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Volumn 89, Issue 5, 2013, Pages 903-917

Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis

Author keywords

[No Author keywords available]

Indexed keywords

GINGIPAIN; GLYCAN; MEMBRANE PROTEIN; PROTEINASE; RGPB PROTEASE; UNCLASSIFIED DRUG;

EID: 84883181202     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12319     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0035159818 scopus 로고    scopus 로고
    • vimA gene downstream of recA is involved in virulence modulation in Porphyromonas gingivalis W83
    • Abaibou, H., Chen, Z., Olango, G.J., Liu, Y., Edwards, J., and Fletcher, H.M. (2001) vimA gene downstream of recA is involved in virulence modulation in Porphyromonas gingivalis W83. Infect Immun 69: 325-335.
    • (2001) Infect Immun , vol.69 , pp. 325-335
    • Abaibou, H.1    Chen, Z.2    Olango, G.J.3    Liu, Y.4    Edwards, J.5    Fletcher, H.M.6
  • 2
    • 84857356491 scopus 로고    scopus 로고
    • A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases
    • Charbonneau, M.E., Cote, J.P., Haurat, M.F., Reiz, B., Crepin, S., Berthiaume, F., etal. (2012) A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases. Mol Microbiol 83: 894-907.
    • (2012) Mol Microbiol , vol.83 , pp. 894-907
    • Charbonneau, M.E.1    Cote, J.P.2    Haurat, M.F.3    Reiz, B.4    Crepin, S.5    Berthiaume, F.6
  • 3
    • 0037189490 scopus 로고    scopus 로고
    • CPG70 is a novel basic metallocarboxypeptidase with C-terminal polycystic kidney disease domains from Porphyromonas gingivalis
    • Chen, Y.Y., Cross, K.J., Paolini, R.A., Fielding, J.E., Slakeski, N., and Reynolds, E.C. (2002) CPG70 is a novel basic metallocarboxypeptidase with C-terminal polycystic kidney disease domains from Porphyromonas gingivalis. J Biol Chem 277: 23433-23440.
    • (2002) J Biol Chem , vol.277 , pp. 23433-23440
    • Chen, Y.Y.1    Cross, K.J.2    Paolini, R.A.3    Fielding, J.E.4    Slakeski, N.5    Reynolds, E.C.6
  • 4
    • 79951811721 scopus 로고    scopus 로고
    • The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis
    • Chen, Y.Y., Peng, B., Yang, Q., Glew, M.D., Veith, P.D., Cross, K.J., etal. (2011) The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis. Mol Microbiol 79: 1380-1401.
    • (2011) Mol Microbiol , vol.79 , pp. 1380-1401
    • Chen, Y.Y.1    Peng, B.2    Yang, Q.3    Glew, M.D.4    Veith, P.D.5    Cross, K.J.6
  • 5
    • 16544395270 scopus 로고    scopus 로고
    • Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4h.
    • Chiu, J., March, P.E., Lee, R., and Tillett, D. (2004) Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4h. Nucleic Acids Res 32: e174.
    • (2004) Nucleic Acids Res , vol.32
    • Chiu, J.1    March, P.E.2    Lee, R.3    Tillett, D.4
  • 6
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue
    • Desvaux, M., Hebraud, M., Talon, R., and Henderson, I.R. (2009) Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 17: 139-145.
    • (2009) Trends Microbiol , vol.17 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 7
    • 0033570275 scopus 로고    scopus 로고
    • Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold
    • Eichinger, A., Beisel, H.G., Jacob, U., Huber, R., Medrano, F.J., Banbula, A., etal. (1999) Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J 18: 5453-5462.
    • (1999) EMBO J , vol.18 , pp. 5453-5462
    • Eichinger, A.1    Beisel, H.G.2    Jacob, U.3    Huber, R.4    Medrano, F.J.5    Banbula, A.6
  • 8
    • 75149168105 scopus 로고    scopus 로고
    • High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism
    • Fitzpatrick, R.E., Aprico, A., Wijeyewickrema, L.C., Pagel, C.N., Wong, D.M., Potempa, J., etal. (2009) High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism. J Innate Immun 1: 109-117.
    • (2009) J Innate Immun , vol.1 , pp. 109-117
    • Fitzpatrick, R.E.1    Aprico, A.2    Wijeyewickrema, L.C.3    Pagel, C.N.4    Wong, D.M.5    Potempa, J.6
  • 9
    • 2942544238 scopus 로고    scopus 로고
    • Innate immune recognition of invasive bacteria accelerates atherosclerosis in apolipoprotein E-deficient mice
    • Gibson, F.C., 3rd, Hong, C., Chou, H.H., Yumoto, H., Chen, J., Lien, E., etal. (2004) Innate immune recognition of invasive bacteria accelerates atherosclerosis in apolipoprotein E-deficient mice. Circulation 109: 2801-2806.
    • (2004) Circulation , vol.109 , pp. 2801-2806
    • Gibson 3rd, F.C.1    Hong, C.2    Chou, H.H.3    Yumoto, H.4    Chen, J.5    Lien, E.6
  • 10
    • 84863806174 scopus 로고    scopus 로고
    • PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis
    • Glew, M.D., Veith, P.D., Peng, B., Chen, Y.Y., Gorasia, D.G., Yang, Q., etal. (2012) PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis. J Biol Chem 287: 24605-24617.
    • (2012) J Biol Chem , vol.287 , pp. 24605-24617
    • Glew, M.D.1    Veith, P.D.2    Peng, B.3    Chen, Y.Y.4    Gorasia, D.G.5    Yang, Q.6
  • 11
    • 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
  • 12
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family: sequence analysis and 3D structure comparisons
    • Halaby, D.M., Poupon, A., and Mornon, J. (1999) The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Protein Eng 12: 563-571.
    • (1999) Protein Eng , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.3
  • 13
    • 0035447136 scopus 로고    scopus 로고
    • Local and spatial factors determining HIV-1 protease substrate recognition
    • Hazebrouck, S., Machtelinckx-Delmas, V., Kupiec, J.J., and Sonigo, P. (2001) Local and spatial factors determining HIV-1 protease substrate recognition. Biochem J 358: 505-510.
    • (2001) Biochem J , vol.358 , pp. 505-510
    • Hazebrouck, S.1    Machtelinckx-Delmas, V.2    Kupiec, J.J.3    Sonigo, P.4
  • 14
    • 75149177562 scopus 로고    scopus 로고
    • A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037
    • Karim, A.Y., Kulczycka, M., Kantyka, T., Dubin, G., Jabaiah, A., Daugherty, P.S., etal. (2010) A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biol Chem 391: 105-117.
    • (2010) Biol Chem , vol.391 , pp. 105-117
    • Karim, A.Y.1    Kulczycka, M.2    Kantyka, T.3    Dubin, G.4    Jabaiah, A.5    Daugherty, P.S.6
  • 15
    • 0036307830 scopus 로고    scopus 로고
    • Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen
    • Kaufmann, M., Lindner, P., Honegger, A., Blank, K., Tschopp, M., Capitani, G., etal. (2002) Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen. J Mol Biol 318: 135-147.
    • (2002) J Mol Biol , vol.318 , pp. 135-147
    • Kaufmann, M.1    Lindner, P.2    Honegger, A.3    Blank, K.4    Tschopp, M.5    Capitani, G.6
  • 16
    • 84872151763 scopus 로고    scopus 로고
    • Gliding motility and Por secretion system genes are widespread among members of the phylum bacteroidetes
    • McBride, M.J., and Zhu, Y. (2013) Gliding motility and Por secretion system genes are widespread among members of the phylum bacteroidetes. J Bacteriol 195: 270-278.
    • (2013) J Bacteriol , vol.195 , pp. 270-278
    • McBride, M.J.1    Zhu, Y.2
  • 18
    • 0041335299 scopus 로고    scopus 로고
    • Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83
    • Nelson, K.E., Fleischmann, R.D., DeBoy, R.T., Paulsen, I.T., Fouts, D.E., Eisen, J.A., etal. (2003) Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83. J Bacteriol 185: 5591-5601.
    • (2003) J Bacteriol , vol.185 , pp. 5591-5601
    • Nelson, K.E.1    Fleischmann, R.D.2    DeBoy, R.T.3    Paulsen, I.T.4    Fouts, D.E.5    Eisen, J.A.6
  • 19
    • 33846604620 scopus 로고    scopus 로고
    • Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-negative bacteria?
    • Nguyen, K.A., Travis, J., and Potempa, J. (2007) Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-negative bacteria? J Bacteriol 189: 833-843.
    • (2007) J Bacteriol , vol.189 , pp. 833-843
    • Nguyen, K.A.1    Travis, J.2    Potempa, J.3
  • 21
    • 62449341627 scopus 로고    scopus 로고
    • Porphyromonas gingivalis RgpA-Kgp proteinase-adhesin complexes penetrate gingival tissue and induce proinflammatory cytokines or apoptosis in a concentration-dependent manner
    • O'Brien-Simpson, N.M., Pathirana, R.D., Walker, G.D., and Reynolds, E.C. (2009) Porphyromonas gingivalis RgpA-Kgp proteinase-adhesin complexes penetrate gingival tissue and induce proinflammatory cytokines or apoptosis in a concentration-dependent manner. Infect Immun 77: 1246-1261.
    • (2009) Infect Immun , vol.77 , pp. 1246-1261
    • O'Brien-Simpson, N.M.1    Pathirana, R.D.2    Walker, G.D.3    Reynolds, E.C.4
  • 22
    • 80051739212 scopus 로고    scopus 로고
    • Dynamics of preferential substrate recognition in HIV-1 protease: redefining the substrate envelope
    • Ozen, A., Haliloglu, T., and Schiffer, C.A. (2011) Dynamics of preferential substrate recognition in HIV-1 protease: redefining the substrate envelope. J Mol Biol 410: 726-744.
    • (2011) J Mol Biol , vol.410 , pp. 726-744
    • Ozen, A.1    Haliloglu, T.2    Schiffer, C.A.3
  • 23
    • 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
  • 24
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipains R), 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 (gingipains R), 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
  • 25
    • 0344825092 scopus 로고    scopus 로고
    • Gingipains, the major cysteine proteinases and virulence factors of Porphyromonas gingivalis: structure, function and assembly of multidomain protein complexes
    • Potempa, J., Sroka, A., Imamura, T., and Travis, J. (2003) Gingipains, the major cysteine proteinases and virulence factors of Porphyromonas gingivalis: structure, function and assembly of multidomain protein complexes. Curr Protein Pept Sci 4: 397-407.
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 397-407
    • Potempa, J.1    Sroka, A.2    Imamura, T.3    Travis, J.4
  • 26
    • 61449091498 scopus 로고    scopus 로고
    • Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3
    • Potempa, M., Potempa, J., Kantyka, T., Nguyen, K.A., Wawrzonek, K., Manandhar, S.P., etal. (2009) Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3. PLoS Pathog 5: e1000316.
    • (2009) PLoS Pathog , vol.5
    • Potempa, M.1    Potempa, J.2    Kantyka, T.3    Nguyen, K.A.4    Wawrzonek, K.5    Manandhar, S.P.6
  • 27
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes
    • Prabu-Jeyabalan, M., Nalivaika, E., and Schiffer, C.A. (2002) Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 10: 369-381.
    • (2002) Structure , vol.10 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 28
    • 79251531089 scopus 로고    scopus 로고
    • Adsorption of components of the plasma kinin-forming system on the surface of Porphyromonas gingivalis involves gingipains as the major docking platforms
    • Rapala-Kozik, M., Bras, G., Chruscicka, B., Karkowska-Kuleta, J., Sroka, A., Herwald, H., etal. (2011) Adsorption of components of the plasma kinin-forming system on the surface of Porphyromonas gingivalis involves gingipains as the major docking platforms. Infect Immun 79: 797-805.
    • (2011) Infect Immun , vol.79 , pp. 797-805
    • Rapala-Kozik, M.1    Bras, G.2    Chruscicka, B.3    Karkowska-Kuleta, J.4    Sroka, A.5    Herwald, H.6
  • 29
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., Kahne, D., and Silhavy, T.J. (2006) Advances in understanding bacterial outer-membrane biogenesis. Nat Rev Microbiol 4: 57-66.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 30
    • 77956037813 scopus 로고    scopus 로고
    • Identification of a novel Porphyromonas gingivalis outer membrane protein, PG534, required for the production of active gingipains
    • Saiki, K., and Konishi, K. (2010) Identification of a novel Porphyromonas gingivalis outer membrane protein, PG534, required for the production of active gingipains. FEMS Microbiol Lett 310: 168-174.
    • (2010) FEMS Microbiol Lett , vol.310 , pp. 168-174
    • Saiki, K.1    Konishi, K.2
  • 31
    • 76249128306 scopus 로고    scopus 로고
    • A protein secretion system linked to bacteroidete gliding motility and pathogenesis
    • Sato, K., Naito, M., Yukitake, H., Hirakawa, H., Shoji, M., McBride, M.J., etal. (2009) A protein secretion system linked to bacteroidete gliding motility and pathogenesis. Proc Natl Acad Sci USA 107: 276-281.
    • (2009) Proc Natl Acad Sci USA , vol.107 , pp. 276-281
    • Sato, K.1    Naito, M.2    Yukitake, H.3    Hirakawa, H.4    Shoji, M.5    McBride, M.J.6
  • 32
    • 33749023323 scopus 로고    scopus 로고
    • The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis
    • Seers, C.A., Slakeski, N., Veith, P.D., Nikolof, T., Chen, Y.Y., Dashper, S.G., and Reynolds, E.C. (2006) The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. J Bacteriol 188: 6376-6386.
    • (2006) J Bacteriol , vol.188 , pp. 6376-6386
    • Seers, C.A.1    Slakeski, N.2    Veith, P.D.3    Nikolof, T.4    Chen, Y.Y.5    Dashper, S.G.6    Reynolds, E.C.7
  • 33
    • 0036232069 scopus 로고    scopus 로고
    • Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains
    • Shoji, M., Ratnayake, D.B., Shi, Y., Kadowaki, T., Yamamoto, K., Yoshimura, F., etal. (2002) Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains. Microbiology 148: 1183-1191.
    • (2002) Microbiology , vol.148 , pp. 1183-1191
    • Shoji, M.1    Ratnayake, D.B.2    Shi, Y.3    Kadowaki, T.4    Yamamoto, K.5    Yoshimura, F.6
  • 34
    • 79959385024 scopus 로고    scopus 로고
    • Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35
    • Shoji, M., Sato, K., Yukitake, H., Kondo, Y., Narita, Y., Kadowaki, T., etal. (2011) Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35. PLoS ONE 6: e21372.
    • (2011) PLoS ONE , vol.6
    • Shoji, M.1    Sato, K.2    Yukitake, H.3    Kondo, Y.4    Narita, Y.5    Kadowaki, T.6
  • 35
    • 78650115933 scopus 로고    scopus 로고
    • The C-terminal domain residues important for the secretion and attachment of RgpB in Porphyromonas gingivalis
    • Slakeski, N., Seers, C.A., Ng, K., Moore, C., Cleal, S.M., Veith, P.D., etal. (2011) The C-terminal domain residues important for the secretion and attachment of RgpB in Porphyromonas gingivalis. J Bacteriol 193: 132-142.
    • (2011) J Bacteriol , vol.193 , pp. 132-142
    • Slakeski, N.1    Seers, C.A.2    Ng, K.3    Moore, C.4    Cleal, S.M.5    Veith, P.D.6
  • 36
    • 21544450833 scopus 로고    scopus 로고
    • Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83
    • Vanterpool, E., Roy, F., and Fletcher, H.M. (2005a) Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83. Infect Immun 73: 3971-3982.
    • (2005) Infect Immun , vol.73 , pp. 3971-3982
    • Vanterpool, E.1    Roy, F.2    Fletcher, H.M.3
  • 37
    • 15544371631 scopus 로고    scopus 로고
    • Altered gingipain maturation in vimA- and vimE-defective isogenic mutants of Porphyromonas gingivalis
    • Vanterpool, E., Roy, F., Sandberg, L., and Fletcher, H.M. (2005b) Altered gingipain maturation in vimA- and vimE-defective isogenic mutants of Porphyromonas gingivalis. Infect Immun 73: 1357-1366.
    • (2005) Infect Immun , vol.73 , pp. 1357-1366
    • Vanterpool, E.1    Roy, F.2    Sandberg, L.3    Fletcher, H.M.4
  • 38
    • 84877866907 scopus 로고    scopus 로고
    • Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases
    • Veillard, F., Sztukowska, M., Mizgalska, D., Ksiazek, M., Houston, J., Potempa, B., etal. (2013) Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases. Biochim Biophys Acta 1830: 4218-4228.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 4218-4228
    • Veillard, F.1    Sztukowska, M.2    Mizgalska, D.3    Ksiazek, M.4    Houston, J.5    Potempa, B.6
  • 39
    • 77955733490 scopus 로고    scopus 로고
    • Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and alpha-enolase: implications for autoimmunity in rheumatoid arthritis
    • Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K.A., Lundberg, K., etal. (2010) Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and alpha-enolase: implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum 62: 2662-2672.
    • (2010) Arthritis Rheum , vol.62 , pp. 2662-2672
    • Wegner, N.1    Wait, R.2    Sroka, A.3    Eick, S.4    Nguyen, K.A.5    Lundberg, K.6
  • 40
    • 0025012996 scopus 로고
    • Periodontal disease
    • Williams, R.C. (1990) Periodontal disease. N Engl J Med 322: 373-382.
    • (1990) N Engl J Med , vol.322 , pp. 373-382
    • Williams, R.C.1


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