메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Trichomoniasis and lactoferrin: Future prospects

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CP65 CYSTEINE PROTEINASE; CYSTEINE PROTEINASE; FERRIC ION; FERROUS ION; IRON; LACTOFERRIN; LACTOFERRIN BINDING RECEPTOR; METRONIDAZOLE; P270 PROTEIN; PROTEINASE; PROTOZOAL PROTEIN; PROTOZOAL VACCINE; RECEPTOR; TRICHOMONAS VAGINALIS VACCINE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CHELATING AGENT;

EID: 84866939594     PISSN: 10647449     EISSN: 10980997     Source Type: Journal    
DOI: 10.1155/2012/536037     Document Type: Review
Times cited : (17)

References (63)
  • 1
    • 40049089082 scopus 로고    scopus 로고
    • Trichomonas vaginalis infection: Can we afford to do nothing?
    • 2-s2.0-40049089082 10.1086/526498
    • McClelland R. S., Trichomonas vaginalis infection: can we afford to do nothing? Journal of Infectious Diseases 2008 197 4 487 489 2-s2.0-40049089082 10.1086/526498
    • (2008) Journal of Infectious Diseases , vol.197 , Issue.4 , pp. 487-489
    • McClelland, R.S.1
  • 2
    • 0031978286 scopus 로고    scopus 로고
    • Clinical and microbiological aspects of Trichomonas vaginalis
    • 2-s2.0-0031978286
    • Petrin D., Delgaty K., Bhatt R., Garber G., Clinical and microbiological aspects of Trichomonas vaginalis. Clinical Microbiology Reviews 1998 11 2 300 317 2-s2.0-0031978286
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.2 , pp. 300-317
    • Petrin, D.1    Delgaty, K.2    Bhatt, R.3    Garber, G.4
  • 3
    • 5644250477 scopus 로고    scopus 로고
    • Trichomoniasis
    • 2-s2.0-5644250477 10.1128/CMR.17.4.794-803.2004
    • Schwebke J. R., Burgess D., Trichomoniasis. Clinical Microbiology Reviews 2004 17 4 794 803 2-s2.0-5644250477 10.1128/CMR.17.4.794-803.2004
    • (2004) Clinical Microbiology Reviews , vol.17 , Issue.4 , pp. 794-803
    • Schwebke, J.R.1    Burgess, D.2
  • 4
    • 0027533322 scopus 로고
    • Trichomonas vaginalis: A reemerging pathogen
    • 2-s2.0-0027533322
    • Heine P., McGregor J. A., Trichomonas vaginalis: a reemerging pathogen. Clinical Obstetrics and Gynecology 1993 36 1 137 144 2-s2.0-0027533322
    • (1993) Clinical Obstetrics and Gynecology , vol.36 , Issue.1 , pp. 137-144
    • Heine, P.1    McGregor, J.A.2
  • 5
    • 0036968688 scopus 로고    scopus 로고
    • Iron transport: Emerging roles in health and disease
    • 2-s2.0-0036968688 10.1139/o02-159
    • Goswami T., Rolfs A., Hediger M. A., Iron transport: emerging roles in health and disease. Biochemistry and Cell Biology 2002 80 5 679 689 2-s2.0-0036968688 10.1139/o02-159
    • (2002) Biochemistry and Cell Biology , vol.80 , Issue.5 , pp. 679-689
    • Goswami, T.1    Rolfs, A.2    Hediger, M.A.3
  • 6
    • 0016227934 scopus 로고
    • Iron and susceptibility to infectious disease
    • 2-s2.0-0016227934
    • Weinberg E. D., Iron and susceptibility to infectious disease. Science 1974 184 4140 952 956 2-s2.0-0016227934
    • (1974) Science , vol.184 , Issue.4140 , pp. 952-956
    • Weinberg, E.D.1
  • 7
    • 0035148218 scopus 로고    scopus 로고
    • Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins
    • 2-s2.0-0035148218
    • Vanacova S., Rasoloson D., Rázga J., Hrd I., Kulda J., Tachezy J., Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins. Microbiology 2001 147 1 53 62 2-s2.0-0035148218
    • (2001) Microbiology , vol.147 , Issue.1 , pp. 53-62
    • Vanacova, S.1    Rasoloson, D.2    Rázga, J.3    Hrd, I.4    Kulda, J.5    Tachezy, J.6
  • 8
    • 9444246510 scopus 로고    scopus 로고
    • Iron and microbial infection
    • 2-s2.0-10444232719 10.1038/nrmicro1046
    • Schaible U. E., Kaufmann S. H. E., Iron and microbial infection. Nature Reviews Microbiology 2004 2 12 946 953 2-s2.0-10444232719 10.1038/nrmicro1046
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.12 , pp. 946-953
    • Schaible, U.E.1    Kaufmann, S.H.E.2
  • 9
    • 33846691564 scopus 로고    scopus 로고
    • Iron uptake and metabolism in the new millennium
    • 2-s2.0-33846691564 10.1016/j.tcb.2006.12.003
    • Dunn L. L., Rahmanto Y. S., Richardson D. R., Iron uptake and metabolism in the new millennium. Trends in Cell Biology 2007 17 2 93 100 2-s2.0-33846691564 10.1016/j.tcb.2006.12.003
    • (2007) Trends in Cell Biology , vol.17 , Issue.2 , pp. 93-100
    • Dunn, L.L.1    Rahmanto, Y.S.2    Richardson, D.R.3
  • 10
    • 59449109182 scopus 로고    scopus 로고
    • Iron homeostasis: Recently identified proteins provide insight into novel control mechanisms
    • 2-s2.0-59449109182 10.1074/jbc.R800017200
    • Zhang A. S., Enns C. A., Iron homeostasis: recently identified proteins provide insight into novel control mechanisms. Journal of Biological Chemistry 2009 284 2 711 715 2-s2.0-59449109182 10.1074/jbc.R800017200
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.2 , pp. 711-715
    • Zhang, A.S.1    Enns, C.A.2
  • 11
    • 28344440468 scopus 로고    scopus 로고
    • Molecular structure, binding properties and dynamics of lactoferrin
    • 2-s2.0-28344440468 10.1007/s00018-005-5368-9
    • Baker E. N., Baker H. M., Molecular structure, binding properties and dynamics of lactoferrin. Cellular and Molecular Life Sciences 2005 62 22 2531 2539 2-s2.0-28344440468 10.1007/s00018-005-5368-9
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2531-2539
    • Baker, E.N.1    Baker, H.M.2
  • 13
    • 1342322699 scopus 로고    scopus 로고
    • The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis
    • 2-s2.0-1342322699 10.1111/j.1432-1033.2003.03965.x
    • Van Veen H. A., Geerts M. E. J., Van Berkel P. H. C., Nuijens J. H., The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis. European Journal of Biochemistry 2004 271 4 678 684 2-s2.0-1342322699 10.1111/j.1432-1033.2003.03965.x
    • (2004) European Journal of Biochemistry , vol.271 , Issue.4 , pp. 678-684
    • Van Veen, H.A.1    Geerts, M.E.J.2    Van Berkel, P.H.C.3    Nuijens, J.H.4
  • 14
    • 0032737846 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein
    • 2-s2.0-0032737846
    • Vorland L. H., Lactoferrin: a multifunctional glycoprotein. APMIS 1999 107 11 971 981 2-s2.0-0032737846
    • (1999) APMIS , vol.107 , Issue.11 , pp. 971-981
    • Vorland, L.H.1
  • 15
    • 84857355874 scopus 로고    scopus 로고
    • Molecular evolution of the transferrin family and associated receptors
    • 2-s2.0-54049106841 10.1016/j.bbagen.2011.06.002
    • Lambert L. A., Molecular evolution of the transferrin family and associated receptors. Biochimica et Biophysica Acta 2012 1820 3 244 255 2-s2.0-54049106841 10.1016/j.bbagen.2011.06.002
    • (2012) Biochimica et Biophysica Acta , vol.1820 , Issue.3 , pp. 244-255
    • Lambert, L.A.1
  • 17
    • 28344447990 scopus 로고    scopus 로고
    • Multifunctional roles of lactoferrin: A critical overview
    • 2-s2.0-28344447990 10.1007/s00018-005-5369-8
    • Ward P. P., Paz E., Conneely O. M., Multifunctional roles of lactoferrin: a critical overview. Cellular and Molecular Life Sciences 2005 62 22 2540 2548 2-s2.0-28344447990 10.1007/s00018-005-5369-8
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2540-2548
    • Ward, P.P.1    Paz, E.2    Conneely, O.M.3
  • 18
    • 0018147096 scopus 로고
    • Lactoferrin content of peripheral blood cells
    • 2-s2.0-0018147096
    • Bennett R. M., Kokocinski T., Lactoferrin content of peripheral blood cells. British Journal of Haematology 1978 39 4 509 521 2-s2.0-0018147096
    • (1978) British Journal of Haematology , vol.39 , Issue.4 , pp. 509-521
    • Bennett, R.M.1    Kokocinski, T.2
  • 19
    • 28444462150 scopus 로고    scopus 로고
    • Lactoferrin: A modulator of immune and inflammatory responses
    • 2-s2.0-28444462150 10.1007/s00018-005-5370-2
    • Legrand D., Elass E., Carpentier M., Mazurier J., Lactoferrin: a modulator of immune and inflammatory responses. Cellular and Molecular Life Sciences 2005 62 22 2549 2559 2-s2.0-28444462150 10.1007/s00018-005-5370-2
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2549-2559
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 20
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • 2-s2.0-28344457682 10.1007/s00018-005-5372-0
    • Valenti P., Antonini G., Lactoferrin: an important host defence against microbial and viral attack. Cellular and Molecular Life Sciences 2005 62 22 2576 2587 2-s2.0-28344457682 10.1007/s00018-005-5372-0
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 21
    • 58149140244 scopus 로고    scopus 로고
    • Immunomodulatory effects of lactoferrin on antigen presenting cells
    • 2-s2.0-58149140244 10.1016/j.biochi.2008.05.005
    • Puddu P., Valenti P., Gessani S., Immunomodulatory effects of lactoferrin on antigen presenting cells. Biochimie 2009 91 1 11 18 2-s2.0-58149140244 10.1016/j.biochi.2008.05.005
    • (2009) Biochimie , vol.91 , Issue.1 , pp. 11-18
    • Puddu, P.1    Valenti, P.2    Gessani, S.3
  • 22
    • 33748423889 scopus 로고    scopus 로고
    • Oral administration of lactoferrin increases hemoglobin and total serum iron in pregnant women
    • 2-s2.0-33748423889 10.1139/O06-040
    • Paesano R., Torcia F., Berlutti F., Pacifici E., Ebano V., Moscarini M., Valenti P., Oral administration of lactoferrin increases hemoglobin and total serum iron in pregnant women. Biochemistry and Cell Biology 2006 84 3 377 380 2-s2.0-33748423889 10.1139/O06-040
    • (2006) Biochemistry and Cell Biology , vol.84 , Issue.3 , pp. 377-380
    • Paesano, R.1    Torcia, F.2    Berlutti, F.3    Pacifici, E.4    Ebano, V.5    Moscarini, M.6    Valenti, P.7
  • 23
    • 77953249514 scopus 로고    scopus 로고
    • Lactoferrin efficacy versus ferrous sulfate in curing iron deficiency and iron deficiency anemia in pregnant women
    • 2-s2.0-77953249514 10.1007/s10534-010-9335-z
    • Paesano R., Berlutti F., Pietropaoli M., Pantanella F., Pacifici E., Goolsbee W., Valenti P., Lactoferrin efficacy versus ferrous sulfate in curing iron deficiency and iron deficiency anemia in pregnant women. BioMetals 2010 23 3 411 417 2-s2.0-77953249514 10.1007/s10534-010-9335-z
    • (2010) BioMetals , vol.23 , Issue.3 , pp. 411-417
    • Paesano, R.1    Berlutti, F.2    Pietropaoli, M.3    Pantanella, F.4    Pacifici, E.5    Goolsbee, W.6    Valenti, P.7
  • 24
    • 58149105930 scopus 로고    scopus 로고
    • The influence of lactoferrin, orally administered, on systemic iron homeostasis in pregnant women suffering of iron deficiency and iron deficiency anaemia
    • 2-s2.0-58149105930 10.1016/j.biochi.2008.06.004
    • Paesano R., Pietropaoli M., Gessani S., Valenti P., The influence of lactoferrin, orally administered, on systemic iron homeostasis in pregnant women suffering of iron deficiency and iron deficiency anaemia. Biochimie 2009 91 1 44 51 2-s2.0-58149105930 10.1016/j.biochi.2008.06.004
    • (2009) Biochimie , vol.91 , Issue.1 , pp. 44-51
    • Paesano, R.1    Pietropaoli, M.2    Gessani, S.3    Valenti, P.4
  • 25
    • 79960724573 scopus 로고    scopus 로고
    • Bovine lactoferrin counteracts Toll-like receptor mediated activation signals in antigen presenting cells
    • 2-s2.0-79960724573 10.1371/journal.pone.0022504 e22504
    • Puddu P., Latorre D., Carollo M., Catizone A., Ricci G., Valenti P., Gessani S., Bovine lactoferrin counteracts Toll-like receptor mediated activation signals in antigen presenting cells. PLoS One 2011 6 7 2-s2.0-79960724573 10.1371/journal.pone.0022504 e22504
    • (2011) PLoS One , vol.6 , Issue.7
    • Puddu, P.1    Latorre, D.2    Carollo, M.3    Catizone, A.4    Ricci, G.5    Valenti, P.6    Gessani, S.7
  • 26
    • 33748418054 scopus 로고    scopus 로고
    • Lactoferrin downregulates pro-inflammatory cytokines upexpressed in intestinal epithelial cells infected with invasive or noninvasive Escherichia coli strains
    • 2-s2.0-33748418054 10.1139/O06-039
    • Berlutti F., Schippa S., Morea C., Sarli S., Perfetto B., Donnarumma G., Valenti P., Lactoferrin downregulates pro-inflammatory cytokines upexpressed in intestinal epithelial cells infected with invasive or noninvasive Escherichia coli strains. Biochemistry and Cell Biology 2006 84 3 351 357 2-s2.0-33748418054 10.1139/O06-039
    • (2006) Biochemistry and Cell Biology , vol.84 , Issue.3 , pp. 351-357
    • Berlutti, F.1    Schippa, S.2    Morea, C.3    Sarli, S.4    Perfetto, B.5    Donnarumma, G.6    Valenti, P.7
  • 28
    • 53749102295 scopus 로고    scopus 로고
    • The N1 domain of human lactoferrin is required for internalization by caco-2 cells and targeting to the nucleus
    • 2-s2.0-53749102295 10.1021/bi8012164
    • Suzuki Y. A., Wong H., Ashida K. Y., Schryvers A. B., Lönnerdal B., The N1 domain of human lactoferrin is required for internalization by caco-2 cells and targeting to the nucleus. Biochemistry 2008 47 41 10915 10920 2-s2.0-53749102295 10.1021/bi8012164
    • (2008) Biochemistry , vol.47 , Issue.41 , pp. 10915-10920
    • Suzuki, Y.A.1    Wong, H.2    Ashida, K.Y.3    Schryvers, A.B.4    Lönnerdal, B.5
  • 29
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • 2-s2.0-0019640696
    • Bullen J. J., The significance of iron in infection. Reviews of Infectious Diseases 1981 3 6 1127 1138 2-s2.0-0019640696
    • (1981) Reviews of Infectious Diseases , vol.3 , Issue.6 , pp. 1127-1138
    • Bullen, J.J.1
  • 30
    • 0036129834 scopus 로고    scopus 로고
    • Lactoferrin inhibits the lipopolysaccharide-induced expression and proteoglycan-binding ability of interleukin-8 in human endothelial cells
    • 2-s2.0-0036129834 10.1128/IAI.70.4.1860-1866.2002
    • Elass E., Masson M., Mazurier J., Legrand D., Lactoferrin inhibits the lipopolysaccharide-induced expression and proteoglycan-binding ability of interleukin-8 in human endothelial cells. Infection and Immunity 2002 70 4 1860 1866 2-s2.0-0036129834 10.1128/IAI.70.4.1860-1866.2002
    • (2002) Infection and Immunity , vol.70 , Issue.4 , pp. 1860-1866
    • Elass, E.1    Masson, M.2    Mazurier, J.3    Legrand, D.4
  • 32
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • 2-s2.0-70349923239 10.1016/j.bbagen.2008.07.002
    • Weinberg E. D., Iron availability and infection. Biochimica et Biophysica Acta 2009 1790 7 600 605 2-s2.0-70349923239 10.1016/j.bbagen.2008.07.002
    • (2009) Biochimica et Biophysica Acta , vol.1790 , Issue.7 , pp. 600-605
    • Weinberg, E.D.1
  • 34
    • 0034105860 scopus 로고    scopus 로고
    • Microbial pathogens with impaired ability to acquire host iron
    • 2-s2.0-0034105860 10.1023/A:1009293500209
    • Weinberg E. D., Microbial pathogens with impaired ability to acquire host iron. BioMetals 2000 13 1 85 89 2-s2.0-0034105860 10.1023/A:1009293500209
    • (2000) BioMetals , vol.13 , Issue.1 , pp. 85-89
    • Weinberg, E.D.1
  • 35
    • 11044232246 scopus 로고    scopus 로고
    • Siderophore and haem iron use by Tritrichomonas foetus
    • 2-s2.0-11044232246 10.1099/mic.0.27544-0
    • Sutak R., Chamot C., Tachezy J., Camadro J. M., Lesuisse E., Siderophore and haem iron use by Tritrichomonas foetus. Microbiology 2004 150 12 3979 3987 2-s2.0-11044232246 10.1099/mic.0.27544-0
    • (2004) Microbiology , vol.150 , Issue.12 , pp. 3979-3987
    • Sutak, R.1    Chamot, C.2    Tachezy, J.3    Camadro, J.M.4    Lesuisse, E.5
  • 36
    • 0021211306 scopus 로고
    • Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors
    • 2-s2.0-0021211306
    • Peterson K. M., Alderete J. F., Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors. Journal of Experimental Medicine 1984 160 2 398 410 2-s2.0-0021211306
    • (1984) Journal of Experimental Medicine , vol.160 , Issue.2 , pp. 398-410
    • Peterson, K.M.1    Alderete, J.F.2
  • 37
    • 0025354379 scopus 로고
    • Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis
    • 2-s2.0-0025354379 10.1084/jem.171.6.2165
    • Lehker M. W., Chang T. H., Dailey D. C., Alderete J. F., Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis. Journal of Experimental Medicine 1990 171 6 2165 2170 2-s2.0-0025354379 10.1084/jem.171.6.2165
    • (1990) Journal of Experimental Medicine , vol.171 , Issue.6 , pp. 2165-2170
    • Lehker, M.W.1    Chang, T.H.2    Dailey, D.C.3    Alderete, J.F.4
  • 38
    • 0026502193 scopus 로고
    • Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic trichomonad proteins
    • 2-s2.0-0026502193
    • Lehker M. W., Alderete J. F., Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic trichomonad proteins. Molecular Microbiology 1992 6 1 123 132 2-s2.0-0026502193
    • (1992) Molecular Microbiology , vol.6 , Issue.1 , pp. 123-132
    • Lehker, M.W.1    Alderete, J.F.2
  • 39
    • 0023639356 scopus 로고
    • Preliminary observations on lactoferrin secretion in human vaginal mucus: Variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae
    • 2-s2.0-0023639356
    • Cohen M. S., Britigan B. E., French M., Bean K., Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae. American Journal of Obstetrics and Gynecology 1987 157 5 1122 1125 2-s2.0-0023639356
    • (1987) American Journal of Obstetrics and Gynecology , vol.157 , Issue.5 , pp. 1122-1125
    • Cohen, M.S.1    Britigan, B.E.2    French, M.3    Bean, K.4
  • 40
    • 84856014211 scopus 로고    scopus 로고
    • Influence of iron ion on the growth of Trichomonas vaginalis in vitro
    • 2-s2.0-84856014211
    • Yuan Y. Q., Xue C. G., Influence of iron ion on the growth of Trichomonas vaginalis in vitro. Chinese Journal of Parasitology & Parasitic Diseases 2010 28 4 273 276 2-s2.0-84856014211
    • (2010) Chinese Journal of Parasitology & Parasitic Diseases , vol.28 , Issue.4 , pp. 273-276
    • Yuan, Y.Q.1    Xue, C.G.2
  • 41
    • 0036756764 scopus 로고    scopus 로고
    • The complex fibronectin Trichomonas vaginalis interactions and Trichomonosis
    • 2-s2.0-0036756764 10.1016/S1383-5769(02)00015-6
    • Alderete J. F., Benchimol M., Lehker M. W., Crouch M. L., The complex fibronectin Trichomonas vaginalis interactions and Trichomonosis. Parasitology International 2002 51 3 285 292 2-s2.0-0036756764 10.1016/S1383-5769(02)00015-6
    • (2002) Parasitology International , vol.51 , Issue.3 , pp. 285-292
    • Alderete, J.F.1    Benchimol, M.2    Lehker, M.W.3    Crouch, M.L.4
  • 42
    • 0034866226 scopus 로고    scopus 로고
    • Binding of fibronectin by Trichomonas vaginalis is influenced by iron and calcium
    • 2-s2.0-0034866226 10.1006/mpat.2001.0455
    • Crouch M. L., Benchimol M., Alderete J. F., Binding of fibronectin by Trichomonas vaginalis is influenced by iron and calcium. Microbial Pathogenesis 2001 31 3 131 144 2-s2.0-0034866226 10.1006/mpat.2001.0455
    • (2001) Microbial Pathogenesis , vol.31 , Issue.3 , pp. 131-144
    • Crouch, M.L.1    Benchimol, M.2    Alderete, J.F.3
  • 43
    • 34848847880 scopus 로고    scopus 로고
    • The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65
    • 2-s2.0-34848847880 10.1111/j.1462-5822.2007.00979.x
    • Kucknoor A. S., Mundodi V., Alderete J. F., The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65. Cellular Microbiology 2007 9 11 2586 2597 2-s2.0-34848847880 10.1111/j.1462-5822.2007.00979.x
    • (2007) Cellular Microbiology , vol.9 , Issue.11 , pp. 2586-2597
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 44
    • 61949251703 scopus 로고    scopus 로고
    • Transcriptional regulation of an iron-inducible gene by differential and alternate promoter entries of multiple Myb proteins in the protozoan parasite Trichomonas vaginalis
    • 2-s2.0-61949251703 10.1128/EC.00317-08
    • Hsu H. M., Ong S. J., Lee M. C., Tai J. H., Transcriptional regulation of an iron-inducible gene by differential and alternate promoter entries of multiple Myb proteins in the protozoan parasite Trichomonas vaginalis. Eukaryotic Cell 2009 8 3 362 372 2-s2.0-61949251703 10.1128/EC.00317-08
    • (2009) Eukaryotic Cell , vol.8 , Issue.3 , pp. 362-372
    • Hsu, H.M.1    Ong, S.J.2    Lee, M.C.3    Tai, J.H.4
  • 45
    • 0021951972 scopus 로고
    • Effect of culture medium iron content on the biochemical composition and metabolism of Trichomonas vaginalis
    • 2-s2.0-0021951972
    • Gorrell T. E., Effect of culture medium iron content on the biochemical composition and metabolism of Trichomonas vaginalis. Journal of Bacteriology 1985 161 3 1228 1230 2-s2.0-0021951972
    • (1985) Journal of Bacteriology , vol.161 , Issue.3 , pp. 1228-1230
    • Gorrell, T.E.1
  • 46
    • 13844308104 scopus 로고    scopus 로고
    • A Trichomonas vaginalis 120 kDa protein with identity to hydrogenosome pyruvate:ferredoxin oxidoreductase is a surface adhesin induced by iron
    • 2-s2.0-13844308104 10.1111/j.1462-5822.2004.00455.x
    • Moreno-Brito V., Yanez-Gomez C., Meza-Cervantez P., Avila-Gonzalez L., Rodríguez M. A., Ortega-López J., González-Robles A., Arroyo R., A Trichomonas vaginalis 120 kDa protein with identity to hydrogenosome pyruvate:ferredoxin oxidoreductase is a surface adhesin induced by iron. Cellular Microbiology 2005 7 2 245 258 2-s2.0-13844308104 10.1111/j.1462-5822.2004.00455.x
    • (2005) Cellular Microbiology , vol.7 , Issue.2 , pp. 245-258
    • Moreno-Brito, V.1    Yanez-Gomez, C.2    Meza-Cervantez, P.3    Avila-Gonzalez, L.4    Rodríguez, M.A.5    Ortega-López, J.6    González-Robles, A.7    Arroyo, R.8
  • 48
    • 67650032436 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis
    • 2-s2.0-67650032436 10.1128/IAI.00157-09
    • Lama A., Kucknoor A., Mundodi V., Alderete J. F., Glyceraldehyde-3- phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis. Infection and Immunity 2009 77 7 2703 2711 2-s2.0-67650032436 10.1128/IAI.00157-09
    • (2009) Infection and Immunity , vol.77 , Issue.7 , pp. 2703-2711
    • Lama, A.1    Kucknoor, A.2    Mundodi, V.3    Alderete, J.F.4
  • 49
    • 0037085285 scopus 로고    scopus 로고
    • Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis
    • 2-s2.0-0037085285 10.1074/jbc.M110234200
    • Tsai C. D., Liu H. W., Tai J. H., Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis. Journal of Biological Chemistry 2002 277 7 5153 5162 2-s2.0-0037085285 10.1074/jbc.M110234200
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5153-5162
    • Tsai, C.D.1    Liu, H.W.2    Tai, J.H.3
  • 50
    • 0035052105 scopus 로고    scopus 로고
    • Effect of iron on the virulence of Trichomonas vaginalis
    • 2-s2.0-0035052105
    • Ryu J. S., Choi H. K., Min D. Y., Ha S. E., Ahn M. H., Effect of iron on the virulence of Trichomonas vaginalis. Journal of Parasitology 2001 87 2 457 460 2-s2.0-0035052105
    • (2001) Journal of Parasitology , vol.87 , Issue.2 , pp. 457-460
    • Ryu, J.S.1    Choi, H.K.2    Min, D.Y.3    Ha, S.E.4    Ahn, M.H.5
  • 51
    • 0028827837 scopus 로고
    • Iron mediates Trichomonas vaginalis resistance to complement lysis
    • 2-s2.0-0028827837 10.1006/mpat.1995.0049
    • Alderete J. F., Provenzano D., Lehker M. W., Iron mediates Trichomonas vaginalis resistance to complement lysis. Microbial Pathogenesis 1995 19 2 93 103 2-s2.0-0028827837 10.1006/mpat.1995.0049
    • (1995) Microbial Pathogenesis , vol.19 , Issue.2 , pp. 93-103
    • Alderete, J.F.1    Provenzano, D.2    Lehker, M.W.3
  • 53
    • 0023215826 scopus 로고
    • Trichomonas vaginalis phenotypic variation occurs only among trichomonads infected with the double-stranded RNA virus
    • 2-s2.0-0023215826
    • Wang A., Wang C. C., Alderete J. F., Trichomonas vaginalis phenotypic variation occurs only among trichomonads infected with the double-stranded RNA virus. Journal of Experimental Medicine 1987 166 1 142 150 2-s2.0-0023215826
    • (1987) Journal of Experimental Medicine , vol.166 , Issue.1 , pp. 142-150
    • Wang, A.1    Wang, C.C.2    Alderete, J.F.3
  • 54
    • 0032765417 scopus 로고    scopus 로고
    • Iron modulates phenotypic variation and phosphorylation of P270 in double-stranded RNA virus-infected Trichomonas vaginalis
    • 2-s2.0-0032765417
    • Alderete J. F., Iron modulates phenotypic variation and phosphorylation of P270 in double-stranded RNA virus-infected Trichomonas vaginalis. Infection and Immunity 1999 67 8 4298 4302 2-s2.0-0032765417
    • (1999) Infection and Immunity , vol.67 , Issue.8 , pp. 4298-4302
    • Alderete, J.F.1
  • 55
    • 0025766755 scopus 로고
    • The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis
    • 2-s2.0-0025766755
    • Lehker M. W., Arroyo R., Alderete J. F., The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis. Journal of Experimental Medicine 1991 174 2 311 318 2-s2.0-0025766755
    • (1991) Journal of Experimental Medicine , vol.174 , Issue.2 , pp. 311-318
    • Lehker, M.W.1    Arroyo, R.2    Alderete, J.F.3
  • 56
    • 0037338699 scopus 로고    scopus 로고
    • Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis
    • 2-s2.0-0037338699 10.1046/j.1365-2958.2003.03366.x
    • Garcia A. F., Chang T. H., Benchimol M., Klumpp D. J., Lehker M. W., Alderete J. F., Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis. Molecular Microbiology 2003 47 5 1207 1224 2-s2.0-0037338699 10.1046/j.1365-2958.2003.03366.x
    • (2003) Molecular Microbiology , vol.47 , Issue.5 , 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
  • 57
    • 36849079342 scopus 로고    scopus 로고
    • Negative iron regulation of the CP65 cysteine proteinase cytotoxicity in Trichomonas vaginalis
    • 2-s2.0-36849079342 10.1016/j.micinf.2007.09.011
    • Alvarez-Sánchez M. E., Solano-González E., Yañez-Gómez C., Arroyo R., Negative iron regulation of the CP65 cysteine proteinase cytotoxicity in Trichomonas vaginalis. Microbes and Infection 2007 9 14-15 1597 1605 2-s2.0-36849079342 10.1016/j.micinf.2007.09.011
    • (2007) Microbes and Infection , vol.9 , Issue.14-15 , pp. 1597-1605
    • Alvarez-Sánchez, M.E.1    Solano-González, E.2    Yañez-Gómez, C.3    Arroyo, R.4
  • 58
    • 0347596971 scopus 로고    scopus 로고
    • A 39-kDa cysteine proteinase CP39 from Trichomonas vaginalis, which is negatively affected by iron may be involved in Trichomonal Cytotoxicity
    • 2-s2.0-0347596971 10.1111/j.1550-7408.2003.tb00692.x
    • Hernandez-Gutierrez R., Ortega-López J., Arroyo R., A 39-kDa cysteine proteinase CP39 from Trichomonas vaginalis, which is negatively affected by iron may be involved in Trichomonal Cytotoxicity. Journal of Eukaryotic Microbiology 2003 50 696 698 2-s2.0-0347596971 10.1111/j.1550-7408. 2003.tb00692.x
    • (2003) Journal of Eukaryotic Microbiology , vol.50 , pp. 696-698
    • Hernandez-Gutierrez, R.1    Ortega-López, J.2    Arroyo, R.3
  • 59
    • 2942560496 scopus 로고    scopus 로고
    • Tvcp12: A novel Trichomonas vaginalis cathepsin L-like cysteine proteinase-encoding gene
    • 2-s2.0-2942560496
    • León-Sicairos C. R., León-Félix J., Arroyo R., Tvcp12: a novel Trichomonas vaginalis cathepsin L-like cysteine proteinase-encoding gene. Microbiology 2004 150 5 1131 1138 2-s2.0-2942560496
    • (2004) Microbiology , vol.150 , Issue.5 , pp. 1131-1138
    • León-Sicairos, C.R.1    León-Félix, J.2    Arroyo, R.3
  • 60
    • 0035024050 scopus 로고    scopus 로고
    • Trichomonas vaginalis has two fibronectin-like iron-regulated genes
    • 2-s2.0-0035024050 10.1016/S0188-4409(01)00262-4
    • Crouch M. L. V., Alderete J. F., Trichomonas vaginalis has two fibronectin-like iron-regulated genes. Archives of Medical Research 2001 32 2 102 107 2-s2.0-0035024050 10.1016/S0188-4409(01)00262-4
    • (2001) Archives of Medical Research , vol.32 , Issue.2 , pp. 102-107
    • Crouch, M.L.V.1    Alderete, J.F.2
  • 62
    • 1542572794 scopus 로고    scopus 로고
    • Drug resistance in the sexually transmitted protozoan Trichomonas vaginalis
    • 2-s2.0-1542572794 10.1038/sj.cr.7290169
    • Dunne R. L., Dunn L. A., Upcroft P., O'Donoghue P. J., Upcroft J. A., Drug resistance in the sexually transmitted protozoan Trichomonas vaginalis. Cell Research 2003 13 4 239 249 2-s2.0-1542572794 10.1038/sj.cr.7290169
    • (2003) Cell Research , vol.13 , Issue.4 , pp. 239-249
    • Dunne, R.L.1    Dunn, L.A.2    Upcroft, P.3    O'Donoghue, P.J.4    Upcroft, J.A.5
  • 63
    • 0035138734 scopus 로고    scopus 로고
    • Drug targets and mechanisms of resistance in the anaerobic protozoa
    • 2-s2.0-0035138734 10.1128/CMR.14.1.150-164.2001
    • Upcroft P., Upcroft J. A., Drug targets and mechanisms of resistance in the anaerobic protozoa. Clinical Microbiology Reviews 2001 14 1 150 164 2-s2.0-0035138734 10.1128/CMR.14.1.150-164.2001
    • (2001) Clinical Microbiology Reviews , vol.14 , Issue.1 , pp. 150-164
    • Upcroft, P.1    Upcroft, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.