cloning of the interleukin-1β converting enzyme. Science, 256, 97-100.
    • (1992) Science , vol.256 , pp. 97-100
    • Cerretti, D.P.1
  • 7
    • 0032435254 scopus 로고    scopus 로고
    • Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases
    • Chen, J.-M., Rawlings, N.D., Stevens, R.A.E. and Barrett, A.J. (1998) Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett., 441, 361-365.
    • (1998) FEBS Lett. , vol.441 , pp. 361-365
    • Chen, J.-M.1    Rawlings, N.D.2    Stevens, R.A.E.3    Barrett, A.J.4
  • 8
    • 0026644069 scopus 로고
    • Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis
    • Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M. and Travis, J. (1992) Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem., 267, 18896-18901.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18896-18901
    • Chen, Z.1    Potempa, J.2    Polanowski, A.3    Wikstrom, M.4    Travis, J.5
  • 9
    • 0030907070 scopus 로고    scopus 로고
    • The molecular structure of cell adhesion molecules
    • Chothia, C. and Jones, E.Y. (1997) The molecular structure of cell adhesion molecules. Annu. Rev. Biochem., 66, 823-862.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 823-862
    • Chothia, C.1    Jones, E.Y.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 11
    • 0028813652 scopus 로고
    • Pathogenic strategies of the oral anaerobe, Porphyromonas gingivalis
    • Cutler, C.W., Kalmar, J.R. and Genco, C.A. (1995) Pathogenic strategies of the oral anaerobe, Porphyromonas gingivalis. Trends Microbiol., 3, 45-51.
    • (1995) Trends Microbiol. , vol.3 , pp. 45-51
    • Cutler, C.W.1    Kalmar, J.R.2    Genco, C.A.3
  • 12
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 13
    • 0029870771 scopus 로고    scopus 로고
    • Cleavage of human complement component C5 by cysteine proteinases from Porphyromonas (Bacteroides) gingivalis. Prior oxidation of C5 augments proteinase digestion of C5
    • DiScripio, R.G., Daffern, P.J., Kawahara, M., Pike, R., Potempa, J., Travis, J. and Hugli, T.E. (1996) Cleavage of human complement component C5 by cysteine proteinases from Porphyromonas (Bacteroides) gingivalis. Prior oxidation of C5 augments proteinase digestion of C5. Immunology, 87, 660-667.
    • (1996) Immunology , vol.87 , pp. 660-667
    • DiScripio, R.G.1    Daffern, P.J.2    Kawahara, M.3    Pike, R.4    Potempa, J.5    Travis, J.6    Hugli, T.E.7
  • 14
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A, 47, 392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0032526398 scopus 로고    scopus 로고
    • Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis
    • Fujimura, S., Hirai, K., Shibata, Y., Nakayama, K. and Nakamura, T. (1998) Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis. FEMS Microbiol. Lett., 163, 173-179.
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 173-179
    • Fujimura, S.1    Hirai, K.2    Shibata, Y.3    Nakayama, K.4    Nakamura, T.5
  • 16
    • 0031690172 scopus 로고    scopus 로고
    • A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice
    • Genco, C.A., Odusanya, B.M., Mikolajczyk-Pawlinska, J., Potempa, J. and Travis, J. (1998) A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice. Infect. Immun., 66, 4108-4114.
    • (1998) Infect. Immun. , vol.66 , pp. 4108-4114
    • Genco, C.A.1    Odusanya, B.M.2    Mikolajczyk-Pawlinska, J.3    Potempa, J.4    Travis, J.5
  • 17
    • 0023834926 scopus 로고
    • Implantation of Bacteroides gingivalis in nonhuman primates initiates progression of periodontitis
    • Holt, S.C., Ebersole, J., Felton, J., Brunsvold, M. and Kornman, K.S. (1988) Implantation of Bacteroides gingivalis in nonhuman primates initiates progression of periodontitis. Science, 239, 55-57.
    • (1988) Science , vol.239 , pp. 55-57
    • Holt, S.C.1    Ebersole, J.2    Felton, J.3    Brunsvold, M.4    Kornman, K.S.5
  • 18
    • 0028242731 scopus 로고
    • Pathogenesis of periodontitis: A major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway
    • Imamura, T., Pike, R.N., Potempa, J. and Travis, J. (1994) Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway. J. Clin. Invest., 94, 361-367.
    • (1994) J. Clin. Invest. , vol.94 , pp. 361-367
    • Imamura, T.1    Pike, R.N.2    Potempa, J.3    Travis, J.4
  • 19
    • 0030941836 scopus 로고    scopus 로고
    • Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis
    • Imamura, T., Potempa, J., Tanase, S. and Travis, J. (1997) Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis. J. Biol. Chem., 272, 16062-16067.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16062-16067
    • Imamura, T.1    Potempa, J.2    Tanase, S.3    Travis, J.4
  • 20
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T.A. (1978) A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr., 11, 268-272.
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 21
    • 0032582491 scopus 로고    scopus 로고
    • Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis
    • Kadowaki, T., Nakayama, K., Yoshimura, F., Okamoto, K., Abe, N. and Yamamoto, K. (1998) Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. J. Biol. Chem., 273, 29072-29076.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29072-29076
    • Kadowaki, T.1    Nakayama, K.2    Yoshimura, F.3    Okamoto, K.4    Abe, N.5    Yamamoto, K.6
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0032189067 scopus 로고    scopus 로고
    • Proteases of Porphyromonas gingivalis: What don't they do?
    • Kuramitsu, H.K. (1998) Proteases of Porphyromonas gingivalis: what don't they do? Oral Microbiol. Immunol., 13, 263-270.
    • (1998) Oral Microbiol. Immunol. , vol.13 , pp. 263-270
    • Kuramitsu, H.K.1
  • 24
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont, R.J. and Jenkinson, H.F. (1998) Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev., 62, 1244-1263.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 25
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. and Wilson, K.S. (1993) Automated refinement of protein models. Acta Crystallogr. D, 49, 129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Oxford University Press, Oxford, UK
    • Leslie, A.G.W. (1991) Molecular data processing. In Moras, D., Podjarny, A.D. and Thierry, J.C. (eds), Crystallographic Computing 5. Oxford University Press, Oxford, UK, pp. 50-61.
    • (1991) Crystallographic Computing 5 , pp. 50-61
    • Leslie, A.G.W.1
  • 28
    • 0003115798 scopus 로고    scopus 로고
    • A WWW service system for an automatic comparison of protein structures
    • Lu, G. (1996) A WWW service system for an automatic comparison of protein structures. Protein Data Bank Q. Newsl., 78, 10-11.
    • (1996) Protein Data Bank Q. Newsl. , vol.78 , pp. 10-11
    • Lu, G.1
  • 29
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merrit, E.A. and Murphy, M.E.P. (1994) Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D, 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 30
    • 0031951529 scopus 로고    scopus 로고
    • Genetic variations of Porphyromonas gingivalis genes encoding gingipains, cysteine proteinases with arginine or lysine specificity
    • Mikolajczyk-Pawlinska, J., Kordula, T., Pavloff, M., Pemberton, P.A., Kiefer, M.C., Travis, J. and Potempa, J. (1998) Genetic variations of Porphyromonas gingivalis genes encoding gingipains, cysteine proteinases with arginine or lysine specificity. Biol. Chem., 379, 205-211.
    • (1998) Biol. Chem. , vol.379 , pp. 205-211
    • Mikolajczyk-Pawlinska, J.1    Kordula, T.2    Pavloff, M.3    Pemberton, P.A.4    Kiefer, M.C.5    Travis, J.6    Potempa, J.7
  • 32
    • 0030891894 scopus 로고    scopus 로고
    • Domain-specific rearrangement between two arg-gingipain-encoding genes in Porphyromonas gingivalis: Possible involvement of nonreciprocal recombination
    • Nakayama, K. (1997) Domain-specific rearrangement between two arg-gingipain-encoding genes in Porphyromonas gingivalis: possible involvement of nonreciprocal recombination. Microbiol. Immunol., 41, 185-196.
    • (1997) Microbiol. Immunol. , vol.41 , pp. 185-196
    • Nakayama, K.1
  • 33
    • 0028839251 scopus 로고
    • Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence
    • Nakayama, K., Kadowaki, T., Okamoto, K. and Yamamoto, K. (1995) Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence. J. Biol. Chem., 270, 23619-23626.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23619-23626
    • Nakayama, K.1    Kadowaki, T.2    Okamoto, K.3    Yamamoto, K.4
  • 34
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet., 11, 281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 35
    • 0029555645 scopus 로고
    • Active site structure of a hemagglutinating protease from Porphyromonas gingivalis: Similarity to clostripain
    • Nishikata, M. and Yoshimura, F. (1995) Active site structure of a hemagglutinating protease from Porphyromonas gingivalis: similarity to clostripain. Biochem. Mol. Biol. Int., 37, 547-553.
    • (1995) Biochem. Mol. Biol. Int. , vol.37 , pp. 547-553
    • Nishikata, M.1    Yoshimura, F.2
  • 36
    • 0028931990 scopus 로고
    • Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis
    • Okamoto, K., Misumi, Y., Kadowaki, T., Yoneda, M., Yamamoto, K. and Ikehara, Y. (1995) Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis. Arch. Biochem. Biophys., 316, 917-925.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 917-925
    • Okamoto, K.1    Misumi, Y.2    Kadowaki, T.3    Yoneda, M.4    Yamamoto, K.5    Ikehara, Y.6
  • 37
    • 0029616688 scopus 로고    scopus 로고
    • Identification of Porphyromonas gingivalis prefimbrilin possessing a long leader peptide: Possible involvement of trypsin-like protease in fimbrilin maturation
    • Onoe, T., Hoover, C.I., Nakayama, K., Ideka, T., Nakamura, H. and Yoshimura, F. (1996) Identification of Porphyromonas gingivalis prefimbrilin possessing a long leader peptide: possible involvement of trypsin-like protease in fimbrilin maturation. Microbiol. Pathogen., 19, 351-364.
    • (1996) Microbiol. Pathogen. , vol.19 , pp. 351-364
    • Onoe, T.1    Hoover, C.I.2    Nakayama, K.3    Ideka, T.4    Nakamura, H.5    Yoshimura, F.6
  • 38
    • 0032112772 scopus 로고    scopus 로고
    • The pathobiology of periodontal diseases may affect systemic diseases: Inversion of a paradigm
    • Page, R.C. (1998) The pathobiology of periodontal diseases may affect systemic diseases: inversion of a paradigm. Ann. Periodontol., 3, 108-120.
    • (1998) Ann. Periodontol. , vol.3 , pp. 108-120
    • Page, R.C.1
  • 39
    • 0028840005 scopus 로고
    • Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis
    • Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. and Barr, P.J. (1995) Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. J. Biol. Chem., 270, 1007-1010.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1007-1010
    • Pavloff, N.1    Potempa, J.2    Pike, R.N.3    Prochazka, V.4    Kiefer, M.C.5    Travis, J.6    Barr, P.J.7
  • 40
    • 0031018358 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Porphyromonas gingivalis Lys-gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases
    • Pavloff, N., Pemberton, P.A., Potempa, J., Chen, W.C.A., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. and Barr, P.J. (1997) Molecular cloning and characterization of Porphyromonas gingivalis Lys-gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases. J. Biol. Chem., 272, 1595-1600.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1595-1600
    • Pavloff, N.1    Pemberton, P.A.2    Potempa, J.3    Chen, W.C.A.4    Pike, R.N.5    Prochazka, V.6    Kiefer, M.C.7    Travis, J.8    Barr, P.J.9
  • 41
    • 0030338378 scopus 로고    scopus 로고
    • Porphyromonas gingivalis proteinases in periodontitis, a review
    • Potempa, J. and Travis, J. (1996) Porphyromonas gingivalis proteinases in periodontitis, a review. Acta Biochim. Pol., 43, 455-466.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 455-466
    • Potempa, J.1    Travis, J.2
  • 42
    • 0031008093 scopus 로고    scopus 로고
    • Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes
    • Potempa, J., Pike, R. and Travis, J. (1997) Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes. Biol. Chem., 378, 223-230.
    • (1997) Biol. Chem. , vol.378 , pp. 223-230
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 43
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipain Rs), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa, J., Mikolajczyk-Pawlinska, J., Brassell, D., Nelson, D., Thogersen, I.B., Enghild, J.J. and Travis, J. (1998) Comparative properties of two cysteine proteinases (gingipain Rs), the products of two related but individual genes of Porphyromonas gingivalis. J. Biol. Chem., 273, 21648-21657.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21648-21657
    • Potempa, J.1    Mikolajczyk-Pawlinska, J.2    Brassell, D.3    Nelson, D.4    Thogersen, I.B.5    Enghild, J.J.6    Travis, J.7
  • 45
    • 0031036570 scopus 로고    scopus 로고
    • The prpR1 and prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes
    • Rangarajan, M., Aduse-Opoku, J., Slaney, J.M., Young, K.A. and Curtis, M.A. (1997) The prpR1 and prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes. Mol Microbiol., 23, 955-965.
    • (1997) Mol Microbiol. , vol.23 , pp. 955-965
    • Rangarajan, M.1    Aduse-Opoku, J.2    Slaney, J.M.3    Young, K.A.4    Curtis, M.A.5
  • 47
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, J.M. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A, 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, J.M.1
  • 48
    • 15844393657 scopus 로고    scopus 로고
    • The three-dimensional structure of apopain/ CPP32, a key mediator of apoptosis
    • Rotonda, J. et al. (1996) The three-dimensional structure of apopain/ CPP32, a key mediator of apoptosis. Nature Struct. Biol., 3, 619-625.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 619-625
    • Rotonda, J.1
  • 49
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7 and -8
    • Stennicke, H.R. and Salvesen, G.S. (1997) Biochemical characteristics of caspases-3, -6, -7 and -8. J. Biol. Chem., 272, 25719-25723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 50
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A. and Lazebnik, Y. (1998) Caspases: enemies within. Science, 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 51
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes
    • Thornberry, N.A. et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature, 356, 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1
  • 52
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr., 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 53
    • 0028107827 scopus 로고
    • 2 homodimer
    • 2 homodimer. Cell, 78, 343-352.
    • (1994) Cell , vol.78 , pp. 343-352
    • Walker, N.P.1
  • 54
    • 0028170376 scopus 로고
    • Structure and mechanism of interleukin-1β converting enzyme
    • Wilson, K.P. et al. (1994) Structure and mechanism of interleukin-1β converting enzyme. Nature, 370, 270-275.
    • (1994) Nature , vol.370 , pp. 270-275
    • Wilson, K.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.