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Volumn 5 JAN, Issue , 2014, Pages

Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy

Author keywords

Anti fungal target; C. albicans virulence; Fungal V ATPase; PH homeostasis; Vacuolar acidification; Vacuolar proton pump

Indexed keywords

ALEXIDINE DIHYDROCHLORIDE; BAFILOMYCIN; CONCANAMYCIN; DISULFIRAM; EBSELEN; FLUCONAZOLE; FUNGAL PROTEIN; PMA1P PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE INHIBITOR; PYRROLE; TONZONIUM BROMIDE; UNCLASSIFIED DRUG;

EID: 84893487618     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2014.00004     Document Type: Review
Times cited : (31)

References (72)
  • 1
    • 0025830077 scopus 로고
    • Biochemical changes associated with the antifungal action of the triazole ICI 153,066
    • doi: 10.1111/j.1574-6968.1991.tb04517.x
    • Barrett-Bee, K., Newboult, L., and Pinder, P. (1991). Biochemical changes associated with the antifungal action of the triazole ICI 153,066 on Candida albicans and Trichophyton quinckeanum. FEMS Microbiol. Lett. 63, 127-131. doi: 10.1111/j.1574-6968.1991.tb04517.x.
    • (1991) Candida albicans and Trichophyton quinckeanum FEMS Microbiol. Lett. , vol.63 , pp. 127-131
    • Barrett-Bee, K.1    Newboult, L.2    Pinder, P.3
  • 2
    • 70349772774 scopus 로고    scopus 로고
    • Growth inhibitory action of ebselen on fluconazole-resistant Candida albicans: role of the plasma membrane H+-ATPase
    • doi: 10.1089/mdr.2009.0872
    • Billack, B., Santoro, M., and Lau-Cam, C. (2009). Growth inhibitory action of ebselen on fluconazole-resistant Candida albicans: role of the plasma membrane H+-ATPase. Microb. Drug Resist. 15, 77-83. doi: 10.1089/mdr.2009.0872.
    • (2009) Microb. Drug Resist. , vol.15 , pp. 77-83
    • Billack, B.1    Santoro, M.2    Lau-Cam, C.3
  • 3
    • 0035990523 scopus 로고    scopus 로고
    • Effects of antioxidants on surfactant peroxidation by stimulated human polymorphonuclear leukocytes
    • doi: 10.1080/10715760290032593
    • Bouhafs, R. K., and Jarstrand, C. (2002). Effects of antioxidants on surfactant peroxidation by stimulated human polymorphonuclear leukocytes. Free Radic. Res. 36, 727-734. doi: 10.1080/10715760290032593.
    • (2002) Free Radic. Res. , vol.36 , pp. 727-734
    • Bouhafs, R.K.1    Jarstrand, C.2
  • 4
    • 33646537184 scopus 로고    scopus 로고
    • V-ATPases as drug targets
    • doi: 10.1007/s10863-005-9485-9489
    • Bowman, E. J., and Bowman, B. J. (2005). V-ATPases as drug targets. J. Bioenerg. Biomembr. 37, 431-435. doi: 10.1007/s10863-005-9485-9489.
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 431-435
    • Bowman, E.J.1    Bowman, B.J.2
  • 5
    • 0030915676 scopus 로고    scopus 로고
    • Mutations of pma-1, the gene encoding the plasma membrane H+-ATPase of Neurospora crassa, suppress inhibition of growth by concanamycin A, a specific inhibitor of vacuolar ATPases
    • doi: 10.1074/jbc.272.23.14776
    • Bowman, E. J., O'Neill, F. J., and Bowman, B. J. (1997). Mutations of pma-1, the gene encoding the plasma membrane H+-ATPase of Neurospora crassa, suppress inhibition of growth by concanamycin A, a specific inhibitor of vacuolar ATPases. J. Biol. Chem. 272, 14776-14786. doi: 10.1074/jbc.272.23.14776.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14776-14786
    • Bowman, E.J.1    O'Neill, F.J.2    Bowman, B.J.3
  • 6
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • doi: 10.1073/pnas.85.21.7972
    • Bowman, E. J., Siebers, A., and Altendorf, K. (1988). Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U.S.A. 85, 7972-7976. doi: 10.1073/pnas.85.21.7972.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 7
    • 14844311968 scopus 로고    scopus 로고
    • The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle trafficking
    • doi: 10.1091/mbc.E04-11-0999
    • Brett, C. L., Tukaye, D. N., Mukherjee, S., and Rao, R. (2005). The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle trafficking. Mol. Biol. Cell 16, 1396-1405. doi: 10.1091/mbc.E04-11-0999.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1396-1405
    • Brett, C.L.1    Tukaye, D.N.2    Mukherjee, S.3    Rao, R.4
  • 8
    • 0033709349 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence
    • Bruckmann, A., Kunkel, W., Hartl, A., Wetzker, R., and Eck, R. (2000). A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence. Microbiology 146(Pt. 11), 2755-2764.
    • (2000) Microbiology , vol.146 , Issue.PART. 11 , pp. 2755-2764
    • Bruckmann, A.1    Kunkel, W.2    Hartl, A.3    Wetzker, R.4    Eck, R.5
  • 9
    • 0028960454 scopus 로고
    • Inositol trisphosphate-dependent and-independent Ca2+ mobilization pathways at the vacuolar membrane of Candida albicans
    • doi: 10.1074/jbc.270.13.7272
    • Calvert, C. M., and Sanders, D. (1995). Inositol trisphosphate-dependent and-independent Ca2+ mobilization pathways at the vacuolar membrane of Candida albicans. J. Biol. Chem. 270, 7272-7280. doi: 10.1074/jbc.270.13.7272.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7272-7280
    • Calvert, C.M.1    Sanders, D.2
  • 10
    • 84858968929 scopus 로고    scopus 로고
    • Inhibitors of V-ATPase proton transport reveal uncoupling functions of tether linking cytosolic and membrane domains of V0 subunit a (Vph1p)
    • doi: 10.1074/jbc.M111. 321133
    • Chan, C. Y., Prudom, C., Raines, S. M., Charkhzarrin, S., Melman, S. D., De Haro, L. P., et al. (2012). Inhibitors of V-ATPase proton transport reveal uncoupling functions of tether linking cytosolic and membrane domains of V0 subunit a (Vph1p). J. Biol. Chem. 287, 10236-10250. doi: 10.1074/jbc.M111. 321133.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10236-10250
    • Chan, C.Y.1    Prudom, C.2    Raines, S.M.3    Charkhzarrin, S.4    Melman, S.D.5    De Haro, L.P.6
  • 11
    • 35548947499 scopus 로고    scopus 로고
    • Evaluation of the antimicrobial activity of ebselen: role of the yeast plasma membrane H+-ATPase
    • doi: 10.1002/jbt.20189
    • Chan, G., Hardej, D., Santoro, M., Lau-Cam, C., and Billack, B. (2007). Evaluation of the antimicrobial activity of ebselen: role of the yeast plasma membrane H+-ATPase. J. Biochem. Mol. Toxicol. 21, 252-264. doi: 10.1002/jbt.20189.
    • (2007) J. Biochem. Mol. Toxicol. , vol.21 , pp. 252-264
    • Chan, G.1    Hardej, D.2    Santoro, M.3    Lau-Cam, C.4    Billack, B.5
  • 12
    • 55949095987 scopus 로고    scopus 로고
    • In search of the holy grail of antifungal therapy
    • discussion 215-196
    • Chapman, S. W., Sullivan, D. C., and Cleary, J. D. (2008). In search of the holy grail of antifungal therapy. Trans. Am. Clin. Climatol. Assoc. 119, 197-215; discussion 215-196.
    • (2008) Trans. Am. Clin. Climatol. Assoc. , vol.119 , pp. 197-215
    • Chapman, S.W.1    Sullivan, D.C.2    Cleary, J.D.3
  • 13
    • 33748748342 scopus 로고    scopus 로고
    • Analysis of strains with mutations in six genes encoding subunits of the V-ATPase: eukaryotes differ in the composition of the V0 sector of the enzyme
    • doi: 10.1074/jbc.M603883200
    • Chavez, C., Bowman, E. J., Reidling, J. C., Haw, K. H., and Bowman, B. J. (2006). Analysis of strains with mutations in six genes encoding subunits of the V-ATPase: eukaryotes differ in the composition of the V0 sector of the enzyme. J. Biol. Chem. 281, 27052-27062. doi: 10.1074/jbc.M603883200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27052-27062
    • Chavez, C.1    Bowman, E.J.2    Reidling, J.C.3    Haw, K.H.4    Bowman, B.J.5
  • 14
    • 68249103865 scopus 로고    scopus 로고
    • How human pathogenic fungi sense and adapt to pH: the link to virulence
    • doi: 10.1016/j.mib.2009.05.006
    • Davis, D. A. (2009). How human pathogenic fungi sense and adapt to pH: the link to virulence. Curr. Opin. Microbiol. 12, 365-370. doi: 10.1016/j.mib.2009.05.006.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 365-370
    • Davis, D.A.1
  • 15
    • 84856001089 scopus 로고    scopus 로고
    • Evolutionary biology: a ratchet for protein complexity
    • doi: 10.1038/nature10816
    • Doolittle, W. F. (2012). Evolutionary biology: a ratchet for protein complexity. Nature 481, 270-271. doi: 10.1038/nature10816.
    • (2012) Nature , vol.481 , pp. 270-271
    • Doolittle, W.F.1
  • 16
    • 0027322674 scopus 로고
    • Inhibitory effect of modified bafilomycins and concanamycins on P-and V-type adenosinetriphosphatases
    • doi: 10.1021/bi00066a008
    • Drose, S., Bindseil, K. U., Bowman, E. J., Siebers, A., Zeeck, A., and Altendorf, K. (1993). Inhibitory effect of modified bafilomycins and concanamycins on P-and V-type adenosinetriphosphatases. Biochemistry 32, 3902-3906. doi: 10.1021/bi00066a008.
    • (1993) Biochemistry , vol.32 , pp. 3902-3906
    • Drose, S.1    Bindseil, K.U.2    Bowman, E.J.3    Siebers, A.4    Zeeck, A.5    Altendorf, K.6
  • 17
    • 17644399855 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H+-ATPase subunit Vma7p
    • doi: 10.1016/j.ijmm.2004.12.007
    • Eck, R., Nguyen, M., Gunther, J., Kunkel, W., and Zipfel, P. F. (2005). The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H+-ATPase subunit Vma7p. Int. J. Med. Microbiol. 295, 57-66. doi: 10.1016/j.ijmm.2004.12.007.
    • (2005) Int. J. Med. Microbiol. , vol.295 , pp. 57-66
    • Eck, R.1    Nguyen, M.2    Gunther, J.3    Kunkel, W.4    Zipfel, P.F.5
  • 18
    • 0035166540 scopus 로고    scopus 로고
    • Multiple virulence factors of Cryptococcus neoformans are dependent on VPH1
    • doi: 10.1046/j.1365-2958.2001.02712.x
    • Erickson, T., Liu, L., Gueyikian, A., Zhu, X., Gibbons, J., and Williamson, P. R. (2001). Multiple virulence factors of Cryptococcus neoformans are dependent on VPH1. Mol. Microbiol. 42, 1121-1131. doi: 10.1046/j.1365-2958.2001.02712.x.
    • (2001) Mol. Microbiol. , vol.42 , pp. 1121-1131
    • Erickson, T.1    Liu, L.2    Gueyikian, A.3    Zhu, X.4    Gibbons, J.5    Williamson, P.R.6
  • 19
    • 84856022796 scopus 로고    scopus 로고
    • Evolution of increased complexity in a molecular machine
    • doi: 10.1038/nature10724
    • Finnigan, G. C., Hanson-Smith, V., Stevens, T. H., and Thornton, J. W. (2012). Evolution of increased complexity in a molecular machine. Nature 481, 360-364. doi: 10.1038/nature10724.
    • (2012) Nature , vol.481 , pp. 360-364
    • Finnigan, G.C.1    Hanson-Smith, V.2    Stevens, T.H.3    Thornton, J.W.4
  • 20
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • doi: 10.1038/nrm2272
    • Forgac, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929. doi: 10.1038/nrm2272.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 21
    • 0030033020 scopus 로고    scopus 로고
    • Antifungal agents: chemotherapeutic targets and immunologic strategies
    • Georgopapadakou, N. H., and Walsh, T. J. (1996). Antifungal agents: chemotherapeutic targets and immunologic strategies. Antimicrob. Agents Chemother. 40, 279-291.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 279-291
    • Georgopapadakou, N.H.1    Walsh, T.J.2
  • 22
    • 84885627084 scopus 로고    scopus 로고
    • Novel regulatory mechanisms of pathogenicity and virulence to combat MDR in
    • 240209. doi: 10.1155/2013/240209
    • Hameed, S., and Fatima, Z. (2013). Novel regulatory mechanisms of pathogenicity and virulence to combat MDR in. Int. J. Microbiol. 2013, 240209. doi: 10.1155/2013/240209.
    • (2013) Int. J. Microbiol. , vol.2013
    • Hameed, S.1    Fatima, Z.2
  • 23
    • 51649086978 scopus 로고    scopus 로고
    • The Histoplasma capsulatum vacuolar ATPase is required for iron homeostasis, intracellular replication in macrophages and virulence in a murine model of histoplasmosis
    • doi: 10.1111/j.1365-2958.2008.06395.x
    • Hilty, J., Smulian, A. G., and Newman, S. L. (2008). The Histoplasma capsulatum vacuolar ATPase is required for iron homeostasis, intracellular replication in macrophages and virulence in a murine model of histoplasmosis. Mol. Microbiol. 70, 127-139. doi: 10.1111/j.1365-2958.2008.06395.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 127-139
    • Hilty, J.1    Smulian, A.G.2    Newman, S.L.3
  • 24
    • 66949118944 scopus 로고    scopus 로고
    • Epidemiology and outcomes of candidemia in 2019 patients: data from the prospective antifungal therapy alliance registry
    • doi: 10.1086/599039
    • Horn, D. L., Neofytos, D., Anaissie, E. J., Fishman, J. A., Steinbach, W. J., Olyaei, A. J., et al. (2009). Epidemiology and outcomes of candidemia in 2019 patients: data from the prospective antifungal therapy alliance registry. Clin. Infect. Dis 48, 1695-1703. doi: 10.1086/599039.
    • (2009) Clin. Infect. Dis , vol.48 , pp. 1695-1703
    • Horn, D.L.1    Neofytos, D.2    Anaissie, E.J.3    Fishman, J.A.4    Steinbach, W.J.5    Olyaei, A.J.6
  • 25
    • 79953171488 scopus 로고    scopus 로고
    • pH-dependent cargo sorting from the Golgi
    • doi: 10.1074/jbc.M110.197889
    • Huang, C., and Chang, A. (2011). pH-dependent cargo sorting from the Golgi. J. Biol. Chem. 286, 10058-10065. doi: 10.1074/jbc.M110.197889.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10058-10065
    • Huang, C.1    Chang, A.2
  • 26
    • 59149095897 scopus 로고    scopus 로고
    • Inhibitors of V-ATPases: old and new players
    • doi: 10.1242/jeb.024067
    • Huss, M., and Wieczorek, H. (2009). Inhibitors of V-ATPases: old and new players. J. Exp. Biol. 212, 341-346. doi: 10.1242/jeb.024067.
    • (2009) J. Exp. Biol. , vol.212 , pp. 341-346
    • Huss, M.1    Wieczorek, H.2
  • 27
    • 0037306194 scopus 로고    scopus 로고
    • Phagocytosis and intracellular fate of Aspergillus fumigatus conidia in alveolar macrophages
    • doi: 10.1128/IAI.71.2.891-903.2003
    • Ibrahim-Granet, O., Philippe, B., Boleti, H., Boisvieux-Ulrich, E., Grenet, D., Stern, M., et al. (2003). Phagocytosis and intracellular fate of Aspergillus fumigatus conidia in alveolar macrophages. Infect. Immun. 71, 891-903. doi: 10.1128/IAI.71.2.891-903.2003.
    • (2003) Infect. Immun. , vol.71 , pp. 891-903
    • Ibrahim-Granet, O.1    Philippe, B.2    Boleti, H.3    Boisvieux-Ulrich, E.4    Grenet, D.5    Stern, M.6
  • 28
    • 46049100082 scopus 로고    scopus 로고
    • Function, structure and regulation of the vacuolar (H+)-ATPases
    • doi: 10.1016/j.abb.2008.03.025
    • Jefferies, K. C., Cipriano, D. J., and Forgac, M. (2008). Function, structure and regulation of the vacuolar (H+)-ATPases. Arch. Biochem. Biophys. 476, 33-42. doi: 10.1016/j.abb.2008.03.025.
    • (2008) Arch. Biochem. Biophys. , vol.476 , pp. 33-42
    • Jefferies, K.C.1    Cipriano, D.J.2    Forgac, M.3
  • 29
    • 0036208623 scopus 로고    scopus 로고
    • Candida albicans sterol C-14 reductase, encoded by the ERG24 gene, as a potential antifungal target site
    • doi: 10.1128/AAC.46.4.947-957.2002
    • Jia, N., Arthington-Skaggs, B., Lee, W., Pierson, C. A., Lees, N. D., Eckstein, J., et al. (2002). Candida albicans sterol C-14 reductase, encoded by the ERG24 gene, as a potential antifungal target site. Antimicrob. Agents Chemother. 46, 947-957. doi: 10.1128/AAC.46.4.947-957.2002.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 947-957
    • Jia, N.1    Arthington-Skaggs, B.2    Lee, W.3    Pierson, C.A.4    Lees, N.D.5    Eckstein, J.6
  • 30
    • 77649182092 scopus 로고    scopus 로고
    • Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry
    • doi: 10.1016/j.ab.2009.12.020
    • Johnson, R. M., Allen, C., Melman, S. D., Waller, A., Young, S. M., Sklar, L. A., et al. (2010). Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry. Anal. Biochem. 398, 203-211. doi: 10.1016/j.ab.2009.12.020.
    • (2010) Anal. Biochem. , vol.398 , pp. 203-211
    • Johnson, R.M.1    Allen, C.2    Melman, S.D.3    Waller, A.4    Young, S.M.5    Sklar, L.A.6
  • 31
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H +-ATPase
    • doi: 10.1128/MMBR.70.1.177-191.2006
    • Kane, P. M. (2006). The where, when, and how of organelle acidification by the yeast vacuolar H +-ATPase. Microbiol. Mol. Biol. Rev. 70, 177-191. doi: 10.1128/MMBR.70.1.177-191.2006.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 32
    • 38349193176 scopus 로고    scopus 로고
    • The long physiological reach of the yeast vacuolar H+-ATPase
    • doi: 10.1007/s10863-007-9112-z
    • Kane, P. M. (2007). The long physiological reach of the yeast vacuolar H+-ATPase. J. Bioenerg. Biomembr. 39, 415-421. doi: 10.1007/s10863-007-9112-z.
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 415-421
    • Kane, P.M.1
  • 33
    • 84860815342 scopus 로고    scopus 로고
    • Targeting reversible disassembly as a mechanism of controlling V-ATPase activity
    • doi: 10.2174/138920312800493142
    • Kane, P. M. (2012). Targeting reversible disassembly as a mechanism of controlling V-ATPase activity. Curr. Protein Peptide Sci. 13, 117-123. doi: 10.2174/138920312800493142.
    • (2012) Curr. Protein Peptide Sci. , vol.13 , pp. 117-123
    • Kane, P.M.1
  • 34
    • 0033974290 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H(+)-ATPase
    • Kane, P. M., and Parra, K. J. (2000). Assembly and regulation of the yeast vacuolar H(+)-ATPase. J. Exp. Biol. 203, 81-87.
    • (2000) J. Exp. Biol. , vol.203 , pp. 81-87
    • Kane, P.M.1    Parra, K.J.2
  • 35
    • 68249110928 scopus 로고    scopus 로고
    • Fungi pathogenic to humans: molecular bases of virulence of Candida albicans, Cryptococcus neoformans and Aspergillus fumigatus
    • Karkowska-Kuleta, J., Rapala-Kozik, M., and Kozik, A. (2009). Fungi pathogenic to humans: molecular bases of virulence of Candida albicans, Cryptococcus neoformans and Aspergillus fumigatus. Acta Biochim. Pol. 56, 211-224.
    • (2009) Acta Biochim. Pol. , vol.56 , pp. 211-224
    • Karkowska-Kuleta, J.1    Rapala-Kozik, M.2    Kozik, A.3
  • 36
    • 0026040633 scopus 로고
    • Dimorphism-associated changes in plasma membrane H(+)-ATPase activity of Candida albicans
    • doi: 10.1007/BF00248719
    • Kaur, S., and Mishra, P. (1991). Dimorphism-associated changes in plasma membrane H(+)-ATPase activity of Candida albicans. Arch. Microbiol. 156, 412-415. doi: 10.1007/BF00248719.
    • (1991) Arch. Microbiol. , vol.156 , pp. 412-415
    • Kaur, S.1    Mishra, P.2
  • 37
    • 0035947711 scopus 로고    scopus 로고
    • Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation
    • doi: 10.1074/jbc.M010790200
    • Kawasaki-Nishi, S., Nishi, T., and Forgac, M. (2001). Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J. Biol. Chem. 276, 17941-17948. doi: 10.1074/jbc.M010790200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17941-17948
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 38
    • 36549025999 scopus 로고    scopus 로고
    • Polymicrobial bloodstream infections involving Candida species: analysis of patients and review of the literature
    • doi: 10.1016/j.diagmicrobio.2007.07.001
    • Klotz, S. A., Chasin, B. S., Powell, B., Gaur, N. K., and Lipke, P. N. (2007). Polymicrobial bloodstream infections involving Candida species: analysis of patients and review of the literature. Diagn. Microbiol. Infect. Dis. 59, 401-406. doi: 10.1016/j.diagmicrobio.2007.07.001.
    • (2007) Diagn. Microbiol. Infect. Dis. , vol.59 , pp. 401-406
    • Klotz, S.A.1    Chasin, B.S.2    Powell, B.3    Gaur, N.K.4    Lipke, P.N.5
  • 39
    • 0025162975 scopus 로고
    • Defective plasma membrane H(+)-ATPase or orthovanadate resistant mutants from Candida albicans, a pathogenic yeast
    • Mahanty, S. K., Gupta, P., Banerjee, U., Fotedar, R., and Prasad, R. (1990). Defective plasma membrane H(+)-ATPase or orthovanadate resistant mutants from Candida albicans, a pathogenic yeast. Biochem. Int. 22, 11-20.
    • (1990) Biochem. Int. , vol.22 , pp. 11-20
    • Mahanty, S.K.1    Gupta, P.2    Banerjee, U.3    Fotedar, R.4    Prasad, R.5
  • 40
    • 0028224791 scopus 로고
    • STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p
    • Manolson, M. F., Wu, B., Proteau, D., Taillon, B. E., Roberts, B. T., Hoyt, M. A., et al. (1994). STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J. Biol. Chem. 269, 14064-14074.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14064-14074
    • Manolson, M.F.1    Wu, B.2    Proteau, D.3    Taillon, B.E.4    Roberts, B.T.5    Hoyt, M.A.6
  • 41
    • 47349120492 scopus 로고    scopus 로고
    • The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function
    • doi: 10.1016/j.ceb.2008.03.015
    • Marshansky, V., and Futai, M. (2008). The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function. Curr. Opin. Cell Biol. 20, 415-426. doi: 10.1016/j.ceb.2008.03.015.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 42
    • 50649120655 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast
    • doi: 10.1074/jbc.M710470200
    • Martinez-Munoz, G. A., and Kane, P. (2008). Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast. J. Biol. Chem. 283, 20309-20319. doi: 10.1074/jbc.M710470200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20309-20319
    • Martinez-Munoz, G.A.1    Kane, P.2
  • 43
    • 0025872045 scopus 로고
    • Cloning and characterization of the plasma membrane H(+)-ATPase from Candida albicans
    • Monk, B. C., Kurtz, M. B., Marrinan, J. A., and Perlin, D. S. (1991). Cloning and characterization of the plasma membrane H(+)-ATPase from Candida albicans. J. Bacteriol. 173, 6826-6836.
    • (1991) J. Bacteriol. , vol.173 , pp. 6826-6836
    • Monk, B.C.1    Kurtz, M.B.2    Marrinan, J.A.3    Perlin, D.S.4
  • 44
    • 0027177656 scopus 로고
    • The Candida albicans plasma membrane and H(+)-ATPase during yeast growth and germ tube formation
    • Monk, B. C., Niimi, M., and Shepherd, M. G. (1993). The Candida albicans plasma membrane and H(+)-ATPase during yeast growth and germ tube formation. J. Bacteriol. 175, 5566-5574.
    • (1993) J. Bacteriol. , vol.175 , pp. 5566-5574
    • Monk, B.C.1    Niimi, M.2    Shepherd, M.G.3
  • 45
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans secreted aspartyl proteinases in virulence and pathogenesis
    • doi: 10.1128/MMBR.67.3.400-428.2003
    • Naglik, J. R., Challacombe, S. J., and Hube, B. (2003). Candida albicans secreted aspartyl proteinases in virulence and pathogenesis. Microbiol. Mol. Biol. Rev. 67, 400-428. doi: 10.1128/MMBR.67.3.400-428.2003.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 46
    • 84859737001 scopus 로고    scopus 로고
    • Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase
    • doi: 10.1074/jbc.M112.343962
    • Oot, R. A., and Wilkens, S. (2012). Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase. J. Biol. Chem. 287, 13396-13406. doi: 10.1074/jbc.M112.343962.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13396-13406
    • Oot, R.A.1    Wilkens, S.2
  • 47
    • 75849144694 scopus 로고    scopus 로고
    • Candida albicans PEP12 is required for biofilm integrity and in vivo virulence
    • doi: 10.1128/EC.00295-299
    • Palanisamy, S. K., Ramirez, M. A., Lorenz, M., and Lee, S. A. (2010). Candida albicans PEP12 is required for biofilm integrity and in vivo virulence. Eukaryot. Cell. 9, 266-277. doi: 10.1128/EC.00295-299.
    • (2010) Eukaryot. Cell. , vol.9 , pp. 266-277
    • Palanisamy, S.K.1    Ramirez, M.A.2    Lorenz, M.3    Lee, S.A.4
  • 48
    • 84857755621 scopus 로고    scopus 로고
    • Deus ex Candida genetics: overcoming the hurdles for the development of a molecular toolbox in the CTG clade
    • doi: 10.1099/mic.0.055244-55240
    • Papon, N., Courdavault, V., Clastre, M., Simkin, A. J., Creche, J., and Giglioli-Guivarc'h, N. (2012). Deus ex Candida genetics: overcoming the hurdles for the development of a molecular toolbox in the CTG clade. Microbiology 158, 585-600. doi: 10.1099/mic.0.055244-55240.
    • (2012) Microbiology , vol.158 , pp. 585-600
    • Papon, N.1    Courdavault, V.2    Clastre, M.3    Simkin, A.J.4    Creche, J.5    Giglioli-Guivarc'h, N.6
  • 49
    • 84884563052 scopus 로고    scopus 로고
    • Vacuolar ATPase (V-ATPase) a model proton pump for antifungal drug discovery
    • eds G. P. Tegos and E. Mylonakis (Oxfordshire: CABI)
    • Parra, K. J. (2012). "Vacuolar ATPase (V-ATPase) a model proton pump for antifungal drug discovery," in Emerging Strategies for Antimicrobial Drug Discovery, eds G. P. Tegos and E. Mylonakis (Oxfordshire: CABI), 89-100.
    • (2012) Emerging Strategies for Antimicrobial Drug Discovery , pp. 89-100
    • Parra, K.J.1
  • 50
    • 84883715425 scopus 로고    scopus 로고
    • Essential role for vacuolar acidification in Candida albicans virulence
    • doi: 10.1074/jbc.M113.494815
    • Patenaude, C., Zhang, Y., Cormack, B., Kohler, J., and Rao, R. (2013). Essential role for vacuolar acidification in Candida albicans virulence. J. Biol. Chem. 288, 26256-26264. doi: 10.1074/jbc.M113.494815.
    • (2013) J. Biol. Chem. , vol.288 , pp. 26256-26264
    • Patenaude, C.1    Zhang, Y.2    Cormack, B.3    Kohler, J.4    Rao, R.5
  • 51
    • 0034704152 scopus 로고    scopus 로고
    • Altered distribution of the yeast plasma membrane H+-ATPase as a feature of vacuolar H+-ATPase null mutants
    • doi: 10.1074/jbc.M007011200
    • Perzov, N., Nelson, H., and Nelson, N. (2000). Altered distribution of the yeast plasma membrane H+-ATPase as a feature of vacuolar H+-ATPase null mutants. J. Biol. Chem. 275, 40088-40095. doi: 10.1074/jbc.M007011200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40088-40095
    • Perzov, N.1    Nelson, H.2    Nelson, N.3
  • 52
    • 33846466508 scopus 로고    scopus 로고
    • Epidemiology of invasive candidiasis: a persistent public health problem
    • doi: 10.1128/CMR.00029-26
    • Pfaller, M. A., and Diekema, D. J. (2007). Epidemiology of invasive candidiasis: a persistent public health problem. Clin. Microbiol. Rev. 20, 133-163. doi: 10.1128/CMR.00029-26.
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 133-163
    • Pfaller, M.A.1    Diekema, D.J.2
  • 53
    • 19044365896 scopus 로고    scopus 로고
    • The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence
    • doi: 10.1099/mic.0.27505-27500
    • Poltermann, S., Nguyen, M., Gunther, J., Wendland, J., Hartl, A., Kunkel, W., et al. (2005). The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence. Microbiology 151, 1645-1655. doi: 10.1099/mic.0.27505-27500.
    • (2005) Microbiology , vol.151 , pp. 1645-1655
    • Poltermann, S.1    Nguyen, M.2    Gunther, J.3    Wendland, J.4    Hartl, A.5    Kunkel, W.6
  • 54
    • 84873738520 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of interactions between subunits of the peripheral stalk region of human V-ATPase
    • doi: 10.1371/journal.pone.0055704
    • Rahman, S., Yamato, I., Saijo, S., Mizutani, K., Ishizuka-Katsura, Y., Ohsawa, N., et al. (2013). Biochemical and biophysical properties of interactions between subunits of the peripheral stalk region of human V-ATPase. PLoS ONE 8:e55704. doi: 10.1371/journal.pone.0055704.
    • (2013) PLoS ONE , vol.8
    • Rahman, S.1    Yamato, I.2    Saijo, S.3    Mizutani, K.4    Ishizuka-Katsura, Y.5    Ohsawa, N.6
  • 55
    • 84874764422 scopus 로고    scopus 로고
    • Deletion of vacuolar proton-translocating ATPase V(o)a isoforms clarifies the role of vacuolar pH as a determinant of virulence-associated traits in Candida albicans
    • doi: 10.1074/jbc.M112.426197
    • Raines, S. M., Rane, H. S., Bernardo, S. M., Binder, J. L., Lee, S. A., and Parra, K. J. (2013). Deletion of vacuolar proton-translocating ATPase V(o)a isoforms clarifies the role of vacuolar pH as a determinant of virulence-associated traits in Candida albicans. J. Biol. Chem. 288, 6190-6201. doi: 10.1074/jbc.M112.426197.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6190-6201
    • Raines, S.M.1    Rane, H.S.2    Bernardo, S.M.3    Binder, J.L.4    Lee, S.A.5    Parra, K.J.6
  • 56
    • 84884538946 scopus 로고    scopus 로고
    • Candida albicans VMA3 is necessary for V-ATPase assembly and function and contributes to secretion and filamentation
    • doi: 10.1128/EC.00118-113
    • Rane, H. S., Bernardo, S. M., Raines, S. M., Binder, J. L., Parra, K. J., and Lee, S. A. (2013). Candida albicans VMA3 is necessary for V-ATPase assembly and function and contributes to secretion and filamentation. Eukaryot. Cell. 12, 1369-1382. doi: 10.1128/EC.00118-113.
    • (2013) Eukaryot. Cell. , vol.12 , pp. 1369-1382
    • Rane, H.S.1    Bernardo, S.M.2    Raines, S.M.3    Binder, J.L.4    Parra, K.J.5    Lee, S.A.6
  • 57
    • 84856551310 scopus 로고    scopus 로고
    • Persistence versus escape: Aspergillus terreus and Aspergillus fumigatus employ different strategies during interactions with macrophages
    • doi: 10.1371/journal.pone.0031223
    • Slesiona, S., Gressler, M., Mihlan, M., Zaehle, C., Schaller, M., Barz, D., et al. (2012). Persistence versus escape: Aspergillus terreus and Aspergillus fumigatus employ different strategies during interactions with macrophages. PLoS ONE 7:e31223. doi: 10.1371/journal.pone.0031223.
    • (2012) PLoS ONE , vol.7
    • Slesiona, S.1    Gressler, M.2    Mihlan, M.3    Zaehle, C.4    Schaller, M.5    Barz, D.6
  • 58
    • 0033840425 scopus 로고    scopus 로고
    • Molecular characterization of the plasma membrane H(+)-ATPase, an antifungal target in Cryptococcus neoformans
    • doi: 10.1128/AAC.44.9.2349-2355.2000
    • Soteropoulos, P., Vaz, T., Santangelo, R., Paderu, P., Huang, D. Y., Tamas, M. J., et al. (2000). Molecular characterization of the plasma membrane H(+)-ATPase, an antifungal target in Cryptococcus neoformans. Antimicrob. Agents Chemother. 44, 2349-2355. doi: 10.1128/AAC.44.9.2349-2355.2000.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2349-2355
    • Soteropoulos, P.1    Vaz, T.2    Santangelo, R.3    Paderu, P.4    Huang, D.Y.5    Tamas, M.J.6
  • 59
    • 0024012977 scopus 로고
    • Cytoplasmic alkalinization during germ tube formation in Candida albicans
    • doi: 10.1099/00221287-134-5-1079
    • Stewart, E., Gow, N. A., and Bowen, D. V. (1988). Cytoplasmic alkalinization during germ tube formation in Candida albicans. J. Gen. Microbiol. 134, 1079-1087. doi: 10.1099/00221287-134-5-1079.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1079-1087
    • Stewart, E.1    Gow, N.A.2    Bowen, D.V.3
  • 60
    • 0024576364 scopus 로고
    • Changes in internal and external pH accompanying growth of Candida albicans: studies of non-dimorphic variants
    • doi: 10.1007/BF00414430
    • Stewart, E., Hawser, S., and Gow, N. A. (1989). Changes in internal and external pH accompanying growth of Candida albicans: studies of non-dimorphic variants. Arch. Microbiol. 151, 149-153. doi: 10.1007/BF00414430.
    • (1989) Arch. Microbiol. , vol.151 , pp. 149-153
    • Stewart, E.1    Hawser, S.2    Gow, N.A.3
  • 61
    • 80052965456 scopus 로고    scopus 로고
    • Growth of Candida albicans hyphae
    • doi: 10.1038/nrmicro2636
    • Sudbery, P. E. (2011). Growth of Candida albicans hyphae. Nat. Rev. Microbiol. 9, 737-748. doi: 10.1038/nrmicro2636.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 737-748
    • Sudbery, P.E.1
  • 62
    • 79952201156 scopus 로고    scopus 로고
    • Vacuolar-type proton pump ATPases: roles of subunit isoforms in physiology and pathology
    • Sun-Wada, G. H., and Wada, Y. (2010). Vacuolar-type proton pump ATPases: roles of subunit isoforms in physiology and pathology. Histol. Histopathol. 25, 1611-1620.
    • (2010) Histol. Histopathol. , vol.25 , pp. 1611-1620
    • Sun-Wada, G.H.1    Wada, Y.2
  • 63
    • 0142089017 scopus 로고    scopus 로고
    • Vacuolar H+ pumping ATPases in luminal acidic organelles and extracellular compartments: common rotational mechanism and diverse physiological roles
    • doi: 10.1023/A:1025780932403
    • Sun-Wada, G. H., Wada, Y., and Futai, M. (2003). Vacuolar H+ pumping ATPases in luminal acidic organelles and extracellular compartments: common rotational mechanism and diverse physiological roles. J. Bioenerg. Biomembr. 35, 347-358. doi: 10.1023/A:1025780932403.
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 347-358
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 64
    • 80051532058 scopus 로고    scopus 로고
    • Consequences of loss of Vph1 protein-containing vacuolar ATPases (V-ATPases) for overall cellular pH homeostasis
    • doi: 10.1074/jbc.M111.251363
    • Tarsio, M., Zheng, H., Smardon, A. M., Martinez-Munoz, G. A., and Kane, P. M. (2011). Consequences of loss of Vph1 protein-containing vacuolar ATPases (V-ATPases) for overall cellular pH homeostasis. J. Biol. Chem. 286, 28089-28096. doi: 10.1074/jbc.M111.251363.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28089-28096
    • Tarsio, M.1    Zheng, H.2    Smardon, A.M.3    Martinez-Munoz, G.A.4    Kane, P.M.5
  • 65
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • doi: 10.1021/bi100397s
    • Toei, M., Saum, R., and Forgac, M. (2010). Regulation and isoform function of the V-ATPases. Biochemistry 49, 4715-4723. doi: 10.1021/bi100397s.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 66
    • 84875706479 scopus 로고    scopus 로고
    • Intracellular pH homeostasis in Candida glabrata in infection-associated conditions
    • doi: 10.1099/mic.0.063610-63610
    • Ullah, A., Lopes, M. I., Brul, S., and Smits, G. J. (2013). Intracellular pH homeostasis in Candida glabrata in infection-associated conditions. Microbiology 159, 803-813. doi: 10.1099/mic.0.063610-63610.
    • (2013) Microbiology , vol.159 , pp. 803-813
    • Ullah, A.1    Lopes, M.I.2    Brul, S.3    Smits, G.J.4
  • 67
    • 0022167826 scopus 로고
    • Biochemical targets for antifungal azole derivatives: hypothesis on the mode of action
    • doi: 10.1007/978-1-4613-9547-8_12
    • Vanden Bossche, H. (1985). Biochemical targets for antifungal azole derivatives: hypothesis on the mode of action. Curr. Top. Med. Mycol. 1, 313-351. doi: 10.1007/978-1-4613-9547-8_12.
    • (1985) Curr. Top. Med. Mycol. , vol.1 , pp. 313-351
    • Vanden Bossche, H.1
  • 68
    • 56949088879 scopus 로고    scopus 로고
    • Vacuoles and fungal biology
    • doi: 10.1016/j.mib.2008.09.017 doi: 10.1016/j.mib.2008.09.017
    • Veses, V., Richards, A., and Gow, N. A. (2008). Vacuoles and fungal biology. Curr. Opin. Microbiol. 11, 503-510. doi: 10.1016/j.mib.2008.09.017 doi: 10.1016/j.mib.2008.09.017.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 503-510
    • Veses, V.1    Richards, A.2    Gow, N.A.3
  • 69
    • 45149086178 scopus 로고    scopus 로고
    • An endocytic mechanism for haemoglobin-iron acquisition in Candida albicans
    • doi: 10.1111/j.1365-2958.2008.06277.x doi: 10.1111/j.1365-2958.2008.06277.x
    • Weissman, Z., Shemer, R., Conibear, E., and Kornitzer, D. (2008). An endocytic mechanism for haemoglobin-iron acquisition in Candida albicans. Mol. Microbiol. 69, 201-217. doi: 10.1111/j.1365-2958.2008.06277.x doi: 10.1111/j.1365-2958.2008.06277.x.
    • (2008) Mol. Microbiol. , vol.69 , pp. 201-217
    • Weissman, Z.1    Shemer, R.2    Conibear, E.3    Kornitzer, D.4
  • 70
    • 1542268206 scopus 로고    scopus 로고
    • Selective optimization of side activities: another way for drug discovery
    • doi: 10.1021/jm030480f
    • Wermuth, C. G. (2004). Selective optimization of side activities: another way for drug discovery. J. Med. Chem. 47, 1303-1314. doi: 10.1021/jm030480f.
    • (2004) J. Med. Chem. , vol.47 , pp. 1303-1314
    • Wermuth, C.G.1
  • 71
    • 8444247959 scopus 로고    scopus 로고
    • Azaanalogues of ebselen as antimicrobial and antiviral agents: synthesis and properties
    • doi: 10.1016/j.farmac.2004.07.003
    • Wojtowicz, H., Kloc, K., Maliszewska, I., Mlochowski, J., Pietka, M., and Piasecki, E. (2004). Azaanalogues of ebselen as antimicrobial and antiviral agents: synthesis and properties. Farmaco 59, 863-868. doi: 10.1016/j.farmac.2004.07.003.
    • (2004) Farmaco , vol.59 , pp. 863-868
    • Wojtowicz, H.1    Kloc, K.2    Maliszewska, I.3    Mlochowski, J.4    Pietka, M.5    Piasecki, E.6
  • 72
    • 77954685203 scopus 로고    scopus 로고
    • Requirement for ergosterol in V-ATPase function underlies antifungal activity of azole drugs
    • doi: 10.1371/journal.ppat.1000939
    • Zhang, Y. Q., Gamarra, S., Garcia-Effron, G., Park, S., Perlin, D. S., and Rao, R. (2010). Requirement for ergosterol in V-ATPase function underlies antifungal activity of azole drugs. PLoS Pathog. 6:e1000939. doi: 10.1371/journal.ppat.1000939.
    • (2010) PLoS Pathog. , vol.6
    • Zhang, Y.Q.1    Gamarra, S.2    Garcia-Effron, G.3    Park, S.4    Perlin, D.S.5    Rao, R.6


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