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Volumn 8, Issue 6, 2012, Pages

Crystal structures reveal the multi-ligand binding mechanism of Staphylococcus aureus ClfB

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOKERATIN 10; DERMOKINE; ENGRAILED PROTEIN; FIBRINOGEN; FIBRINOGEN ALPHA; GLYCINE; MAJOR HISTOCOMPATIBILITY ANTIGEN; PEPTIDE DERIVATIVE; PROTEIN CLFB; PROTEIN SDRG; PROTEIN TCF20; SERINE; UNCLASSIFIED DRUG; ADHESIN; CLFB PROTEIN, STAPHYLOCOCCUS AUREUS; DMKN PROTEIN, HUMAN; LIGAND; PROTEIN; TCF20 PROTEIN, HUMAN; TRANSCRIPTION FACTOR;

EID: 84864058069     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002751     Document Type: Article
Times cited : (53)

References (45)
  • 1
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy FD, (1998) Staphylococcus aureus infections. N Engl J Med 339: 520-532.
    • (1998) N Engl J Med , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 2
    • 0038015340 scopus 로고    scopus 로고
    • Fluid shear contributions to bacteria cell detachment initiated by a monoclonal antibody
    • Mascari L, Ymele-Leki P, Eggleton CD, Speziale P, Ross JM, (2003) Fluid shear contributions to bacteria cell detachment initiated by a monoclonal antibody. Biotechnol Bioeng 83: 65-74.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 65-74
    • Mascari, L.1    Ymele-Leki, P.2    Eggleton, C.D.3    Speziale, P.4    Ross, J.M.5
  • 3
    • 0036736573 scopus 로고    scopus 로고
    • Comparative proteomics of Staphylococcus aureus and the response of methicillin-resistant and methicillin-sensitive strains to Triton X-100
    • Cordwell SJ, Larsen MR, Cole RT, Walsh BJ, (2002) Comparative proteomics of Staphylococcus aureus and the response of methicillin-resistant and methicillin-sensitive strains to Triton X-100. Microbiology 148: 2765-2781.
    • (2002) Microbiology , vol.148 , pp. 2765-2781
    • Cordwell, S.J.1    Larsen, M.R.2    Cole, R.T.3    Walsh, B.J.4
  • 4
    • 0035804274 scopus 로고    scopus 로고
    • Nasal carriage as a source of Staphylococcus aureus bacteremia. Study Group
    • von Eiff C, Becker K, Machka K, Stammer H, Peters G, (2001) Nasal carriage as a source of Staphylococcus aureus bacteremia. Study Group. N Engl J Med 344: 11-16.
    • (2001) N Engl J Med , vol.344 , pp. 11-16
    • von Eiff, C.1    Becker, K.2    Machka, K.3    Stammer, H.4    Peters, G.5
  • 5
    • 4344571589 scopus 로고    scopus 로고
    • Risk and outcome of nosocomial Staphylococcus aureus bacteraemia in nasal carriers versus non-carriers
    • Wertheim HF, Vos MC, Ott A, van Belkum A, Voss A, et al. (2004) Risk and outcome of nosocomial Staphylococcus aureus bacteraemia in nasal carriers versus non-carriers. Lancet 364: 703-705.
    • (2004) Lancet , vol.364 , pp. 703-705
    • Wertheim, H.F.1    Vos, M.C.2    Ott, A.3    van Belkum, A.4    Voss, A.5
  • 6
    • 0031816677 scopus 로고    scopus 로고
    • Factors affecting the collagen binding capacity of Staphylococcus aureus
    • Gillaspy AF, Lee CY, Sau S, Cheung AL, Smeltzer MS, (1998) Factors affecting the collagen binding capacity of Staphylococcus aureus. Infect Immun 66: 3170-3178.
    • (1998) Infect Immun , vol.66 , pp. 3170-3178
    • Gillaspy, A.F.1    Lee, C.Y.2    Sau, S.3    Cheung, A.L.4    Smeltzer, M.S.5
  • 7
  • 8
    • 0027992980 scopus 로고
    • Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria
    • Navarre WW, Schneewind O, (1994) Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol Microbiol 14: 115-121.
    • (1994) Mol Microbiol , vol.14 , pp. 115-121
    • Navarre, W.W.1    Schneewind, O.2
  • 9
    • 74749090539 scopus 로고    scopus 로고
    • Structural and functional role of Staphylococcus aureus surface components recognizing adhesive matrix molecules of the host
    • Speziale P, Pietrocola G, Rindi S, Provenzano M, Provenza G, et al. (2009) Structural and functional role of Staphylococcus aureus surface components recognizing adhesive matrix molecules of the host. Future Microbiol 4: 1337-1352.
    • (2009) Future Microbiol , vol.4 , pp. 1337-1352
    • Speziale, P.1    Pietrocola, G.2    Rindi, S.3    Provenzano, M.4    Provenza, G.5
  • 10
    • 0032408683 scopus 로고    scopus 로고
    • Three new members of the serine-aspartate repeat protein multigene family of Staphylococcus aureus
    • Josefsson E, McCrea KW, Ni Eidhin D, O'Connell D, Cox J, et al. (1998) Three new members of the serine-aspartate repeat protein multigene family of Staphylococcus aureus. Microbiology 144 (Pt 12): 3387-3395.
    • (1998) Microbiology , vol.144 , Issue.Pt 12 , pp. 3387-3395
    • Josefsson, E.1    McCrea, K.W.2    Ni Eidhin, D.3    O'Connell, D.4    Cox, J.5
  • 11
    • 33644923551 scopus 로고    scopus 로고
    • Distribution of the serine-aspartate repeat protein-encoding sdr genes among nasal-carriage and invasive Staphylococcus aureus strains
    • Sabat A, Melles DC, Martirosian G, Grundmann H, van Belkum A, et al. (2006) Distribution of the serine-aspartate repeat protein-encoding sdr genes among nasal-carriage and invasive Staphylococcus aureus strains. J Clin Microbiol 44: 1135-1138.
    • (2006) J Clin Microbiol , vol.44 , pp. 1135-1138
    • Sabat, A.1    Melles, D.C.2    Martirosian, G.3    Grundmann, H.4    van Belkum, A.5
  • 12
    • 0027531317 scopus 로고
    • Adhesion of Staphylococcus aureus to surface-bound platelets: role of fibrinogen/fibrin and platelet integrins
    • Herrmann M, Lai QJ, Albrecht RM, Mosher DF, Proctor RA, (1993) Adhesion of Staphylococcus aureus to surface-bound platelets: role of fibrinogen/fibrin and platelet integrins. J Infect Dis 167: 312-322.
    • (1993) J Infect Dis , vol.167 , pp. 312-322
    • Herrmann, M.1    Lai, Q.J.2    Albrecht, R.M.3    Mosher, D.F.4    Proctor, R.A.5
  • 13
    • 0028334112 scopus 로고
    • Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus
    • McDevitt D, Francois P, Vaudaux P, Foster TJ, (1994) Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus. Mol Microbiol 11: 237-248.
    • (1994) Mol Microbiol , vol.11 , pp. 237-248
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 14
    • 0028834487 scopus 로고
    • Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis
    • Moreillon P, Entenza JM, Francioli P, McDevitt D, Foster TJ, et al. (1995) Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis. Infect Immun 63: 4738-4743.
    • (1995) Infect Immun , vol.63 , pp. 4738-4743
    • Moreillon, P.1    Entenza, J.M.2    Francioli, P.3    McDevitt, D.4    Foster, T.J.5
  • 15
    • 15444353754 scopus 로고    scopus 로고
    • Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus
    • Ni Eidhin D, Perkins S, Francois P, Vaudaux P, Hook M, et al. (1998) Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus. Mol Microbiol 30: 245-257.
    • (1998) Mol Microbiol , vol.30 , pp. 245-257
    • Ni Eidhin, D.1    Perkins, S.2    Francois, P.3    Vaudaux, P.4    Hook, M.5
  • 16
    • 0035976893 scopus 로고    scopus 로고
    • Structural organization of the fibrinogen-binding region of the clumping factor B MSCRAMM of Staphylococcus aureus
    • Perkins S, Walsh EJ, Deivanayagam CC, Narayana SV, Foster TJ, et al. (2001) Structural organization of the fibrinogen-binding region of the clumping factor B MSCRAMM of Staphylococcus aureus. J Biol Chem 276: 44721-44728.
    • (2001) J Biol Chem , vol.276 , pp. 44721-44728
    • Perkins, S.1    Walsh, E.J.2    Deivanayagam, C.C.3    Narayana, S.V.4    Foster, T.J.5
  • 17
    • 0036854622 scopus 로고    scopus 로고
    • Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: implications for nasal colonization
    • O'Brien LM, Walsh EJ, Massey RC, Peacock SJ, Foster TJ, (2002) Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: implications for nasal colonization. Cell Microbiol 4: 759-770.
    • (2002) Cell Microbiol , vol.4 , pp. 759-770
    • O'Brien, L.M.1    Walsh, E.J.2    Massey, R.C.3    Peacock, S.J.4    Foster, T.J.5
  • 18
    • 10944263785 scopus 로고    scopus 로고
    • Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10
    • Walsh EJ, O'Brien LM, Liang X, Hook M, Foster TJ, (2004) Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10. J Biol Chem 279: 50691-50699.
    • (2004) J Biol Chem , vol.279 , pp. 50691-50699
    • Walsh, E.J.1    O'Brien, L.M.2    Liang, X.3    Hook, M.4    Foster, T.J.5
  • 19
    • 0035951871 scopus 로고    scopus 로고
    • Identification of residues in the Staphylococcus aureus fibrinogen-binding MSCRAMM clumping factor A (ClfA) that are important for ligand binding
    • Hartford OM, Wann ER, Hook M, Foster TJ, (2001) Identification of residues in the Staphylococcus aureus fibrinogen-binding MSCRAMM clumping factor A (ClfA) that are important for ligand binding. J Biol Chem 276: 2466-2473.
    • (2001) J Biol Chem , vol.276 , pp. 2466-2473
    • Hartford, O.M.1    Wann, E.R.2    Hook, M.3    Foster, T.J.4
  • 20
    • 0030758696 scopus 로고    scopus 로고
    • Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen
    • McDevitt D, Nanavaty T, House-Pompeo K, Bell E, Turner N, et al. (1997) Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen. Eur J Biochem 247: 416-424.
    • (1997) Eur J Biochem , vol.247 , pp. 416-424
    • McDevitt, D.1    Nanavaty, T.2    House-Pompeo, K.3    Bell, E.4    Turner, N.5
  • 21
    • 0142227210 scopus 로고    scopus 로고
    • A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen
    • Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, et al. (2003) A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen. Cell 115: 217-228.
    • (2003) Cell , vol.115 , pp. 217-228
    • Ponnuraj, K.1    Bowden, M.G.2    Davis, S.3    Gurusiddappa, S.4    Moore, D.5
  • 22
    • 17144371855 scopus 로고    scopus 로고
    • The cornified envelope: a model of cell death in the skin
    • Candi E, Schmidt R, Melino G, (2005) The cornified envelope: a model of cell death in the skin. Nat Rev Mol Cell Biol 6: 328-340.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 328-340
    • Candi, E.1    Schmidt, R.2    Melino, G.3
  • 23
  • 24
    • 33645532283 scopus 로고    scopus 로고
    • Immunization with Staphylococcus aureus clumping factor B, a major determinant in nasal carriage, reduces nasal colonization in a murine model
    • Schaffer AC, Solinga RM, Cocchiaro J, Portoles M, Kiser KB, et al. (2006) Immunization with Staphylococcus aureus clumping factor B, a major determinant in nasal carriage, reduces nasal colonization in a murine model. Infect Immun 74: 2145-2153.
    • (2006) Infect Immun , vol.74 , pp. 2145-2153
    • Schaffer, A.C.1    Solinga, R.M.2    Cocchiaro, J.3    Portoles, M.4    Kiser, K.B.5
  • 25
    • 0036093924 scopus 로고    scopus 로고
    • Multiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A
    • O'Brien L, Kerrigan SW, Kaw G, Hogan M, Penades J, et al. (2002) Multiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A. Mol Microbiol 44: 1033-1044.
    • (2002) Mol Microbiol , vol.44 , pp. 1033-1044
    • O'Brien, L.1    Kerrigan, S.W.2    Kaw, G.3    Hogan, M.4    Penades, J.5
  • 26
    • 0033857887 scopus 로고    scopus 로고
    • Contribution of clumping factor B to pathogenesis of experimental endocarditis due to Staphylococcus aureus
    • Entenza JM, Foster TJ, Eidhin DN, Vaudaux P, Francioli P, et al. (2000) Contribution of clumping factor B to pathogenesis of experimental endocarditis due to Staphylococcus aureus. Infect Immun 68: 5443-5446.
    • (2000) Infect Immun , vol.68 , pp. 5443-5446
    • Entenza, J.M.1    Foster, T.J.2    Eidhin, D.N.3    Vaudaux, P.4    Francioli, P.5
  • 27
    • 39749134910 scopus 로고    scopus 로고
    • Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the alphaC-domain of human fibrinogen
    • Walsh EJ, Miajlovic H, Gorkun OV, Foster TJ, (2008) Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the alphaC-domain of human fibrinogen. Microbiology 154: 550-558.
    • (2008) Microbiology , vol.154 , pp. 550-558
    • Walsh, E.J.1    Miajlovic, H.2    Gorkun, O.V.3    Foster, T.J.4
  • 28
    • 57149093798 scopus 로고    scopus 로고
    • A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics
    • Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, et al. (2008) A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog 4: e1000226.
    • (2008) PLoS Pathog , vol.4
    • Ganesh, V.K.1    Rivera, J.J.2    Smeds, E.3    Ko, Y.P.4    Bowden, M.G.5
  • 29
    • 79960422109 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions
    • Ganesh VK, Barbu EM, Deivanayagam CC, Le B, Anderson AS, et al. (2011) Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions. J Biol Chem 286: 25963-25972.
    • (2011) J Biol Chem , vol.286 , pp. 25963-25972
    • Ganesh, V.K.1    Barbu, E.M.2    Deivanayagam, C.C.3    Le, B.4    Anderson, A.S.5
  • 30
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, et al. (2002) A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A. EMBO J 21: 6660-6672.
    • (2002) EMBO J , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5
  • 31
    • 77949904457 scopus 로고    scopus 로고
    • Molecular characterization of the interaction of staphylococcal microbial surface components recognizing adhesive matrix molecules (MSCRAMM) ClfA and Fbl with fibrinogen
    • Geoghegan JA, Ganesh VK, Smeds E, Liang X, Hook M, et al. (2010) Molecular characterization of the interaction of staphylococcal microbial surface components recognizing adhesive matrix molecules (MSCRAMM) ClfA and Fbl with fibrinogen. J Biol Chem 285: 6208-6216.
    • (2010) J Biol Chem , vol.285 , pp. 6208-6216
    • Geoghegan, J.A.1    Ganesh, V.K.2    Smeds, E.3    Liang, X.4    Hook, M.5
  • 32
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved
    • DeLano WL, (2002) The PyMOL molecular graphics system. Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
    • (2002)
    • DeLano, W.L.1
  • 33
    • 10944263785 scopus 로고    scopus 로고
    • Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10
    • Walsh EJ, O'Brien LM, Liang XW, Hook M, Foster TJ, (2004) Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10. J Biol Chem 279: 50691-50699.
    • (2004) J Biol Chem , vol.279 , pp. 50691-50699
    • Walsh, E.J.1    O'Brien, L.M.2    Liang, X.W.3    Hook, M.4    Foster, T.J.5
  • 34
    • 0037150105 scopus 로고    scopus 로고
    • Structural organization of the fibrin(ogen) alpha C-domain
    • Tsurupa G, Tsonev L, Medved L, (2002) Structural organization of the fibrin(ogen) alpha C-domain. Biochemistry 41: 6449-6459.
    • (2002) Biochemistry , vol.41 , pp. 6449-6459
    • Tsurupa, G.1    Tsonev, L.2    Medved, L.3
  • 35
    • 3042568765 scopus 로고    scopus 로고
    • Identification of novel keratinocyte-secreted peptides dermokine-alpha/-beta and a new stratified epithelium-secreted protein gene complex on human chromosome 19q13.1
    • Matsui T, Hayashi-Kisumi F, Kinoshita Y, Katahira S, Morita K, et al. (2004) Identification of novel keratinocyte-secreted peptides dermokine-alpha/-beta and a new stratified epithelium-secreted protein gene complex on human chromosome 19q13.1. Genomics 84: 384-397.
    • (2004) Genomics , vol.84 , pp. 384-397
    • Matsui, T.1    Hayashi-Kisumi, F.2    Kinoshita, Y.3    Katahira, S.4    Morita, K.5
  • 36
    • 3142602945 scopus 로고    scopus 로고
    • Identification of a conserved cluster of skin-specific genes encoding secreted proteins
    • Moffatt P, Salois P, St-Amant N, Gaumond M-H, Lanctot C, (2004) Identification of a conserved cluster of skin-specific genes encoding secreted proteins. Gene 334: 123-131.
    • (2004) Gene , vol.334 , pp. 123-131
    • Moffatt, P.1    Salois, P.2    St-Amant, N.3    Gaumond, M.-H.4    Lanctot, C.5
  • 37
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre WW, Schneewind O, (1999) Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 63: 174-229.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 38
    • 23744478147 scopus 로고    scopus 로고
    • Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus
    • Sinha B, Herrmann M, (2005) Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus. Thromb Haemost 94: 266-277.
    • (2005) Thromb Haemost , vol.94 , pp. 266-277
    • Sinha, B.1    Herrmann, M.2
  • 39
    • 0025913445 scopus 로고
    • Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium
    • Jancarik J, Scott WG, Milligan DL, Koshland DE Jr, Kim SH, (1991) Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. J Mol Biol 221: 31-34.
    • (1991) J Mol Biol , vol.221 , pp. 31-34
    • Jancarik, J.1    Scott, W.G.2    Milligan, D.L.3    Koshland Jr., D.E.4    Kim, S.H.5
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • In: Carter CW, Sweet RM, editors, San Diego, Academic Press
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. In: Carter CW, Sweet RM, editors. Macromolecular Crystallography San Diego Academic Press pp. 307-326.
    • (1997) Macromolecular Crystallography , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • Cowtan KD, Main P, (1993) Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr D Biol Crystallogr 49: 148-157.
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 44
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


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