메뉴 건너뛰기




Volumn 3, Issue 10, 2012, Pages 769-780

An octamer of enolase from Streptococcus suis

Author keywords

enolase; octamer; plasminogen binding; Streptococcus suis; structure

Indexed keywords

ENOLASE; PLASMINOGEN; SS2 ENOLASE; UNCLASSIFIED DRUG;

EID: 84878097610     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-012-2040-7     Document Type: Article
Times cited : (30)

References (52)
  • 2
    • 52449135569 scopus 로고    scopus 로고
    • alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis
    • Agarwal, S., Kulshreshtha, P., Mukku, D. B., and Bhatnagar, R. (2008). alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis. Bba-Proteins Proteom 1784, 986-994.
    • (2008) Bba-Proteins Proteom , vol.1784 , pp. 986-994
    • Agarwal, S.1    Kulshreshtha, P.2    Mukku, D.B.3    Bhatnagar, R.4
  • 3
    • 0031552061 scopus 로고    scopus 로고
    • The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein
    • Andronicos, N. M., Ranson, M., Bognacki, J., and Baker, M. S. (1997). The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein. Bba-Protein Struct M 1337, 27-39.
    • (1997) Bba-Protein Struct M , vol.1337 , pp. 27-39
    • Andronicos, N.M.1    Ranson, M.2    Bognacki, J.3    Baker, M.S.4
  • 5
    • 0016810498 scopus 로고
    • Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data
    • Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., Wilson, I. A., Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., et al. (1975). Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2. 5 angstrom resolution using amino acid sequence data. Nature 255, 609-614.
    • (1975) Nature , vol.255 , pp. 609-614
    • Banner, D.W.1    Bloomer, A.C.2    Petsko, G.A.3    Phillips, D.C.4    Pogson, C.I.5    Wilson, I.A.6    Corran, P.H.7    Furth, A.J.8    Milman, J.D.9    Offord, R.E.10
  • 6
    • 33750481888 scopus 로고    scopus 로고
    • Identification of a novel virulence determinant with serum opacification activity in Streptococcus suis
    • Baums, C. G., Kaim, U., Fulde, M., Ramachandran, G., Goethe, R., and Valentin-Weigand, P. (2006). Identification of a novel virulence determinant with serum opacification activity in Streptococcus suis. Infect Immun 74, 6154-6162.
    • (2006) Infect Immun , vol.74 , pp. 6154-6162
    • Baums, C.G.1    Kaim, U.2    Fulde, M.3    Ramachandran, G.4    Goethe, R.5    Valentin-Weigand, P.6
  • 7
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S., Rohde, M., Chhatwal, G. S., and Hammerschmidt, S. (2001). alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40, 1273-1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 8
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann, S., Wild, D., Diekmann, O., Frank, R., Bracht, D., Chhatwal, G. S., and Hammerschmidt, S. (2003). Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol 49, 411-423.
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 9
    • 0032422012 scopus 로고    scopus 로고
    • A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis
    • Brown, C. K., Kuhlman, P. L., Mattingly, S., Slates, K., Calie, P. J., and Farrar, W. W. (1998). A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis. J Protein Chem 17, 855-866.
    • (1998) J Protein Chem , vol.17 , pp. 855-866
    • Brown, C.K.1    Kuhlman, P.L.2    Mattingly, S.3    Slates, K.4    Calie, P.J.5    Farrar, W.W.6
  • 11
    • 33645097025 scopus 로고    scopus 로고
    • Recognition of enolase in the Escherichia coli RNA degradosome
    • Chandran, V., and Luisi, B. F. (2006). Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol 358, 8-15.
    • (2006) J Mol Biol , vol.358 , pp. 8-15
    • Chandran, V.1    Luisi, B.F.2
  • 12
    • 55849107401 scopus 로고    scopus 로고
    • A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates
    • Chen, C., Tang, J., Dong, W., Wang, C., Feng, Y., Wang, J., Zheng, F., Pan, X., Liu, D., Li, M., et al. (2007). A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates. Plos One 2, e315.
    • (2007) Plos One , vol.2
    • Chen, C.1    Tang, J.2    Dong, W.3    Wang, C.4    Feng, Y.5    Wang, J.6    Zheng, F.7    Pan, X.8    Liu, D.9    Li, M.10
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite:programs for protein crystallography
    • collaborative
    • collaborative. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol crystallography 50, 760-763.
    • (1994) Acta Crystallogr D Biol Crystallography , vol.50 , pp. 760-763
  • 15
    • 0346881417 scopus 로고    scopus 로고
    • Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci
    • Derbise, A., Song, Y. P., Parikh, S., Fischetti, V. A., and Pancholi, V. (2004). Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci. Infect Immun 72, 94-105.
    • (2004) Infect Immun , vol.72 , pp. 94-105
    • Derbise, A.1    Song, Y.P.2    Parikh, S.3    Fischetti, V.A.4    Pancholi, V.5
  • 16
    • 5144224570 scopus 로고    scopus 로고
    • Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites
    • Ehinger, S., Schubert, W. D., Bergmann, S., Hammerschmidt, S., and Heinz, D. W. (2004). Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites. J Mol Biol 343, 997-1005.
    • (2004) J Mol Biol , vol.343 , pp. 997-1005
    • Ehinger, S.1    Schubert, W.D.2    Bergmann, S.3    Hammerschmidt, S.4    Heinz, D.W.5
  • 17
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and 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
  • 18
    • 53449101619 scopus 로고    scopus 로고
    • Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis
    • Esgleas, M., Li, Y., Hancock, M. A., Harel, J., Dubreuil, J. D., and Gottschalk, M. (2008). Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis. Microbiology 154, 2668-2679.
    • (2008) Microbiology , vol.154 , pp. 2668-2679
    • Esgleas, M.1    Li, Y.2    Hancock, M.A.3    Harel, J.4    Dubreuil, J.D.5    Gottschalk, M.6
  • 19
    • 70449723681 scopus 로고    scopus 로고
    • Streptococcus suis enolase functions as a protective antigen displayed on the bacterial cell surface
    • Feng, Y., Pan, X., Sun, W., Wang, C., Zhang, H., Li, X., Ma, Y., Shao, Z., Ge, J., Zheng, F., et al. (2009). Streptococcus suis enolase functions as a protective antigen displayed on the bacterial cell surface. J Infect Dis 200, 1583-1592.
    • (2009) J Infect Dis , vol.200 , pp. 1583-1592
    • Feng, Y.1    Pan, X.2    Sun, W.3    Wang, C.4    Zhang, H.5    Li, X.6    Ma, Y.7    Shao, Z.8    Ge, J.9    Zheng, F.10
  • 20
    • 77449130855 scopus 로고    scopus 로고
    • Uncovering newly emerging variants of Streptococcus suis, an important zoonotic agent
    • Feng, Y., Zhang, H., Ma, Y., and Gao, G. F. (2010). Uncovering newly emerging variants of Streptococcus suis, an important zoonotic agent. Trends Microbiol 18, 124-131.
    • (2010) Trends Microbiol , vol.18 , pp. 124-131
    • Feng, Y.1    Zhang, H.2    Ma, Y.3    Gao, G.F.4
  • 21
    • 84855286291 scopus 로고    scopus 로고
    • Divergent evolution in enolase superfamily: strategies for assigning functions
    • Gerlt, J. A., Babbitt, P. C., Jacobson, M. P., and Almo, S. C. (2012). Divergent evolution in enolase superfamily: strategies for assigning functions. J Biol Chem 287, 29-34.
    • (2012) J Biol Chem , vol.287 , pp. 29-34
    • Gerlt, J.A.1    Babbitt, P.C.2    Jacobson, M.P.3    Almo, S.C.4
  • 22
    • 9744279773 scopus 로고    scopus 로고
    • Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity
    • Gerlt, J. A., Babbitt, P. C., and Rayment, I. (2005). Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch Biochem Biophys 433, 59-70.
    • (2005) Arch Biochem Biophys , vol.433 , pp. 59-70
    • Gerlt, J.A.1    Babbitt, P.C.2    Rayment, I.3
  • 24
    • 84863648388 scopus 로고    scopus 로고
    • The two-component system Ihk/Irr contributes to the virulence of Streptococcus suis serotype 2 strain 05ZYH33 through alteration of the bacterial cell metabolism
    • In Press
    • Han, H., Liu, C., Wang, Q., Xuan, C., Zheng, B., Tang, J., Yan, J., Zhang, J., Li, M., Cheng, H., et al. (2012). The two-component system Ihk/Irr contributes to the virulence of Streptococcus suis serotype 2 strain 05ZYH33 through alteration of the bacterial cell metabolism. Microbiology. (In Press).
    • (2012) Microbiology
    • Han, H.1    Liu, C.2    Wang, Q.3    Xuan, C.4    Zheng, B.5    Tang, J.6    Yan, J.7    Zhang, J.8    Li, M.9    Cheng, H.10
  • 25
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L., and Sander, C. (1996). Mapping the protein universe. Science 273, 595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 26
    • 0041810543 scopus 로고    scopus 로고
    • Crystal structure of Enterococcus hirae enolase at 2.8 A resolution
    • Hosaka, T., Meguro, T., Yamato, I., and Shirakihara, Y. (2003). Crystal structure of Enterococcus hirae enolase at 2. 8 A resolution. J Biochem 133, 817-823.
    • (2003) J Biochem , vol.133 , pp. 817-823
    • Hosaka, T.1    Meguro, T.2    Yamato, I.3    Shirakihara, Y.4
  • 27
    • 36048997622 scopus 로고    scopus 로고
    • Cloning and characterization of an alpha-enolase of the oral pathogen Streptococcus mutans that binds human plasminogen
    • Jones, M. N., and Holt, R. G. (2007). Cloning and characterization of an alpha-enolase of the oral pathogen Streptococcus mutans that binds human plasminogen. Biochem Bioph Res Co 364, 924-929.
    • (2007) Biochem Bioph Res Co , vol.364 , pp. 924-929
    • Jones, M.N.1    Holt, R.G.2
  • 28
    • 45749150355 scopus 로고    scopus 로고
    • Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme
    • Kang, H. J., Jung, S. K., Kim, S. J., and Chung, S. J. (2008). Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. Acta Crystallogr D Biol Crystallogr 64, 651-657.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 651-657
    • Kang, H.J.1    Jung, S.K.2    Kim, S.J.3    Chung, S.J.4
  • 29
    • 77952505984 scopus 로고    scopus 로고
    • Dissociation of the octameric enolase from S. pyogenes-one interface stabilizes another
    • Karbassi, F., Quiros, V., Pancholi, V., and Kornblatt, M. J. (2010). Dissociation of the octameric enolase from S. pyogenes-one interface stabilizes another. Plos One 5, e8810.
    • (2010) Plos One , vol.5
    • Karbassi, F.1    Quiros, V.2    Pancholi, V.3    Kornblatt, M.J.4
  • 30
    • 0035955548 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli RNA degradosome component enolase
    • Kuhnel, K., and Luisi, B. F. (2001). Crystal structure of the Escherichia coli RNA degradosome component enolase. J Mol Biol 313, 583-592.
    • (2001) J Mol Biol , vol.313 , pp. 583-592
    • Kuhnel, K.1    Luisi, B.F.2
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thorton, 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    Thorton, J.M.4
  • 32
    • 79952410859 scopus 로고    scopus 로고
    • GI-type T4SS-mediated horizontal transfer of the 89K pathogenicity island in epidemic Streptococcus suis serotype 2
    • Li, M., Shen, X., Yan, J., Han, H., Zheng, B., Liu, D., Cheng, H., Zhao, Y., Rao, X., Wang, C., et al. (2011). GI-type T4SS-mediated horizontal transfer of the 89K pathogenicity island in epidemic Streptococcus suis serotype 2. Mol Microbiol 79, 1670-1683.
    • (2011) Mol Microbiol , vol.79 , pp. 1670-1683
    • Li, M.1    Shen, X.2    Yan, J.3    Han, H.4    Zheng, B.5    Liu, D.6    Cheng, H.7    Zhao, Y.8    Rao, X.9    Wang, C.10
  • 33
    • 47749113315 scopus 로고    scopus 로고
    • SalK/SalR, a two-component signal transduction system, is essential for full virulence of highly invasive Streptococcus suis serotype 2
    • Li, M., Wang, C., Feng, Y., Pan, X., Cheng, G., Wang, J., Ge, J., Zheng, F., Cao, M., Dong, Y., et al. (2008). SalK/SalR, a two-component signal transduction system, is essential for full virulence of highly invasive Streptococcus suis serotype 2. Plos One 3, e2080.
    • (2008) Plos One , vol.3
    • Li, M.1    Wang, C.2    Feng, Y.3    Pan, X.4    Cheng, G.5    Wang, J.6    Ge, J.7    Zheng, F.8    Cao, M.9    Dong, Y.10
  • 34
    • 80051574122 scopus 로고    scopus 로고
    • A novel "open-form" structure of sortaseC from Streptococcus suis
    • Lu, G., Qi, J., Gao, F., Yan, J., Tang, J., and Gao, G. F. (2011a). A novel "open-form" structure of sortaseC from Streptococcus suis. Proteins 79, 2764-2769.
    • (2011) Proteins , vol.79 , pp. 2764-2769
    • Lu, G.1    Qi, J.2    Gao, F.3    Yan, J.4    Tang, J.5    Gao, G.F.6
  • 35
    • 79953188713 scopus 로고    scopus 로고
    • hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA
    • Lu, G., Zhang, J., Li, Y., Li, Z., Zhang, N., Xu, X., Wang, T., Guan, Z., Gao, G. F., and Yan, J. (2011b). hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA. Protein Cell 2, 64-73.
    • (2011) Protein Cell , vol.2 , pp. 64-73
    • Lu, G.1    Zhang, J.2    Li, Y.3    Li, Z.4    Zhang, N.5    Xu, X.6    Wang, T.7    Guan, Z.8    Gao, G.F.9    Yan, J.10
  • 36
    • 70349312906 scopus 로고    scopus 로고
    • Avian influenza virus, Streptococcus suis serotype 2, severe acute respiratory syndrome-coronavirus and beyond: molecular epidemiology, ecology and the situation in China
    • Ma, Y., Feng, Y., Liu, D., and Gao, G. F. (2009). Avian influenza virus, Streptococcus suis serotype 2, severe acute respiratory syndrome-coronavirus and beyond: molecular epidemiology, ecology and the situation in China. Philos Trans R Soc Lond B Biol Sci 364, 2725-2737.
    • (2009) Philos Trans R Soc Lond B Biol Sci , vol.364 , pp. 2725-2737
    • Ma, Y.1    Feng, Y.2    Liu, D.3    Gao, G.F.4
  • 37
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53, 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Academic Press)
    • Otwinowski, Z., Minor, W., and Charles W. Carter, Jr. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods in enzymology (Academic Press), pp. 307-326.
    • (1997) Methods in enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter Jr., C.W.3
  • 40
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • Pancholi, V. (2001). Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 58, 902-920.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 41
    • 0028912631 scopus 로고
    • Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing
    • Schurig, H., Rutkat, K., Rachel, R., and Jaenicke, R. (1995). Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. Protein Sci 4, 228-236.
    • (1995) Protein Sci , vol.4 , pp. 228-236
    • Schurig, H.1    Rutkat, K.2    Rachel, R.3    Jaenicke, R.4
  • 42
    • 38449110766 scopus 로고    scopus 로고
    • Enolase on the surface of prockaryotic and eukaryotic cells is a receptor for human plasminogen
    • Seweryn, E., Pietkiewicz, J., Szamborska, A., and Gamian, A. (2007). [Enolase on the surface of prockaryotic and eukaryotic cells is a receptor for human plasminogen]. Postepy Hig Med Dosw (Online) 61, 672-682.
    • (2007) Postepy Hig Med Dosw (Online) , vol.61 , pp. 672-682
    • Seweryn, E.1    Pietkiewicz, J.2    Szamborska, A.3    Gamian, A.4
  • 43
    • 0033040620 scopus 로고    scopus 로고
    • Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor
    • Smith, H. E., Damman, M., van der Velde, J., Wagenaar, F., Wisselink, H. J., Stockhofe-Zurwieden, N., and Smits, M. A. (1999). Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor. Infect Immun 67, 1750-1756.
    • (1999) Infect Immun , vol.67 , pp. 1750-1756
    • Smith, H.E.1    Damman, M.2    van der Velde, J.3    Wagenaar, F.4    Wisselink, H.J.5    Stockhofe-Zurwieden, N.6    Smits, M.A.7
  • 44
    • 0025192588 scopus 로고
    • Refined structure of yeast apo-enolase at 2.25 A resolution
    • Stec, B., and Lebioda, L. (1990). Refined structure of yeast apo-enolase at 2. 25 A resolution. J Mol Biol 211, 235-248.
    • (1990) J Mol Biol , vol.211 , pp. 235-248
    • Stec, B.1    Lebioda, L.2
  • 46
    • 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
  • 47
    • 38649106736 scopus 로고    scopus 로고
    • Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins
    • Vanier, G., Sekizaki, T., Dominguez-Punaro, M. C., Esgleas, M., Osaki, M., Takamatsu, D., Segura, M., and Gottschalk, M. (2008). Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins. Vet Microbiol 127, 417-424.
    • (2008) Vet Microbiol , vol.127 , pp. 417-424
    • Vanier, G.1    Sekizaki, T.2    Dominguez-Punaro, M.C.3    Esgleas, M.4    Osaki, M.5    Takamatsu, D.6    Segura, M.7    Gottschalk, M.8
  • 48
    • 58149313618 scopus 로고    scopus 로고
    • The involvement of sortase A in high virulence of STSS-causing Streptococcus suis serotype 2
    • Wang, C., Li, M., Feng, Y., Zheng, F., Dong, Y., Pan, X., Cheng, G., Dong, R., Hu, D., Feng, X., et al. (2009). The involvement of sortase A in high virulence of STSS-causing Streptococcus suis serotype 2. Arch Microbiol 191, 23-33.
    • (2009) Arch Microbiol , vol.191 , pp. 23-33
    • Wang, C.1    Li, M.2    Feng, Y.3    Zheng, F.4    Dong, Y.5    Pan, X.6    Cheng, G.7    Dong, R.8    Hu, D.9    Feng, X.10
  • 49
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: a versatile framework for efficient enzymes
    • Wierenga, R. K. (2001). The TIM-barrel fold: a versatile framework for efficient enzymes. Febs Lett 492, 193-198.
    • (2001) Febs Lett , vol.492 , pp. 193-198
    • Wierenga, R.K.1
  • 50
    • 79953148352 scopus 로고    scopus 로고
    • Crystal structure of cytotoxin protein suilysin from Streptococcus suis
    • Xu, L., Huang, B., Du, H., Zhang, X. C., Xu, J., Li, X., and Rao, Z. (2010). Crystal structure of cytotoxin protein suilysin from Streptococcus suis. Protein Cell 1, 96-105.
    • (2010) Protein Cell , vol.1 , pp. 96-105
    • Xu, L.1    Huang, B.2    Du, H.3    Zhang, X.C.4    Xu, J.5    Li, X.6    Rao, Z.7
  • 51
    • 59649104375 scopus 로고    scopus 로고
    • Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2
    • Zhang, A., Chen, B., Mu, X., Li, R., Zheng, P., Zhao, Y., Chen, H., and Jin, M. (2009). Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2. Vaccine 27, 1348-1353.
    • (2009) Vaccine , vol.27 , pp. 1348-1353
    • Zhang, A.1    Chen, B.2    Mu, X.3    Li, R.4    Zheng, P.5    Zhao, Y.6    Chen, H.7    Jin, M.8
  • 52
    • 79960044038 scopus 로고    scopus 로고
    • An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis
    • Zheng, B., Tan, S., Gao, J., Han, H., Liu, J., Lu, G., Liu, D., Yi, Y., Zhu, B., and Gao, G. F. (2011). An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis. Protein Cell 2, 250-258.
    • (2011) Protein Cell , vol.2 , pp. 250-258
    • Zheng, B.1    Tan, S.2    Gao, J.3    Han, H.4    Liu, J.5    Lu, G.6    Liu, D.7    Yi, Y.8    Zhu, B.9    Gao, G.F.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.