메뉴 건너뛰기




Volumn 288, Issue 20, 2013, Pages 14287-14296

Porphyromonas gingivalis virulence factor gingipain RgpB shows a unique zymogenic mechanism for cysteine peptidases

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYSTEINES; CATALYTIC DOMAINS; CYSTEINE PEPTIDASE; INHIBITORY MECHANISM; PERIODONTAL DISEASE; REGULATORY MECHANISM; STRUCTURAL DETERMINANTS; SUBSTRATE SPECIFICITY;

EID: 84877912442     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.444927     Document Type: Article
Times cited : (31)

References (73)
  • 1
    • 30944431967 scopus 로고    scopus 로고
    • Strengthening the prevention of periodontal disease: The WHO approach
    • DOI 10.1902/jop.2005.76.12.2187
    • Petersen, P. E., and Ogawa, H. (2005) Strengthening the prevention of periodontal disease: the WHO approach. J. Periodontol. 76, 2187-2193 (Pubitemid 43116083)
    • (2005) Journal of Periodontology , vol.76 , Issue.12 , pp. 2187-2193
    • Petersen, P.E.1    Ogawa, H.2
  • 2
    • 84863826834 scopus 로고    scopus 로고
    • Porphyromonas gingivalis: An invasive and evasive opportunistic oral pathogen
    • Bostanci, N., and Belibasakis, G. N. (2012) Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen. FEMS Microbiol. Lett. 333, 1-9
    • (2012) FEMS Microbiol. Lett. , vol.333 , pp. 1-9
    • Bostanci, N.1    Belibasakis, G.N.2
  • 3
    • 80053328180 scopus 로고    scopus 로고
    • The lysine-specific gingipain of Porphyromonas gingivalis: Importance to pathogenicity and potential strategies for inhibition
    • Yongqing, T., Potempa, J., Pike, R. N., and Wijeyewickrema, L. C. (2011) The lysine-specific gingipain of Porphyromonas gingivalis : importance to pathogenicity and potential strategies for inhibition. Adv. Exp. Med. Biol. 712, 15-29
    • (2011) Adv. Exp. Med. Biol. , vol.712 , pp. 15-29
    • Yongqing, T.1    Potempa, J.2    Pike, R.N.3    Wijeyewickrema, L.C.4
  • 4
    • 33747853795 scopus 로고    scopus 로고
    • The breadth of bacterial diversity in the human periodontal pocket and other oral sites
    • DOI 10.1111/j.1600-0757.2006.00174.x
    • Paster, B. J., Olsen, I., Aas, J. A., and Dewhirst, F. E. (2006) The breadth of bacterial diversity in the human periodontal pocket and other oral sites. Periodontol. 2000 42, 80-87 (Pubitemid 44286048)
    • (2006) Periodontology 2000 , vol.42 , Issue.1 , pp. 80-87
    • Paster, B.J.1    Olsen, I.2    Aas, J.A.3    Dewhirst, F.E.4
  • 6
    • 4644245420 scopus 로고    scopus 로고
    • Occurrence of Porphyromonas gingivalis and Tannerella forsythensis in periodontally diseased and healthy subjects
    • Yang, H. W., Huang, Y. F., and Chou, M. Y. (2004) Occurrence of Porphyromonas gingivalis and Tannerella forsythensis in periodontally diseased and healthy subjects. J. Periodontol. 75, 1077-1083
    • (2004) J. Periodontol. , vol.75 , pp. 1077-1083
    • Yang, H.W.1    Huang, Y.F.2    Chou, M.Y.3
  • 7
    • 0036835212 scopus 로고    scopus 로고
    • Porphyromonas gingivalis, Bacteroides forsythus and other putative periodontal pathogens in subjects with and without periodontal destruction
    • DOI 10.1034/j.1600-051X.2002.291107.x
    • van Winkelhoff, A. J., Loos, B. G., van der Reijden, W. A., and van der Velden, U. (2002) Porphyromonas gingivalis, Bacteroides forsythus, and other putative periodontal pathogens in subjects with and without periodontal destruction. J. Clin. Periodontol. 29, 1023-1028 (Pubitemid 41697772)
    • (2002) Journal of Clinical Periodontology , vol.29 , Issue.11 , pp. 1023-1028
    • Van Winkelhoff, A.J.1    Loos, B.G.2    Van Der, R.W.A.3    Van Der, V.U.4
  • 8
    • 55549083867 scopus 로고    scopus 로고
    • The chronicles of Porphyromonas gingivalis: The microbium, the human oral epithelium, and their interplay
    • Yilmaz, O. (2008) The chronicles of Porphyromonas gingivalis: the microbium, the human oral epithelium, and their interplay. Microbiology 154, 2897-2903
    • (2008) Microbiology , vol.154 , pp. 2897-2903
    • Yilmaz, O.1
  • 9
    • 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 (Pubitemid 28558298)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.4 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 10
    • 77955760680 scopus 로고    scopus 로고
    • Dichotomy of gingipains action as virulence factors: From cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins
    • Guo, Y., Nguyen, K. A., and Potempa, J. (2010) Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins. Periodontol. 2000 54, 15-44
    • (2010) Periodontol. 2000 , vol.54 , pp. 15-44
    • Guo, Y.1    Nguyen, K.A.2    Potempa, J.3
  • 11
    • 0031008093 scopus 로고    scopus 로고
    • Titration and mapping of the active site of cysteine proteinases from Porphyromonas ginaivalis (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 (Pubitemid 27230607)
    • (1997) Biological Chemistry , vol.378 , Issue.3-4 , pp. 223-230
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 12
    • 0030183787 scopus 로고    scopus 로고
    • Effect of protoporphyrin IX limitation on porphyromonas gingivalis
    • Schifferle, R. E., Shostad, S. A., Bayers-Thering, M. T., Dyer, D. W., and Neiders, M. E. (1996) Effect of protoporphyrin IX limitation on Porphyromonas gingivalis. J. Endod. 22, 352-355 (Pubitemid 126730469)
    • (1996) Journal of Endodontics , vol.22 , Issue.7 , pp. 352-355
    • Schifferle, R.E.1
  • 13
    • 0035192014 scopus 로고    scopus 로고
    • Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model
    • DOI 10.1128/IAI.69.12.7527-7534.2001
    • O'Brien-Simpson, N. M., Paolini, R. A., Hoffmann, B., Slakeski, N., Dashper, S. G., and Reynolds, E. C. (2001) Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model. Infect. Immun. 69, 7527-7534 (Pubitemid 33086579)
    • (2001) Infection and Immunity , vol.69 , Issue.12 , pp. 7527-7534
    • O'Brien-Simpson, N.M.1    Paolini, R.A.2    Hoffmann, B.3    Slakeski, N.4    Dashper, S.G.5    Reynolds, E.C.6
  • 15
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan, A. R., and James, M. N. (1998) Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7, 815-836 (Pubitemid 28216525)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 815-836
    • Khan, A.R.1    James, M.N.G.2
  • 16
    • 0036882399 scopus 로고    scopus 로고
    • Prodomains and protein folding catalysis
    • Bryan, P. N. (2002) Prodomains and protein folding catalysis. Chem. Rev. 102, 4805-4816
    • (2002) Chem. Rev. , vol.102 , pp. 4805-4816
    • Bryan, P.N.1
  • 17
    • 2442610018 scopus 로고    scopus 로고
    • Structure-function relationships in class CA1 cysteine peptidase propeptides
    • Wiederanders, B. (2003) Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochim. Pol. 50, 691-713
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 691-713
    • Wiederanders, B.1
  • 18
    • 0028309017 scopus 로고
    • The proregion of cathepsin L is required for proper folding, stability, and ER exit
    • DOI 10.1006/abbi.1994.1203
    • Tao, K., Stearns, N. A., Dong, J., Wu, Q. L., and Sahagian, G. G. (1994) The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch Biochem. Biophys 311, 19-27 (Pubitemid 24190097)
    • (1994) Archives of Biochemistry and Biophysics , vol.311 , Issue.1 , pp. 19-27
    • Tao, K.1    Stearns, N.A.2    Dong, J.3    Wu, Q.-L.4    Sahagian, G.G.5
  • 20
    • 35548965455 scopus 로고    scopus 로고
    • Opportunities for structure-based design of protease-directed drugs
    • DOI 10.1016/j.sbi.2006.10.014, PII S0959440X06001874, Catalysis and Regulation / Proteins
    • Mittl, P. R., and Grütter, M. G. (2006) Opportunities for structure-based design of protease-directed drugs. Curr. Opin. Struct. Biol. 16, 769-775 (Pubitemid 44827737)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.6 , pp. 769-775
    • Mittl, P.R.1    Grutter, M.G.2
  • 21
    • 0028013159 scopus 로고
    • Lysine- and arginine-specific proteinases from Porphyromonas gingivalis: Isolation, characterization, and evidence for the existence of complexes with hemagglutinins
    • Pike, R., McGraw, W., Potempa, J., and Travis, J. (1994) Lysine- and arginine-specific proteinases from Porphyromonas gingivalis: isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J. Biol. Chem. 269, 406-411
    • (1994) J. Biol. Chem. , vol.269 , pp. 406-411
    • Pike, R.1    McGraw, W.2    Potempa, J.3    Travis, J.4
  • 22
    • 0033570275 scopus 로고    scopus 로고
    • Crystal structure of gingipain R: An Arg-specific bacterial cysteine proteinase with a caspase-like fold
    • DOI 10.1093/emboj/18.20.5453
    • Eichinger, A., Beisel, H. G., Jacob, U., Huber, R., Medrano, F. J., Banbula, A., Potempa, J., Travis, J., and Bode, W. (1999) Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J. 18, 5453-5462 (Pubitemid 29486365)
    • (1999) EMBO Journal , vol.18 , Issue.20 , pp. 5453-5462
    • Eichinger, A.1    Beisel, H.-G.2    Jacob, U.3    Huber, R.4    Medrano, F.-J.5    Banbula, A.6    Potempa, J.7    Travis, J.8    Bode, W.9
  • 23
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J., and Bateman, A. (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 40, D343-D350
    • (2012) Nucleic Acids Res. , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 25
    • 0038786304 scopus 로고    scopus 로고
    • Chapter 25.2.9: XDS
    • Crystallography of Biological Macromolecules. (Rossmann, M. G., and Arnold, E. eds.), 1st Ed., Kluwer Academic Publishers (for The International Union of Crystallography), Dordrecht, The Netherlands
    • Kabsch, W. (2001) Chapter 25.2.9: XDS. in International Tables for Crystallography. Volume F: Crystallography of Biological Macromolecules. (Rossmann, M. G., and Arnold, E. eds.), 1st Ed., pp 730-734, Kluwer Academic Publishers (for The International Union of Crystallography), Dordrecht, The Netherlands
    • (2001) International Tables for Crystallography , vol.F , pp. 730-734
    • Kabsch, W.1
  • 27
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modification
    • Cowtan, K. (2010) Recent developments in classical density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 470-478
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 34
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 37
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 38
    • 54249136672 scopus 로고    scopus 로고
    • Structure and mechanism of metallocarboxypeptidases
    • Gomis-Rüth, F. X. (2008) Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 43, 319-345
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 319-345
    • Gomis-Rüth, F.X.1
  • 40
    • 0031569199 scopus 로고    scopus 로고
    • The PLEES proteins: A family of structurally related enzymes widely distributed from bacteria to humans
    • Puente, X. S., and López-Otín, C. (1997) The PLEES proteins: a family of structurally related enzymes widely distributed from bacteria to humans. Biochem. J. 332, 947-949
    • (1997) Biochem. J. , vol.332 , pp. 947-949
    • Puente, X.S.1    López-Otín, C.2
  • 41
    • 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
    • DOI 10.1016/S0014-5793(98)01574-9, PII S0014579398015749
    • Chen, J. M., Rawlings, N. D., Stevens, R. A., 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 (Pubitemid 29065315)
    • (1998) FEBS Letters , vol.441 , Issue.3 , pp. 361-365
    • Chen, J.-M.1    Rawlings, N.D.2    Stevens, R.A.E.3    Barrett, A.J.4
  • 42
    • 0034613018 scopus 로고    scopus 로고
    • Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes
    • Guarné, A., Hampoelz, B., Glaser, W., Carpena, X., Tormo, J., Fita, I., and Skern, T. (2000) Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes. J. Mol. Biol. 302, 1227-1240
    • (2000) J. Mol. Biol. , vol.302 , pp. 1227-1240
    • Guarné, A.1    Hampoelz, B.2    Glaser, W.3    Carpena, X.4    Tormo, J.5    Fita, I.6    Skern, T.7
  • 43
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork, P., Holm, L., and Sander, C. (1994) The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 45
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J., and Chothia, C. (1990) The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 46
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1993.1648
    • Lawrence, M. C., and Colman, P. M. (1993) Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (Pubitemid 24027225)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 47
    • 22644435471 scopus 로고    scopus 로고
    • Fighting an enemy within: Cytoplasmic inhibitors of bacterial cysteine proteases
    • DOI 10.1111/j.1365-2958.2005.04714.x
    • Potempa, J., Golonka, E., Filipek, R., and Shaw, L. N. (2005) Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases. Mol. Microbiol. 57, 605-610 (Pubitemid 41025944)
    • (2005) Molecular Microbiology , vol.57 , Issue.3 , pp. 605-610
    • Potempa, J.1    Golonka, E.2    Filipek, R.3    Shaw, L.N.4
  • 49
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft
    • Groves, M. R., Taylor, M. A., Scott, M., Cummings, N. J., Pickersgill, R. W., and Jenkins, J. A. (1996) The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft. Structure 4, 1193-1203 (Pubitemid 27005387)
    • (1996) Structure , vol.4 , Issue.10 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.J.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 50
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R., Grochulski, P., Sivaraman, J., Ménard, R., Mort, J. S., and Cygler, M. (1996) Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15, 5492-5503 (Pubitemid 26385609)
    • (1996) EMBO Journal , vol.15 , Issue.20 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 51
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Ä resolution reveals the native active site of a papain-like cysteine protease zymogen
    • DOI 10.1006/jmbi.1997.1218
    • Podobnik, M., Kuhelj, R., Turk, V., and Turk, D. (1997) Crystal structure of the wild-type human procathepsin B at 2.5 Ä resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271, 774-788 (Pubitemid 27376053)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.5 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 52
    • 0030584678 scopus 로고    scopus 로고
    • Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion
    • Cygler, M., Sivaraman, J., Grochulski, P., Coulombe, R., Storer, A. C., and Mort, J. S. (1996) Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4, 405-416 (Pubitemid 126657535)
    • (1996) Structure , vol.4 , Issue.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.S.6
  • 53
    • 0344938353 scopus 로고    scopus 로고
    • Crystal structure of wild-type human procathepsin K
    • Sivaraman, J., Lalumière, M., Ménard, R., and Cygler, M. (1999) Crystal structure of wild-type human procathepsin K. Protein. Sci. 8, 283-290 (Pubitemid 29072428)
    • (1999) Protein Science , vol.8 , Issue.2 , pp. 283-290
    • Sivaraman, J.1    Lalumiere, M.2    Menard, R.3    Cygler, M.4
  • 54
    • 0034723144 scopus 로고    scopus 로고
    • Crystal structure of human procathepsin X: A cysteine protease with the proregion covalently linked to the active site cysteine
    • Sivaraman, J., Nägler, D. K., Zhang, R., Ménard, R., and Cygler, M. (2000) Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. J. Mol. Biol. 295, 939-951
    • (2000) J. Mol. Biol. , vol.295 , pp. 939-951
    • Sivaraman, J.1    Nägler, D.K.2    Zhang, R.3    Ménard, R.4    Cygler, M.5
  • 58
    • 65249094873 scopus 로고    scopus 로고
    • Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation
    • Elliott, J. M., Rouge, L., Wiesmann, C., and Scheer, J. M. (2009) Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation. J. Biol. Chem. 284, 6546-6553
    • (2009) J. Biol. Chem. , vol.284 , pp. 6546-6553
    • Elliott, J.M.1    Rouge, L.2    Wiesmann, C.3    Scheer, J.M.4
  • 59
  • 60
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • DOI 10.1016/S0092-8674(01)00544-X
    • Chai, J., Wu, Q., Shiozaki, E., Srinivasula, S. M., Alnemri, E. S., and Shi, Y. (2001) Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107, 399-407 (Pubitemid 33049982)
    • (2001) Cell , vol.107 , Issue.3 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 62
    • 66249094552 scopus 로고    scopus 로고
    • Mechanism of procaspase-8 activation by c-FLIPL
    • Yu, J. W., Jeffrey, P. D., and Shi, Y. (2009) Mechanism of procaspase-8 activation by c-FLIPL. Proc. Natl. Acad. Sci. U.S.A. 106, 8169-8174
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8169-8174
    • Yu, J.W.1    Jeffrey, P.D.2    Shi, Y.3
  • 63
    • 61449175831 scopus 로고    scopus 로고
    • Structural and biochemical studies on procaspase-8: New insights on initiator caspase activation
    • Keller, N., Mares, J., Zerbe, O., and Grütter, M. G. (2009) Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation. Structure 17, 438-448
    • (2009) Structure , vol.17 , pp. 438-448
    • Keller, N.1    Mares, J.2    Zerbe, O.3    Grütter, M.G.4
  • 64
    • 33646839270 scopus 로고    scopus 로고
    • Structure and activation mechanism of the Drosophila initiator caspase Dronc
    • DOI 10.1074/jbc.M513232200
    • Yan, N., Huh, J. R., Schirf, V., Demeler, B., Hay, B. A., and Shi, Y. (2006) Structure and activation mechanism of the Drosophila initiator caspase Dronc. J. Biol. Chem. 281, 8667-8674 (Pubitemid 43847971)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8667-8674
    • Yan, N.1    Huh, J.R.2    Schirf, V.3    Demeler, B.4    Hay, B.A.5    Shi, Y.6
  • 66
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • DOI 10.1042/BJ20041142
    • Fuentes-Prior, P., and Salvesen, G. S. (2004) The protein structures that shape caspase activity, specificity, activation, and inhibition. Biochem. J. 384, 201-232 (Pubitemid 39656233)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 67
    • 8344267637 scopus 로고    scopus 로고
    • Prostaphopain B structure: A comparison of proregion-mediated and staphostatin-mediated protease inhibition
    • DOI 10.1021/bi048661m
    • Filipek, R., Szczepanowski, R., Sabat, A., Potempa, J., and Bochtler, M. (2004) Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition. Biochemistry 43, 14306-14315 (Pubitemid 39482781)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14306-14315
    • Filipek, R.1    Szczepanowski, R.2    Sabat, A.3    Potempa, J.4    Bochtler, M.5
  • 70
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 71
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • Weiss, M. S. (2001) Global indicators of X-ray data quality. J. Appl. Crystallogr. 34, 130-135
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 130-135
    • Weiss, M.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.