메뉴 건너뛰기




Volumn 408, Issue , 1996, Pages 207-223

Trichomonas vaginalis adhesin proteins display molecular mimicry to metabolic enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; MALATE DEHYDROGENASE (DECARBOXYLATING); VIRULENCE FACTOR;

EID: 0029760250     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0415-9_25     Document Type: Conference Paper
Times cited : (25)

References (86)
  • 1
    • 0022388614 scopus 로고
    • Specific nature of Trichomonas vaginalis parasitism of host cell surfaces
    • Alderete, J.F., and Garza, G.E., 1985, Specific nature of Trichomonas vaginalis parasitism of host cell surfaces, Infect. Immun. 50:701-708.
    • (1985) Infect. Immun. , vol.50 , pp. 701-708
    • Alderete, J.F.1    Garza, G.E.2
  • 2
    • 10144257802 scopus 로고
    • Trichomonas vaginalis attachment to host cell surfaces and role of cytoadherence in cytotoxicity
    • Alderete, J.F., and Garza, G.E., 1987, Trichomonas vaginalis attachment to host cell surfaces and role of cytoadherence in cytotoxicity, Acta Universitatis Carolinae - Biologica. 10:373- 380.
    • (1987) Acta Universitatis Carolinae - Biologica , vol.10 , pp. 373-380
    • Alderete, J.F.1    Garza, G.E.2
  • 3
    • 0023911337 scopus 로고
    • Identification and properties of Trichomonas vaginalis proteins involved in cytoadherence
    • Alderete, J.F., and Garza, G.E., 1988, Identification and properties of Trichomonas vaginalis proteins involved in cytoadherence, Infect. Immun. 56:28-33.
    • (1988) Infect. Immun. , vol.56 , pp. 28-33
    • Alderete, J.F.1    Garza, G.E.2
  • 4
    • 0022535810 scopus 로고
    • Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis
    • Alderete, J.F., and Kasmala, L., 1986, Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis, Infect. Immun. 53:697-699.
    • (1986) Infect. Immun. , vol.53 , pp. 697-699
    • Alderete, J.F.1    Kasmala, L.2
  • 6
    • 0022516743 scopus 로고
    • Phenotypic variation and diversity among Trichomonas vaginalis isolates and correlation of phenotype with trichomonal virulence determinants
    • Alderete, J.F., Kasmala, L., Metcalfe, E., and Garza, G.E., 1986a, Phenotypic variation and diversity among Trichomonas vaginalis isolates and correlation of phenotype with trichomonal virulence determinants, Infect. Immun. 53:285-293.
    • (1986) Infect. Immun. , vol.53 , pp. 285-293
    • Alderete, J.F.1    Kasmala, L.2    Metcalfe, E.3    Garza, G.E.4
  • 7
    • 0026094615 scopus 로고
    • Antibody in sera of patients infected with Trichomonas vaginalis is to trichomonad proteinases
    • Alderete, J.F., Newton, E., Dennis, C., and Neale, K.A., 1991a, Antibody in sera of patients infected with Trichomonas vaginalis is to trichomonad proteinases, Genitourin. Med. 67:331-334.
    • (1991) Genitourin. Med. , vol.67 , pp. 331-334
    • Alderete, J.F.1    Newton, E.2    Dennis, C.3    Neale, K.A.4
  • 8
    • 0026321491 scopus 로고
    • The vagina of women infected with Trichomonas vaginalis has numerous proteinases and antibody to trichomonad proteinases
    • Alderete, J.F., Newton, E., Dennis, C., and Neale, K.A., 1991b, The vagina of women infected with Trichomonas vaginalis has numerous proteinases and antibody to trichomonad proteinases, Cenitourin. Med. 67:469-474.
    • (1991) Cenitourin. Med. , vol.67 , pp. 469-474
    • Alderete, J.F.1    Newton, E.2    Dennis, C.3    Neale, K.A.4
  • 10
    • 0028827837 scopus 로고
    • Iron mediates Trichomonas vaginalis resistance to complement lysis
    • Alderete, J.F., Provenzano, D., and Lehker, M.W., 1995b, Iron mediates Trichomonas vaginalis resistance to complement lysis, Microbial Pathogen. 19:93-103.
    • (1995) Microbial Pathogen , vol.19 , pp. 93-103
    • Alderete, J.F.1    Provenzano, D.2    Lehker, M.W.3
  • 11
    • 0022627838 scopus 로고
    • Monoclonal antibody to a major surface glycoprotein immunogen differentiates isolates and subpopulations of Trichomonas vaginalis
    • Alderete, J.F., Suprun-Brown, L., and Kasmala, L., 1986b, Monoclonal antibody to a major surface glycoprotein immunogen differentiates isolates and subpopulations of Trichomonas vaginalis, Infect. Immun. 52:70-75.
    • (1986) Infect. Immun. , vol.52 , pp. 70-75
    • Alderete, J.F.1    Suprun-Brown, L.2    Kasmala, L.3
  • 12
    • 0024432880 scopus 로고
    • Trichomonas vaginalis surface proteinase activity is necessary for parasite adherence to epithelial cells
    • Arroyo, R., and Alderete, J.F., 1989, Trichomonas vaginalis surface proteinase activity is necessary for parasite adherence to epithelial cells. Infect. Immun. 57:2991-2997.
    • (1989) Infect. Immun. , vol.57 , pp. 2991-2997
    • Arroyo, R.1    Alderete, J.F.2
  • 13
    • 0029081255 scopus 로고
    • Two Trichomonas vaginalis surface proteinases bind to host epithelial cells and are related to levels of cytoadherence and cytotoxicity
    • Arroyo, R., and Alderete, J.F., 1995, Two Trichomonas vaginalis surface proteinases bind to host epithelial cells and are related to levels of cytoadherence and cytotoxicity, Arch. Med. Res. 26:279-285.
    • (1995) Arch. Med. Res. , vol.26 , pp. 279-285
    • Arroyo, R.1    Alderete, J.F.2
  • 14
    • 0026533051 scopus 로고
    • Molecular basis of host epithelial cell recognition by Trichomonas vaginalis
    • Arroyo, R., Engbring, J., and Alderete, J.F., 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
  • 15
  • 16
    • 0027454897 scopus 로고
    • Signalling of Trichomonas vaginalis for amoeboid transformation and adhesion synthesis follows cytoadherence
    • Arroyo, R., González-Robles, A., Martinez-Palomo, A., and Alderete, J.F., 1993, Signalling of Trichomonas vaginalis for amoeboid transformation and adhesion synthesis follows cytoadherence, Mol. Microbiol. 7:299-309.
    • (1993) Mol. Microbiol. , vol.7 , pp. 299-309
    • Arroyo, R.1    González-Robles, A.2    Martinez-Palomo, A.3    Alderete, J.F.4
  • 17
    • 0023644514 scopus 로고
    • Structure and expression of murine malic enzyme mRNA. Differentiation-dependent accumulation of two forms of malic enzyme mRNA in 3T3-L1 cells
    • Bagchi, S., Wise, L.S., Brown, M.L., Bregman, D., Su, J.S., and Rubin, C.S., 1987, Structure and expression of murine malic enzyme mRNA. Differentiation-dependent accumulation of two forms of malic enzyme mRNA in 3T3-L1 cells, J. Biol. Chem. 262:1558-1565
    • (1987) J. Biol. Chem. , vol.262 , pp. 1558-1565
    • Bagchi, S.1    Wise, L.S.2    Brown, M.L.3    Bregman, D.4    Su, J.S.5    Rubin, C.S.6
  • 18
    • 3843104085 scopus 로고
    • Bacterial adherence
    • Switalski, L., Hook, M., and Beachey, E.H., eds., Springer-Verlag, New York
    • Beachey, E.H., 1989, Bacterial adherence, in Molecular Mechanisms of Microbial Adhesion, (Switalski, L., Hook, M., and Beachey, E.H., eds.), pp.1-4, Springer-Verlag, New York.
    • (1989) Molecular Mechanisms of Microbial Adhesion , pp. 1-4
    • Beachey, E.H.1
  • 19
    • 0017237073 scopus 로고
    • Study of female babies of women entering confinement with vaginal trichomoiasis
    • Bramley, M., 1976, Study of female babies of women entering confinement with vaginal trichomoiasis, Brit. J. Vener. Dis. 52:58-62.
    • (1976) Brit. J. Vener. Dis. , vol.52 , pp. 58-62
    • Bramley, M.1
  • 20
    • 0022397910 scopus 로고
    • Primary structure of the succinyl-CoA synthetase of Escherichia coli
    • Buck, D., Spencer, M.E., and Guest, J.R., 1985, Primary structure of the succinyl-CoA synthetase of Escherichia coli, Biochemistry 24:6245-6252.
    • (1985) Biochemistry , vol.24 , pp. 6245-6252
    • Buck, D.1    Spencer, M.E.2    Guest, J.R.3
  • 21
    • 0027999183 scopus 로고
    • A neuramindase from streptococcus pneumoniae has the features of a surface protein
    • Camara, M., Boulnois, G.T., Andrew, P.W., and Mitchell, T.J., 1994, A neuramindase from streptococcus pneumoniae has the features of a surface protein, Infect. Immun. 62:3688-3695.
    • (1994) Infect. Immun. , vol.62 , pp. 3688-3695
    • Camara, M.1    Boulnois, G.T.2    Andrew, P.W.3    Mitchell, T.J.4
  • 22
    • 0028131915 scopus 로고
    • Selective degradation of early-response-gene mRNAs: Functional analyses of sequence features of the AU-rich elements
    • Chen, C.-Y.A., and Shyu, A.-B., 1994, Selective degradation of early-response-gene mRNAs: functional analyses of sequence features of the AU-rich elements, Mol. Cell. Biol. 14:8471-8482.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8471-8482
    • Chen, C.-Y.A.1    Shyu, A.-B.2
  • 23
    • 0023639356 scopus 로고
    • Preliminary observations on lactoferrin secretion in human vaginal mucus: Variation during menstrual cycle, evidence of hormonal regulation and implications for infection with Neisseria gonorrhoeae
    • Cohen, M.S., Britigan, B.E., French, M., and Bean, K., 1987, Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during menstrual cycle, evidence of hormonal regulation and implications for infection with Neisseria gonorrhoeae, Am. J. Obstet. Gynecol. 157:1122-1125.
    • (1987) Am. J. Obstet. Gynecol. , vol.157 , pp. 1122-1125
    • Cohen, M.S.1    Britigan, B.E.2    French, M.3    Bean, K.4
  • 25
    • 0025011018 scopus 로고
    • Characterization of Trichomonas vaginalis haemolysis
    • Dailey, D.C., Chang, T., and Alderete, J.F., 1990, Characterization of Trichomonas vaginalis haemolysis, Parasitol. 101:171-175.
    • (1990) Parasitol , vol.101 , pp. 171-175
    • Dailey, D.C.1    Chang, T.2    Alderete, J.F.3
  • 26
    • 0024367999 scopus 로고
    • Molecular mimicry: Parasite evasion and host defense
    • Damian, R.T., 1989, Molecular mimicry: parasite evasion and host defense, Curr. Top. Microbiol. Immunol. 145:101-115.
    • (1989) Curr. Top. Microbiol. Immunol. , vol.145 , pp. 101-115
    • Damian, R.T.1
  • 27
    • 0024358130 scopus 로고
    • The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde- 3P-dehydrogenase
    • Goudot-Crozel, V., Caillol, D., Djabali, M., and Dessein, A.J., 1989, The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde- 3P-dehydrogenase, J. Exp. Med. 170:2065-2080.
    • (1989) J. Exp. Med. , vol.170 , pp. 2065-2080
    • Goudot-Crozel, V.1    Caillol, D.2    Djabali, M.3    Dessein, A.J.4
  • 29
    • 0029372609 scopus 로고
    • Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes
    • Hrdy, I., and Müller, M., 1995. Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes, J. Euk. Micro. 42:593-603.
    • (1995) J. Euk. Micro. , vol.42 , pp. 593-603
    • Hrdy, I.1    Müller, M.2
  • 31
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel, P., and Pantaloni, D., 1985, Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP. Eur. J. Biochem. 150:265-269.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 265-269
    • Huitorel, P.1    Pantaloni, D.2
  • 32
    • 0028323014 scopus 로고
    • Nucleotide sequence of a porphyromonas gingivalis gene encoding a surface-associated glutamate dehydrogenase and construction of a glutamate dehydro-genase- Deficient isogenic mutant
    • Joe, A., Murray, C.S., and McBride, B.C., 1994, Nucleotide sequence of a porphyromonas gingivalis gene encoding a surface-associated glutamate dehydrogenase and construction of a glutamate dehydro-genase- deficient isogenic mutant, Infect. Immun. 62:1358-1368.
    • (1994) Infect. Immun. , vol.62 , pp. 1358-1368
    • Joe, A.1    Murray, C.S.2    McBride, B.C.3
  • 33
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto, R.M., and Caswell, A.H., 1986, Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes, Biochemistry. 25:656-661.
    • (1986) Biochemistry , vol.25 , pp. 656-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 34
    • 0027443124 scopus 로고
    • Multiple double-stranded RNA segments are associated with virus particles infecting Trichomonas vaginalis
    • Khoshnan, A., and Alderete, J.F., 1993, Multiple double-stranded RNA segments are associated with virus particles infecting Trichomonas vaginalis, J. Virol. 67:6950-6955.
    • (1993) J. Virol. , vol.67 , pp. 6950-6955
    • Khoshnan, A.1    Alderete, J.F.2
  • 35
    • 0028308513 scopus 로고
    • Trichomonas vaginalis with a double-stranded RNA virus has upregulated levels of phenotypically variable immunogen mRNA
    • Khoshnan, A., and Alderete, J.F., 1994, Trichomonas vaginalis with a double-stranded RNA virus has upregulated levels of phenotypically variable immunogen mRNA, J. Virol. 68:4035-4038.
    • (1994) J. Virol. , vol.68 , pp. 4035-4038
    • Khoshnan, A.1    Alderete, J.F.2
  • 37
    • 0025069933 scopus 로고
    • Characteristics of Trichomonas vaginalis isolates from women with and without colpitis macularis
    • Krieger, J.N., Wolner-Hanssen, P., Steven, C., and Holmes, K.K., 1990, Characteristics of Trichomonas vaginalis isolates from women with and without colpitis macularis, J. Infect. Dis. 161:307-311.
    • (1990) J. Infect. Dis. , vol.161 , pp. 307-311
    • Krieger, J.N.1    Wolner-Hanssen, P.2    Steven, C.3    Holmes, K.K.4
  • 38
    • 0027164984 scopus 로고
    • Cloning and nucleotide sequence of a full- Length cDNA encoding Ascaris suum malic enzyme
    • Kulkarni, G., Cook, P.F., and Harris, B.G., 1993, Cloning and nucleotide sequence of a full- length cDNA encoding Ascaris suum malic enzyme, Arch. Biochem. Biophys. 300:231- 237.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 231-237
    • Kulkarni, G.1    Cook, P.F.2    Harris, B.G.3
  • 40
    • 0028168012 scopus 로고
    • Molecular characterization of the α-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase
    • Lahti, C.J., Bradley, P.J., and Johnson, P.J., 1994, Molecular characterization of the α-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase, Mol. Biochem. Parasitol. 66:309-318.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 309-318
    • Lahti, C.J.1    Bradley, P.J.2    Johnson, P.J.3
  • 41
    • 0026641622 scopus 로고
    • Beta-succinyl coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino terminal sequence that resembles motochondrial presequences
    • Lahti, C.J., d'Oliveira, C.E., and Johnson, P.J., 1992, Beta-succinyl coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino terminal sequence that resembles motochondrial presequences, J. Bacteriol. 174:6822-6830.
    • (1992) J. Bacteriol. , vol.174 , pp. 6822-6830
    • Lahti, C.J.1    D'Oliveira, C.E.2    Johnson, P.J.3
  • 42
    • 0026502193 scopus 로고
    • Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic proteins
    • Lehker, M., and Alderete, J.F., 1992, Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic proteins, Mol. Microbiol. 6:123-132.
    • (1992) Mol. Microbiol. , vol.6 , pp. 123-132
    • Lehker, M.1    Alderete, J.F.2
  • 43
    • 0025766755 scopus 로고
    • The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis
    • Lehker, M., Arroyo, R., and Alderete, J.F., 1991, The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis, J. Exp. Med. 174:311-318.
    • (1991) J. Exp. Med. , vol.174 , pp. 311-318
    • Lehker, M.1    Arroyo, R.2    Alderete, J.F.3
  • 44
    • 0025354379 scopus 로고
    • Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis
    • Lehker, M.L., Chang, T.H., Dailey, D.C., and Alderete, J.F., 1990, Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis, J. Exp. Med. 171:2165-2170.
    • (1990) J. Exp. Med. , vol.171 , pp. 2165-2170
    • Lehker, M.L.1    Chang, T.H.2    Dailey, D.C.3    Alderete, J.F.4
  • 45
    • 0025766755 scopus 로고
    • The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis
    • Lehker, M. W., and Alderete, J.F., 1991, The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis, J. Exp. Med. 174:311-318.
    • (1991) J. Exp. Med. , vol.174 , pp. 311-318
    • Lehker, M.W.1    Alderete, J.F.2
  • 46
    • 10144260537 scopus 로고
    • Failure of trichomonads to convert or retroconvert long chain fatty acids or cholesterol
    • Lindmark, D.G., 1983, Failure of trichomonads to convert or retroconvert long chain fatty acids or cholesterol, J. Protozool. 30:5A.
    • (1983) J. Protozool. , vol.30
    • Lindmark, D.G.1
  • 48
    • 0026673916 scopus 로고
    • Cloning sequence analysis and expression in Escherichia coli of a streptococcal plasmin receptor
    • Lottenberg, R., Broder, C.C., Boyle, M.O.P., Kain, S.J., Schroeder, B.L., and Curtis III, R., 1992, Cloning sequence analysis and expression in Escherichia coli of a streptococcal plasmin receptor, J. Bacteriol 174:5204-5210.
    • (1992) J. Bacteriol , vol.174 , pp. 5204-5210
    • Lottenberg, R.1    Broder, C.C.2    Boyle, M.O.P.3    Kain, S.J.4    Schroeder, B.L.5    Curtis III, R.6
  • 49
    • 0025718594 scopus 로고
    • Site-directed mutagenesis of Escherichia coli succinyl- CoA synthetase
    • Lou, G.X., and Nishimura, J.S., 1991, Site-directed mutagenesis of Escherichia coli succinyl- CoA synthetase, J. Biol. Chem. 266:20781-20785.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20781-20785
    • Lou, G.X.1    Nishimura, J.S.2
  • 50
    • 10144230619 scopus 로고
    • Steroid requirement of trichomonads
    • Lund, P.G., and Shorb, M.S., 1962, Steroid requirement of trichomonads, J. Protozool. 9:151- 154.
    • (1962) J. Protozool. , vol.9 , pp. 151-154
    • Lund, P.G.1    Shorb, M.S.2
  • 51
    • 0025977083 scopus 로고
    • Functional consequences of substitution of the active site (phospho) histidine residue of Escherichia coli succinyl-CoA synthetase
    • Majumdar, R., Guest, J.R., and Bridger, W.A., 1991, Functional consequences of substitution of the active site (phospho) histidine residue of Escherichia coli succinyl-CoA synthetase, Biochim. Biophys. Acta. 1076:86-90.
    • (1991) Biochim. Biophys. Acta. , vol.1076 , pp. 86-90
    • Majumdar, R.1    Guest, J.R.2    Bridger, W.A.3
  • 52
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external excretions
    • Masson, P.L., Heremans, J.F., and Dive, C.H., 1966, An iron-binding protein common to many external excretions, Clin. Chim. Acta. 14:735-739.
    • (1966) Clin. Chim. Acta. , vol.14 , pp. 735-739
    • Masson, P.L.1    Heremans, J.F.2    Dive, C.H.3
  • 53
    • 0029041327 scopus 로고
    • Cytoplasmic mRNA-protein interactions in eukaryotic gene expression
    • McCarthy, J.E.G., and Kollmuss, H., 1995, Cytoplasmic mRNA-protein interactions in eukaryotic gene expression, Trends Biochem. Sci. 20:191-197.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 191-197
    • McCarthy, J.E.G.1    Kollmuss, H.2
  • 54
    • 0026070055 scopus 로고
    • A human nuclear uracil DNA glycosylase is the 37 kDa subunit of glyceraldehyde-3- Phosphate dehydrogenase
    • Meyer-Siegler, K., Mauro, D.J., Seal, G., Wurzer, J., DeRiel, J.K., and Sirover, M.M., 1991, A human nuclear uracil DNA glycosylase is the 37 kDa subunit of glyceraldehyde-3- phosphate dehydrogenase Proc. Natl. Acad. Sci. USA 88:8460-8464.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8460-8464
    • Meyer-Siegler, K.1    Mauro, D.J.2    Seal, G.3    Wurzer, J.4    Deriel, J.K.5    Sirover, M.M.6
  • 55
    • 0025819231 scopus 로고
    • Role of cell- Surface lysines in plasminogen binding to cells: Identification of α-enalase as a candidate plasminogen receptor
    • Miles, L.A., Dahlberg, C.M., Plescia, J., Felez, J., Kato, K., and Plow, E.F., 1991, Role of cell- surface lysines in plasminogen binding to cells: identification of α-enalase as a candidate plasminogen receptor, Biochemistry. 30:1682-1691.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 57
    • 0019215030 scopus 로고
    • Three metronidazole- Resistant strains of Trichomonas vaginalis from the U.S.A
    • Müller, M., Meingassner, J.G., Miller, M.A., and Ledger, W.J., 1980, Three metronidazole- resistant strains of Trichomonas vaginalis from the U.S.A., Am. J. Obstet. Gynecol. 138:808-812.
    • (1980) Am. J. Obstet. Gynecol. , vol.138 , pp. 808-812
    • Müller, M.1    Meingassner, J.G.2    Miller, M.A.3    Ledger, W.J.4
  • 58
    • 0025093384 scopus 로고
    • Analysis of the proteinases of representative Trichomonas vaginalis isolates
    • Neale, K.A., and Alderete, J.F., 1990, Analysis of the proteinases of representative Trichomonas vaginalis isolates, Infect. Immun. 58:157-162.
    • (1990) Infect. Immun. , vol.58 , pp. 157-162
    • Neale, K.A.1    Alderete, J.F.2
  • 60
    • 0029894595 scopus 로고    scopus 로고
    • Molecular characterization of a third AP65 adhesin gene of Trichomonas vaginalis
    • In press
    • O'Brien, J.L., Lauriano, C.M., and Alderete, J.F., 1996, Molecular characterization of a third AP65 adhesin gene of Trichomonas vaginalis, Microbial Pathogen. In press.
    • (1996) Microbial Pathogen
    • O'Brien, J.L.1    Lauriano, C.M.2    Alderete, J.F.3
  • 61
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and Fischetti, V.A., 1992, A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity, J. Exp. Med. 176:415-426.
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 62
    • 0027249488 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme
    • Pancholi, V., and Fischetti, V.A., 1993, Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme, Proc. Natl. Acad. Sci. USA 90:8154-8158.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8154-8158
    • Pancholi, V.1    Fischetti, V.A.2
  • 64
    • 0021164441 scopus 로고
    • Selective acquisition of plasma proteins by Trichomonas vaginalis and human lipoproteins as a growth requirement by this species
    • Peterson, K.M., and Alderete, J.F., 1984a, Selective acquisition of plasma proteins by Trichomonas vaginalis and human lipoproteins as a growth requirement by this species, Mol. Biochem. Parasitol. 12:37-48.
    • (1984) Mol. Biochem. Parasitol. , vol.12 , pp. 37-48
    • Peterson, K.M.1    Alderete, J.F.2
  • 65
    • 0021673647 scopus 로고
    • Trichomonas vaginalis is dependent on uptake and degradation of human low density lipoproteins
    • Peterson, K.M., and Alderete, J.F., 1984b, Trichomonas vaginalis is dependent on uptake and degradation of human low density lipoproteins, J. Exp. Med. 160:1261-1271.
    • (1984) J. Exp. Med. , vol.160 , pp. 1261-1271
    • Peterson, K.M.1    Alderete, J.F.2
  • 66
    • 0021211306 scopus 로고
    • Iron uptake and increased intracellular enzyme activity follows host lactoferrin binding by Trichomonas vaginalis receptors
    • Peterson, K.M., and Alderete, J.F., 1984c, Iron uptake and increased intracellular enzyme activity follows host lactoferrin binding by Trichomonas vaginalis receptors, J. Exp. Med. 160:398-410.
    • (1984) J. Exp. Med. , vol.160 , pp. 398-410
    • Peterson, K.M.1    Alderete, J.F.2
  • 67
    • 0024520027 scopus 로고
    • Enzyme/crystallins: Gene sharing as an evolutionary strategy
    • Piatigorsky, J., and Wistow, G.J., 1989, Enzyme/crystallins: gene sharing as an evolutionary strategy, Cell 57:197-199.
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 68
    • 0020712577 scopus 로고
    • Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase
    • Poulouse, A.J., and Kolattukudy, P.E., 1983, Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase, Arch. Biochem. Biophys. 220:652-656.
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 652-656
    • Poulouse, A.J.1    Kolattukudy, P.E.2
  • 69
    • 0029155731 scopus 로고
    • Analysis of human immunoglobulin-degrading cysteine proteinases of Trichomonas vaginalis
    • Provenzano, D., and Alderete, J.F., 1995, Analysis of human immunoglobulin-degrading cysteine proteinases of Trichomonas vaginalis, Infect. Immun. 63:3388-3395.
    • (1995) Infect. Immun. , vol.63 , pp. 3388-3395
    • Provenzano, D.1    Alderete, J.F.2
  • 70
    • 0028328269 scopus 로고
    • Similarity between a ubiquitous promoter element in an ancient eukaryote and mammalian initiator elements
    • Quon, D.V.K., Delgadillo, M.G., Khachi, A., Smale, S.T., and Johnson, P.J., 1994, Similarity between a ubiquitous promoter element in an ancient eukaryote and mammalian initiator elements, Proc. Natl. Acad. Sci. 91:4579-4583.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 4579-4583
    • Quon, D.V.K.1    Delgadillo, M.G.2    Khachi, A.3    Smale, S.T.4    Johnson, P.J.5
  • 71
    • 0027479279 scopus 로고
    • Sexual intercourse during pregnancy and preterm delivery: Effects of vaginal microorganisms
    • Read, J.S., and Klebanoff, M.A., 1993, Sexual intercourse during pregnancy and preterm delivery: effects of vaginal microorganisms, Am. J. Obstet. Gynecol. 168:514-519.
    • (1993) Am. J. Obstet. Gynecol. , vol.168 , pp. 514-519
    • Read, J.S.1    Klebanoff, M.A.2
  • 73
    • 0024331913 scopus 로고
    • Primary structure of the maize NADP-dependent malic enzyme
    • Rothermel, B.A., and Nelson, T., 1989, Primary structure of the maize NADP-dependent malic enzyme, J. Biol. Chem. 264:19587-19592.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19587-19592
    • Rothermel, B.A.1    Nelson, T.2
  • 74
    • 0025866317 scopus 로고
    • Duck liver malic enzyme: Sequence of a tryptic peptide containing one cysteine residue labelled by the substrate analog bromopyruvate
    • Satterlee, J., and Hsu, R.Y., 1991, Duck liver malic enzyme: sequence of a tryptic peptide containing one cysteine residue labelled by the substrate analog bromopyruvate, Biochim. Biophys. Acta. 1079:247-252.
    • (1991) Biochim. Biophys. Acta. , vol.1079 , pp. 247-252
    • Satterlee, J.1    Hsu, R.Y.2
  • 75
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton, N.S., Berry, A., and Perham, R.N., 1990, Redesign of the coenzyme specificity of a dehydrogenase by protein engineering, Nature 343:38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 76
    • 0028153922 scopus 로고
    • FimH family of type I fimbrial adhesins: Functional heterogeneity due to minor sequence variations among fimH genes
    • Sokurenko, E.V., Courtney, H.S., Ohman, D.E., Klemm, P., and Hasty, D.L., 1994, FimH family of type I fimbrial adhesins: functional heterogeneity due to minor sequence variations among fimH genes, J. Bacteriol. 176:748-755.
    • (1994) J. Bacteriol. , vol.176 , pp. 748-755
    • Sokurenko, E.V.1    Courtney, H.S.2    Ohman, D.E.3    Klemm, P.4    Hasty, D.L.5
  • 77
    • 0028342592 scopus 로고
    • Racial variation in vaginal pH among healthy sexually active adolescents
    • Stevens-Simon, C., Jamison, J., McGregor, J.A, and Douglas, J.M., 1994, Racial variation in vaginal pH among healthy sexually active adolescents, Sex. Trans. Dis. 21:168-172.
    • (1994) Sex. Trans. Dis. , vol.21 , pp. 168-172
    • Stevens-Simon, C.1    Jamison, J.2    McGregor, J.A.3    Douglas, J.M.4
  • 78
    • 0028169442 scopus 로고
    • Adaptation of the carbon metabolism of Trichomonas vaginalis to the nature and availability of carbon source
    • Ter Kuile, B.H., 1994, Adaptation of the carbon metabolism of Trichomonas vaginalis to the nature and availability of carbon source, Microbiol. 140:2503-2510.
    • (1994) Microbiol , vol.140 , pp. 2503-2510
    • Ter Kuile, B.H.1
  • 79
    • 0028290561 scopus 로고
    • Glucosyltransferase mediates adhesion of streptococcus gordonii to human endothelial cells in vitro
    • Vacca-Smith, A.M., Jones, C.A., Levine, M.J., and Stinson, M.W., 1994, Glucosyltransferase mediates adhesion of streptococcus gordonii to human endothelial cells in vitro, Infect. Immun. 62:2187-2194.
    • (1994) Infect. Immun. , vol.62 , pp. 2187-2194
    • Vacca-Smith, A.M.1    Jones, C.A.2    Levine, M.J.3    Stinson, M.W.4
  • 80
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne, G., Steppuhn, J., and Herrmann, R.G., 1989, Domain structure of mitochondrial and chloroplast targeting peptides, Eur. J. Biochem. 180:535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 81
    • 0023215826 scopus 로고
    • Trichomonas vaginalis phenotypic variation occurs only among trichomonads infected with the double-stranded RNA Virus
    • Wang, A., Wang, C.C., and Alderete, J.F., 1987, Trichomonas vaginalis phenotypic variation occurs only among trichomonads infected with the double-stranded RNA Virus, J. Exp. Med. 166:142-150.
    • (1987) J. Exp. Med. , vol.166 , pp. 142-150
    • Wang, A.1    Wang, C.C.2    Alderete, J.F.3
  • 83
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moities with α-helixes in dinucleotide-binding proteins
    • Wierenga, R.K., DeMaeyer, M.C.H., and Hol, W.G.J., 1985, Interaction of pyrophosphate moities with α-helixes in dinucleotide-binding proteins, Biochemistry 24:1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    DeMaeyer, M.C.H.2    Hol, W.G.J.3
  • 84
    • 0027225772 scopus 로고
    • Lens crystallins: Gene recruitment and evolutionary dynamism
    • Wistow, G., 1993, Lens crystallins: gene recruitment and evolutionary dynamism, Trends Biochem. Sci. 18:301-306.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 301-306
    • Wistow, G.1
  • 85
    • 0023225865 scopus 로고
    • Recruitment of enzymes as lens structural proteins
    • Wistow, G., and Piatigorsky, J., 1987, Recruitment of enzymes as lens structural proteins, Science 236:1554-1555.
    • (1987) Science , vol.236 , pp. 1554-1555
    • Wistow, G.1    Piatigorsky, J.2
  • 86
    • 0028900073 scopus 로고
    • The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation
    • Zubiaga, A.M., Belasco, J.G., and Greenberg, M.E., 1995, The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation, Mol. Cell. Biol. 15:2219- 2230.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2219-2230
    • Zubiaga, A.M.1    Belasco, J.G.2    Greenberg, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.