메뉴 건너뛰기




Volumn 76, Issue 2, 2008, Pages 523-531

Immunogenic and plasminogen-binding surface-associated α-enolase of Trichomonas vaginalis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; AMINOCAPROIC ACID; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; LIGAND; LYSINE; MONOCLONAL ANTIBODY; PLASMINOGEN; THROMBIN;

EID: 39149123184     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.01352-07     Document Type: Article
Times cited : (90)

References (59)
  • 1
    • 0020671996 scopus 로고
    • Antigen analysis of several pathogenic strains of Trichomonas vaginalis
    • Alderete, J. F. 1983. Antigen analysis of several pathogenic strains of Trichomonas vaginalis. Infect. Immun. 39:1041-1047.
    • (1983) Infect. Immun , vol.39 , pp. 1041-1047
    • Alderete, J.F.1
  • 2
    • 0021717971 scopus 로고
    • Soluble Trichomonas vaginalis antigens in cell-free culture supernatants
    • Alderete, J. F., and G. E. Garza. 1984. Soluble Trichomonas vaginalis antigens in cell-free culture supernatants. Mol. Biochem. Parasitol. 13:147-158.
    • (1984) Mol. Biochem. Parasitol , vol.13 , pp. 147-158
    • Alderete, J.F.1    Garza, G.E.2
  • 3
    • 0026321491 scopus 로고
    • The women infected with Trichomonas vaginalis have numerous proteinases and antibody to trichomonal proteinases
    • Alderete, J. F., E. Newton, C. Dennis, and K. A. Neale. 1991. The women infected with Trichomonas vaginalis have numerous proteinases and antibody to trichomonal proteinases. Genitourin. Med. 67:469-474.
    • (1991) Genitourin. Med , vol.67 , pp. 469-474
    • Alderete, J.F.1    Newton, E.2    Dennis, C.3    Neale, K.A.4
  • 4
    • 0029151459 scopus 로고
    • Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence
    • Alderete, J. F., J. L. O'Brien, R. Arroyo, J. A. Engbring, O. Musatovova, O. Lopez, C. Lauriano, and J. Nguyen. 1995. Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence. Mol. Microbiol. 17:69-83.
    • (1995) Mol. Microbiol , vol.17 , pp. 69-83
    • Alderete, J.F.1    O'Brien, J.L.2    Arroyo, R.3    Engbring, J.A.4    Musatovova, O.5    Lopez, O.6    Lauriano, C.7    Nguyen, J.8
  • 5
    • 79959954951 scopus 로고    scopus 로고
    • The vagina has reducing environment sufficient for activation of Trichomonas vaginalis cysteine proteinases
    • Alderete, J. F., and D. Provenzano. 1997. The vagina has reducing environment sufficient for activation of Trichomonas vaginalis cysteine proteinases. Genitourin. Med. 73:291-296.
    • (1997) Genitourin. Med , vol.73 , pp. 291-296
    • Alderete, J.F.1    Provenzano, D.2
  • 6
    • 0036756764 scopus 로고    scopus 로고
    • The complex fibronectin-Trichomonas vaginalis interactions and trichomonosis
    • Alderete, J. F., M. Benchimol, M. W. Lehker, and M. L. Crouch. 2002. The complex fibronectin-Trichomonas vaginalis interactions and trichomonosis. Parasitol. Int. 51:285-292.
    • (2002) Parasitol. Int , vol.51 , pp. 285-292
    • Alderete, J.F.1    Benchimol, M.2    Lehker, M.W.3    Crouch, M.L.4
  • 8
    • 0026533051 scopus 로고
    • Molecular basis of host epithelial cell recognition by Trichomonas vaginalis
    • Arroyo, R., J. Engbring, and J. F. Alderete. 1992. Molecular basis of host epithelial cell recognition by Trichomonas vaginalis. Mol. Microbiol. 6:853-862.
    • (1992) Mol. Microbiol , vol.6 , pp. 853-862
    • Arroyo, R.1    Engbring, J.2    Alderete, J.F.3
  • 9
    • 0027454897 scopus 로고
    • Signaling of Trichomonas vaginalis for amoeboid transformation and adhesin synthesis follows cytoadherence
    • Arroyo, R., A. Gonzalez-Robles, A. Martinez-Palomo, and J. F. Alderete. 1993. Signaling of Trichomonas vaginalis for amoeboid transformation and adhesin synthesis follows cytoadherence. Mol. Microbiol. 7:299-309.
    • (1993) Mol. Microbiol , vol.7 , pp. 299-309
    • Arroyo, R.1    Gonzalez-Robles, A.2    Martinez-Palomo, A.3    Alderete, J.F.4
  • 10
    • 0034931519 scopus 로고    scopus 로고
    • α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S., M. Rohde, G. S. Chhatwal, and S. Hammerschmidt. 2001. α-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
  • 11
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraledyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., M. Rohde, G. S. Chhatwal, and S. Hammerschmidt. 2004. Glyceraledyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect. Immun. 72:2416-2419.
    • (2004) Infect. Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 12
    • 1842636779 scopus 로고    scopus 로고
    • Identification of enolase as a plasminogen-binding protein in excretory-secretory products of Fasciola hepatica
    • Bernal, D., J. E. de la Rubia, A. M. Carrasco-Abad, R. Toledo, S. Mas-Coma, and A. Marcilla. 2004. Identification of enolase as a plasminogen-binding protein in excretory-secretory products of Fasciola hepatica. FEBS Lett. 563:203-206.
    • (2004) FEBS Lett , vol.563 , pp. 203-206
    • Bernal, D.1    de la Rubia, J.E.2    Carrasco-Abad, A.M.3    Toledo, R.4    Mas-Coma, S.5    Marcilla, A.6
  • 13
    • 25444529704 scopus 로고    scopus 로고
    • Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties
    • Boël, G., H. Jin, and V. Pancholi. 2005. Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties. Infect. Immun. 73:6237-6248.
    • (2005) Infect. Immun , vol.73 , pp. 6237-6248
    • Boël, G.1    Jin, H.2    Pancholi, V.3
  • 14
    • 0011793744 scopus 로고    scopus 로고
    • Casta e Silva Filho, F., W. de Souza, and J. D. Lopes. 1988. Presence of laminin-binding proteins in trichomonads and their role in adhesion. Proc. Natl. Acad. Sci. USA 85:8042-8046.
    • Casta e Silva Filho, F., W. de Souza, and J. D. Lopes. 1988. Presence of laminin-binding proteins in trichomonads and their role in adhesion. Proc. Natl. Acad. Sci. USA 85:8042-8046.
  • 15
    • 0345722746 scopus 로고    scopus 로고
    • Cates, W., Jr., and The American Social Health Association Panel. 1999. Estimates of the incidence and prevalence of sexually transmitted diseases in the United States. Sex. Transm. Dis. 26:S2-S7.
    • Cates, W., Jr., and The American Social Health Association Panel. 1999. Estimates of the incidence and prevalence of sexually transmitted diseases in the United States. Sex. Transm. Dis. 26:S2-S7.
  • 16
    • 0031587871 scopus 로고    scopus 로고
    • Plasminogen is required for efficient dissemination of B. burgdorferi in ticks and for enhancement of spirochetemia in mice
    • Coleman, J. L., J. A. Gebbia, J. Piesman, J. L. Dengen, T. H. Bugge, and J. L. Benach. 1997. Plasminogen is required for efficient dissemination of B. burgdorferi in ticks and for enhancement of spirochetemia in mice. Cell 89:1111-1119.
    • (1997) Cell , vol.89 , pp. 1111-1119
    • Coleman, J.L.1    Gebbia, J.A.2    Piesman, J.3    Dengen, J.L.4    Bugge, T.H.5    Benach, J.L.6
  • 17
    • 0032866063 scopus 로고    scopus 로고
    • Trichomonas vaginalis interactions with fibronectin and laminin
    • Crouch, M. L., and J. F. Alderete. 1999. Trichomonas vaginalis interactions with fibronectin and laminin. Microbiology 145:2835-2843.
    • (1999) Microbiology , vol.145 , pp. 2835-2843
    • Crouch, M.L.1    Alderete, J.F.2
  • 18
    • 0001419545 scopus 로고
    • The establishment of various trichomonads of animals and man in axenic cultures
    • Diamond, L. S. 1957. The establishment of various trichomonads of animals and man in axenic cultures. J. Parasitol. 43:488-490.
    • (1957) J. Parasitol , vol.43 , pp. 488-490
    • Diamond, L.S.1
  • 19
    • 0031768784 scopus 로고    scopus 로고
    • Characterization of Trichomonas vaginalis AP33 adhesin and cell surface interactive domains
    • Engbring, J. A., and J. F. Alderete. 1998. Characterization of Trichomonas vaginalis AP33 adhesin and cell surface interactive domains. Microbiology 144:3011-3018.
    • (1998) Microbiology , vol.144 , pp. 3011-3018
    • Engbring, J.A.1    Alderete, J.F.2
  • 20
    • 0037338699 scopus 로고    scopus 로고
    • Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis
    • Garcia, A. F., T. H. Chang, M. Benchimol, D. J. Klumpp, M. W. Lehker, and J. F. Alderete. 2003. Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis. Mol. Microbiol. 47:1207-1224.
    • (2003) Mol. Microbiol , vol.47 , pp. 1207-1224
    • Garcia, A.F.1    Chang, T.H.2    Benchimol, M.3    Klumpp, D.J.4    Lehker, M.W.5    Alderete, J.F.6
  • 21
    • 0037786554 scopus 로고    scopus 로고
    • Molecular cloning of an alpha-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogen
    • Jolodar, A., P. Fischer, S. Bergmann, D. W. Buttner, S. Hammerschmidt, and N. W. Brattig. 2003. Molecular cloning of an alpha-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogen. Biochim. Biophys. Acta 1627:111-120.
    • (2003) Biochim. Biophys. Acta , vol.1627 , pp. 111-120
    • Jolodar, A.1    Fischer, P.2    Bergmann, S.3    Buttner, D.W.4    Hammerschmidt, S.5    Brattig, N.W.6
  • 22
    • 0043030106 scopus 로고    scopus 로고
    • Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells
    • Jong, A. Y., S. H. Chen, M. F. Stins, K. S. Kim, T. L. Tuan, and S. H. Huang. 2003. Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells. J. Med. Microbiol. 52:615-622.
    • (2003) J. Med. Microbiol , vol.52 , pp. 615-622
    • Jong, A.Y.1    Chen, S.H.2    Stins, M.F.3    Kim, K.S.4    Tuan, T.L.5    Huang, S.H.6
  • 23
    • 0036891427 scopus 로고    scopus 로고
    • Epithelial differentiation promotes the adherence of type 1-piliated Escherichia coli to human vaginal cells
    • Klumpp, D. J., S. G. Forrestal, J. E. Karr, C. S. Mudge, B. E. Anderson, and A. J. Schaeffer. 2002. Epithelial differentiation promotes the adherence of type 1-piliated Escherichia coli to human vaginal cells. J. Infect. Dis. 186:1631-1638.
    • (2002) J. Infect. Dis , vol.186 , pp. 1631-1638
    • Klumpp, D.J.1    Forrestal, S.G.2    Karr, J.E.3    Mudge, C.S.4    Anderson, B.E.5    Schaeffer, A.J.6
  • 24
    • 19644381931 scopus 로고    scopus 로고
    • Trichomonas vaginalis adherence mediates differential gene expression in human vaginal epithelial cells
    • Kucknoor, A., V. Mundodi, and J. F. Alderete. 2005. Trichomonas vaginalis adherence mediates differential gene expression in human vaginal epithelial cells. Cell. Microbiol. 7:887-897.
    • (2005) Cell. Microbiol , vol.7 , pp. 887-897
    • Kucknoor, A.1    Mundodi, V.2    Alderete, J.F.3
  • 25
    • 25444509858 scopus 로고    scopus 로고
    • Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin
    • Kucknoor, A. S., V. Mundodi, and J. F. Alderete. 2005. Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin. BMC Mol. Biol. 6:5.
    • (2005) BMC Mol. Biol , vol.6 , pp. 5
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 26
    • 25444435394 scopus 로고    scopus 로고
    • Adherence to human vaginal epithelial cells signals for increased expression of Trichomonas vaginalis genes
    • Kucknoor, A. S., V. Mundodi, and J. F. Alderete. 2005. Adherence to human vaginal epithelial cells signals for increased expression of Trichomonas vaginalis genes. Infect. Immun. 73:6472-6478.
    • (2005) Infect. Immun , vol.73 , pp. 6472-6478
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 27
    • 34848847880 scopus 로고    scopus 로고
    • The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65
    • Kucknoor, A. S., V. Mundodi, and J. F. Alderete. 2007. The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65. Cell. Microbiol. 9:2586-2597.
    • (2007) Cell. Microbiol , vol.9 , pp. 2586-2597
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0029149950 scopus 로고
    • Bacterial plasminogen receptors: In vitro evidence for a role in degradation of the mammalian extracellular matrix
    • Lähteenmäki, K., R. Virkola, R. Pouttu, P. Kuusela, M. Kukkonen, and T. K. Korhonen. 1995. Bacterial plasminogen receptors: in vitro evidence for a role in degradation of the mammalian extracellular matrix. Infect. Immun. 63:3659-3664.
    • (1995) Infect. Immun , vol.63 , pp. 3659-3664
    • Lähteenmäki, K.1    Virkola, R.2    Pouttu, R.3    Kuusela, P.4    Kukkonen, M.5    Korhonen, T.K.6
  • 31
    • 0032825036 scopus 로고    scopus 로고
    • Trichomonad invasion of the mucous layer requires adhesins, mucinases, and motility
    • Lehker, M. W., and D. Sweeney. 1999. Trichomonad invasion of the mucous layer requires adhesins, mucinases, and motility. Sex. Transm. Infect. 75:231-238.
    • (1999) Sex. Transm. Infect , vol.75 , pp. 231-238
    • Lehker, M.W.1    Sweeney, D.2
  • 32
    • 0030959780 scopus 로고    scopus 로고
    • Streptococcus uberis acquires plasmin activity following growth in the presence of bovine plasminogen through the action of its specific plasminogen activator
    • Leigh, J. A., and R. A. Lincoln. 1997. Streptococcus uberis acquires plasmin activity following growth in the presence of bovine plasminogen through the action of its specific plasminogen activator. FEMS Microbiol. Lett. 154:123-129.
    • (1997) FEMS Microbiol. Lett , vol.154 , pp. 123-129
    • Leigh, J.A.1    Lincoln, R.A.2
  • 33
    • 0034927107 scopus 로고    scopus 로고
    • Plasmin and matrix metalloproteinases in vascular remodeling
    • Lijnen, H. R. 2001. Plasmin and matrix metalloproteinases in vascular remodeling. Thromb. Haemost. 86:324-333.
    • (2001) Thromb. Haemost , vol.86 , pp. 324-333
    • Lijnen, H.R.1
  • 34
    • 0025988405 scopus 로고
    • Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation
    • McCoy, H. E., C. C. Broder, and R. Lottenberg. 1991. Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation. J. Infect. Dis. 164:515-521.
    • (1991) J. Infect. Dis , vol.164 , pp. 515-521
    • McCoy, H.E.1    Broder, C.C.2    Lottenberg, R.3
  • 35
    • 0037165649 scopus 로고    scopus 로고
    • Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase
    • Molkanen, T., J. Tyynela, J. Helin, N. Kalkkinen, and P. Kuusela. 2002. Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase. FEBS Lett. 517:72-78.
    • (2002) FEBS Lett , vol.517 , pp. 72-78
    • Molkanen, T.1    Tyynela, J.2    Helin, J.3    Kalkkinen, N.4    Kuusela, P.5
  • 36
    • 0020315806 scopus 로고
    • Plasminogen in human saliva
    • Moody, G. H. 1982. Plasminogen in human saliva. Int. J. Oral Surg. 11:110-114.
    • (1982) Int. J. Oral Surg , vol.11 , pp. 110-114
    • Moody, G.H.1
  • 37
    • 4344563422 scopus 로고    scopus 로고
    • Silencing the ap65 gene reduces adherence to vaginal epithelial cells by Trichomonas vaginalis
    • Mundodi, V., A. S. Kucknoor, D. J. Klumpp, T. H. Chang, and J. F. Alderete. 2004. Silencing the ap65 gene reduces adherence to vaginal epithelial cells by Trichomonas vaginalis. Mol. Microbiol. 53:1099-1108.
    • (2004) Mol. Microbiol , vol.53 , pp. 1099-1108
    • Mundodi, V.1    Kucknoor, A.S.2    Klumpp, D.J.3    Chang, T.H.4    Alderete, J.F.5
  • 38
    • 34447648775 scopus 로고    scopus 로고
    • Antisense RNA decreases AP33 gene expression and cytoadherence by T. vaginalis
    • Mundodi, V., A. S. Kucknoor, and J. F. Alderete. 2007. Antisense RNA decreases AP33 gene expression and cytoadherence by T. vaginalis. BMC Microbiol. 3:64.
    • (2007) BMC Microbiol , vol.3 , pp. 64
    • Mundodi, V.1    Kucknoor, A.S.2    Alderete, J.F.3
  • 39
    • 11244271736 scopus 로고    scopus 로고
    • Regulation and interactions in the activation of cell-associated plasminogen
    • Myohanen, H., and A. Vaheri. 2004. Regulation and interactions in the activation of cell-associated plasminogen. Cell. Mol. Life Sci. 61:2840-2858.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 2840-2858
    • Myohanen, H.1    Vaheri, A.2
  • 40
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin-( ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., and V. A. Fischetti. 1998. α-Enolase, a novel strong plasmin-( ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273:14503-14515.
    • (1998) J. Biol. Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 41
    • 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
  • 42
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Pancholi, V., and G. S. Chhatwal. 2003. Housekeeping enzymes as virulence factors for pathogens. Int. J. Med. Microbiol. 293:391-401.
    • (2003) Int. J. Med. Microbiol , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 43
    • 0025913364 scopus 로고
    • Cellular regulation of fibronolysis
    • Plow, E. F., J. Felez, and L. A. Miles. 1991. Cellular regulation of fibronolysis. Thromb. Haemost. 66:32-36.
    • (1991) Thromb. Haemost , vol.66 , pp. 32-36
    • Plow, E.F.1    Felez, J.2    Miles, L.A.3
  • 45
    • 33751190062 scopus 로고    scopus 로고
    • Schistosoma bovis: Plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument
    • Ramajo-Hernandez, A., R. Perez-Sanchez, V. Ramajo-Martin, and A. Oleaga. 2007. Schistosoma bovis: plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument. Exp. Parasitol. 115:83-91.
    • (2007) Exp. Parasitol , vol.115 , pp. 83-91
    • Ramajo-Hernandez, A.1    Perez-Sanchez, R.2    Ramajo-Martin, V.3    Oleaga, A.4
  • 46
    • 0028839088 scopus 로고
    • The role of an enolase-related molecule in plasminogen binding to cells
    • Redlitz, A., B. J. Fowler, E. F. Plow, and L. A. Miles. 1995. The role of an enolase-related molecule in plasminogen binding to cells. Eur. J. Biochem. 227:407-415.
    • (1995) Eur. J. Biochem , vol.227 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 48
    • 0029691198 scopus 로고    scopus 로고
    • Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover, M. A. 1996. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 58:2271-2277.
    • (1996) Life Sci , vol.58 , pp. 2271-2277
    • Sirover, M.A.1
  • 49
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover, M. A. 1999. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta 1432:159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 53
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 54
    • 30844448754 scopus 로고    scopus 로고
    • Fluorescent labeling study of plasminogen concentration and location in simulated bovine milk systems
    • Wang, L., K. D. Hayes, and L. J. Mauer. 2006. Fluorescent labeling study of plasminogen concentration and location in simulated bovine milk systems. J. Dairy Sci. 89:58-70.
    • (2006) J. Dairy Sci , vol.89 , pp. 58-70
    • Wang, L.1    Hayes, K.D.2    Mauer, L.J.3
  • 55
    • 1342280969 scopus 로고    scopus 로고
    • Weinstock, H., S. Berman, and W. Cates, Jr. 2004. Sexually transmitted diseases among American youth: incidence and prevalence estimates, 2000. Perspect. Sex. Reprod. Health 36:6-10.
    • Weinstock, H., S. Berman, and W. Cates, Jr. 2004. Sexually transmitted diseases among American youth: incidence and prevalence estimates, 2000. Perspect. Sex. Reprod. Health 36:6-10.
  • 56
    • 0029647488 scopus 로고
    • Three hundred, thirty-three million new, STD curable cases in 1995
    • World Health Organization
    • World Health Organization. 1995. Three hundred, thirty-three million new, STD curable cases in 1995. AIDS Wkly. 1995:15-16.
    • (1995) AIDS Wkly , vol.1995 , pp. 15-16
  • 57
    • 0003514452 scopus 로고    scopus 로고
    • Global prevalence and incidence of selected curable sexually transmitted infections. Overview and estimates. World Health Organization, Geneva, Switzerland
    • World Health Organization. 2001. Global prevalence and incidence of selected curable sexually transmitted infections. Overview and estimates. World Health Organization, Geneva, Switzerland.
    • (2001) World Health Organization
  • 58
    • 0035077554 scopus 로고    scopus 로고
    • Plasminogen binding and activation by Mycoplasma fermentas
    • Yavlovich, A., A. A. Higazi, and S. Rotten. 2001. Plasminogen binding and activation by Mycoplasma fermentas. Infect. Immun. 69:1977-1982.
    • (2001) Infect. Immun , vol.69 , pp. 1977-1982
    • Yavlovich, A.1    Higazi, A.A.2    Rotten, S.3
  • 59
    • 0030827288 scopus 로고    scopus 로고
    • Mechanism of enolase: The crystal structure of asymmetric dimmer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
    • Zhang, E., J. M. Brewer, W. Minor, L. A. Carreira, and L. Lebioda. 1997. Mechanism of enolase: the crystal structure of asymmetric dimmer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution. Biochemistry 36:12526-12534.
    • (1997) Biochemistry , vol.36 , pp. 12526-12534
    • Zhang, E.1    Brewer, J.M.2    Minor, W.3    Carreira, L.A.4    Lebioda, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.