메뉴 건너뛰기




Volumn 4, Issue 10, 2008, Pages

The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm

Author keywords

[No Author keywords available]

Indexed keywords

HISTATIN 5; PROPIDIUM IODIDE; RHODAMINE B; ANTIFUNGAL AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; HISTATIN; HTN3 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

EID: 55449131941     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000190     Document Type: Article
Times cited : (108)

References (70)
  • 1
    • 55449119511 scopus 로고    scopus 로고
    • Kwon-Chung KJ, Bennett JE (1992) Medical mycology. Philadelphia: Lea & Febiger. pp ix, 866.
    • Kwon-Chung KJ, Bennett JE (1992) Medical mycology. Philadelphia: Lea & Febiger. pp ix, 866.
  • 2
    • 0024426243 scopus 로고
    • Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs
    • vanderSpek JC, Wyandt HE, Skare JC, Milunsky A, Oppenheim FG, et al. (1989) Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs. Am J Hum Genet 45: 381-387.
    • (1989) Am J Hum Genet , vol.45 , pp. 381-387
    • vanderSpek, J.C.1    Wyandt, H.E.2    Skare, J.C.3    Milunsky, A.4    Oppenheim, F.G.5
  • 3
    • 0025237388 scopus 로고
    • Salivary histatin 5: Dependence of sequence, chain length, and helical conformation for candidacidal activity
    • Raj PA, Edgerton M, Levine MJ (1990) Salivary histatin 5: dependence of sequence, chain length, and helical conformation for candidacidal activity. J Biol Chem 265: 3898-3905.
    • (1990) J Biol Chem , vol.265 , pp. 3898-3905
    • Raj, P.A.1    Edgerton, M.2    Levine, M.J.3
  • 4
    • 0025733707 scopus 로고
    • Anticandidal activity of major human salivary histatins
    • Xu T, Levitz SM, Diamond RD, Oppenheim FG (1991) Anticandidal activity of major human salivary histatins. Infect Immun 59: 2549-2554.
    • (1991) Infect Immun , vol.59 , pp. 2549-2554
    • Xu, T.1    Levitz, S.M.2    Diamond, R.D.3    Oppenheim, F.G.4
  • 5
    • 0031984449 scopus 로고    scopus 로고
    • Structure of human salivary histatin 5 in aqueous and nonaqueous solutions
    • Raj PA, Marcus E, Sukumaran DK (1998) Structure of human salivary histatin 5 in aqueous and nonaqueous solutions. Biopolymers 45: 51-67.
    • (1998) Biopolymers , vol.45 , pp. 51-67
    • Raj, P.A.1    Marcus, E.2    Sukumaran, D.K.3
  • 6
    • 0035937109 scopus 로고    scopus 로고
    • Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation
    • Helmerhorst EJ, van't Hoff W, Breeuwer P, Veerman EC, Abee T, et al. (2001) Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation. J Biol Chem 276: 5643-5649.
    • (2001) J Biol Chem , vol.276 , pp. 5643-5649
    • Helmerhorst, E.J.1    van't Hoff, W.2    Breeuwer, P.3    Veerman, E.C.4    Abee, T.5
  • 7
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y (1998) Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47: 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 8
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear JD, Wasserman ZR, DeGrado WF (1988) Synthetic amphiphilic peptide models for protein ion channels. Science 240: 1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 9
    • 2542550395 scopus 로고    scopus 로고
    • Interactions of histatin 5 and histatin 5-derived peptides with liposome membranes: Surface effects, translocation and permeabilization
    • Den Hertog AL, Wong Fong Sang HW, Kraayenhof R, Bolscher JG, Van't Hof W, et al. (2004) Interactions of histatin 5 and histatin 5-derived peptides with liposome membranes: surface effects, translocation and permeabilization. Biochem J 379: 665-672.
    • (2004) Biochem J , vol.379 , pp. 665-672
    • Den Hertog, A.L.1    Wong2    Fong Sang, H.W.3    Kraayenhof, R.4    Bolscher, J.G.5    Van't Hof, W.6
  • 11
    • 0035807815 scopus 로고    scopus 로고
    • The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species
    • Helmerhorst EJ, Troxler RF, Oppenheim FG (2001) The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species. Proc Natl Acad Sci U S A 98: 14637-14642.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14637-14642
    • Helmerhorst, E.J.1    Troxler, R.F.2    Oppenheim, F.G.3
  • 12
    • 0033516461 scopus 로고    scopus 로고
    • Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death
    • Koshlukova SE, Lloyd TL, Araujo MW, Edgerton M (1999) Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death. J Biol Chem 274: 18872-18879.
    • (1999) J Biol Chem , vol.274 , pp. 18872-18879
    • Koshlukova, S.E.1    Lloyd, T.L.2    Araujo, M.W.3    Edgerton, M.4
  • 13
    • 0032825193 scopus 로고    scopus 로고
    • Histatin 3-mediated killing of Candida albicans: Effect of extracellular salt concentration on binding and internalization
    • Xu Y, Ambudkar I, Yamagishi H, Swaim W, Walsh TJ, et al. (1999) Histatin 3-mediated killing of Candida albicans: effect of extracellular salt concentration on binding and internalization. Antimicrob Agents Chemother 43: 2256-2262.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 2256-2262
    • Xu, Y.1    Ambudkar, I.2    Yamagishi, H.3    Swaim, W.4    Walsh, T.J.5
  • 14
    • 0036716760 scopus 로고    scopus 로고
    • Human salivary histatin 5 causes disordered volume regulation and cell cycle arrest in Candida albicans
    • Baev D, Li XS, Dong J, Keng P, Edgerton M (2002) Human salivary histatin 5 causes disordered volume regulation and cell cycle arrest in Candida albicans. Infect Immun 70: 4777-4784.
    • (2002) Infect Immun , vol.70 , pp. 4777-4784
    • Baev, D.1    Li, X.S.2    Dong, J.3    Keng, P.4    Edgerton, M.5
  • 15
    • 35348887309 scopus 로고    scopus 로고
    • Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway
    • Vylkova S, Jang WS, Li W, Nayyar N, Edgerton M (2007) Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Eukaryot Cell 6: 1876-1888.
    • (2007) Eukaryot Cell , vol.6 , pp. 1876-1888
    • Vylkova, S.1    Jang, W.S.2    Li, W.3    Nayyar, N.4    Edgerton, M.5
  • 17
    • 34547130335 scopus 로고    scopus 로고
    • Energy depletion protects Candida albicans against antimicrobial peptides by rigidifying its cell membrane
    • Veerman EC, Valentijn-Benz M, Nazmi K, Ruissen AL, Walgreen-Weterings E, et al. (2007) Energy depletion protects Candida albicans against antimicrobial peptides by rigidifying its cell membrane. J Biol Chem 282: 18831-18841.
    • (2007) J Biol Chem , vol.282 , pp. 18831-18841
    • Veerman, E.C.1    Valentijn-Benz, M.2    Nazmi, K.3    Ruissen, A.L.4    Walgreen-Weterings, E.5
  • 18
    • 0033977173 scopus 로고    scopus 로고
    • Candida albicans mutants deficient in respiration are resistant to the small cationic salivary antimicrobial peptide histatin 5
    • Gyurko C, Lendenmann U, Troxler RF, Oppenheim FG (2000) Candida albicans mutants deficient in respiration are resistant to the small cationic salivary antimicrobial peptide histatin 5. Antimicrob Agents Chemother 44: 348-354.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 348-354
    • Gyurko, C.1    Lendenmann, U.2    Troxler, R.F.3    Oppenheim, F.G.4
  • 19
    • 0028321505 scopus 로고
    • Membrane-induced helical conformation of an active candidacidal fragment of salivary histatins
    • Raj PA, Soni SD, Levine MJ (1994) Membrane-induced helical conformation of an active candidacidal fragment of salivary histatins. J Biol Chem 269: 9610-9619.
    • (1994) J Biol Chem , vol.269 , pp. 9610-9619
    • Raj, P.A.1    Soni, S.D.2    Levine, M.J.3
  • 20
    • 0042208078 scopus 로고    scopus 로고
    • Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5
    • Li XS, Reddy MS, Baev D, Edgerton M (2003) Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J Biol Chem 278: 28553-28561.
    • (2003) J Biol Chem , vol.278 , pp. 28553-28561
    • Li, X.S.1    Reddy, M.S.2    Baev, D.3    Edgerton, M.4
  • 21
    • 0030476867 scopus 로고    scopus 로고
    • Actin-, myosin- and ubiquitin-dependent endocytosis
    • Riezman H, Munn A, Geli MI, Hicke L (1996) Actin-, myosin- and ubiquitin-dependent endocytosis. Experientia 52: 1033-1041.
    • (1996) Experientia , vol.52 , pp. 1033-1041
    • Riezman, H.1    Munn, A.2    Geli, M.I.3    Hicke, L.4
  • 22
    • 0031980575 scopus 로고    scopus 로고
    • Endocytic internalization in yeast and animal cells: Similar and different
    • Geli MI, Riezman H (1998) Endocytic internalization in yeast and animal cells: similar and different. J Cell Sci 111(Pt 8): 1031-1037.
    • (1998) J Cell Sci , vol.111 , Issue.PART 8 , pp. 1031-1037
    • Geli, M.I.1    Riezman, H.2
  • 23
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D, Riezman H (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315: 201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 24
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt F, Fotin-Mleczek M, Schwarz H, Fischer R, Brock R (2007) A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8: 848-866.
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 25
    • 0037044462 scopus 로고    scopus 로고
    • Peptide-mediated delivery of green fluorescent protein into yeasts and bacteria
    • Rajarao GK, Nekhotiaeva N, Good L (2002) Peptide-mediated delivery of green fluorescent protein into yeasts and bacteria. FEMS Microbiol Lett 215: 267-272.
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 267-272
    • Rajarao, G.K.1    Nekhotiaeva, N.2    Good, L.3
  • 26
    • 33947672319 scopus 로고    scopus 로고
    • The role of released ATP in killing Candida albicans and other extracellular microbial pathogens by cationic peptides
    • Vylkova S, Sun JN, Edgerton M (2007) The role of released ATP in killing Candida albicans and other extracellular microbial pathogens by cationic peptides. Purinergic Signal 3: 91-97.
    • (2007) Purinergic Signal , vol.3 , pp. 91-97
    • Vylkova, S.1    Sun, J.N.2    Edgerton, M.3
  • 28
    • 20544447535 scopus 로고    scopus 로고
    • Candidacidal effects of two antimicrobial peptides: Histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane
    • den Hertog AL, van Marle J, van Veen HA, Van't Hof W, Bolscher JG, et al. (2005) Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane. Biochem J 388: 689-695.
    • (2005) Biochem J , vol.388 , pp. 689-695
    • den Hertog, A.L.1    van Marle, J.2    van Veen, H.A.3    Van't Hof, W.4    Bolscher, J.G.5
  • 29
    • 33645854348 scopus 로고    scopus 로고
    • Role of ubiquitylation in cellular membrane transport
    • Staub O, Rotin D (2006) Role of ubiquitylation in cellular membrane transport. Physiol Rev 86: 669-707.
    • (2006) Physiol Rev , vol.86 , pp. 669-707
    • Staub, O.1    Rotin, D.2
  • 30
    • 33846517041 scopus 로고    scopus 로고
    • Structural insight into the ESCRT-I/-II link and its role in MVB trafficking
    • Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, et al. (2007) Structural insight into the ESCRT-I/-II link and its role in MVB trafficking. Embo J 26: 600-612.
    • (2007) Embo J , vol.26 , pp. 600-612
    • Gill, D.J.1    Teo, H.2    Sun, J.3    Perisic, O.4    Veprintsev, D.B.5
  • 31
    • 0038784064 scopus 로고    scopus 로고
    • Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae
    • Odorizzi G, Katzmann DJ, Babst M, Audhya A, Emr SD (2003) Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae. J Cell Sci 116: 1893-1903.
    • (2003) J Cell Sci , vol.116 , pp. 1893-1903
    • Odorizzi, G.1    Katzmann, D.J.2    Babst, M.3    Audhya, A.4    Emr, S.D.5
  • 32
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli MI, Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272: 533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 33
    • 33747338442 scopus 로고    scopus 로고
    • Transcript profiles of Candida albicans cortical actin patch mutants reflect their cellular defects: Contribution of the Hog1p and Mkc1p signaling pathways
    • Oberholzer U, Nantel A, Berman J, Whiteway M (2006) Transcript profiles of Candida albicans cortical actin patch mutants reflect their cellular defects: contribution of the Hog1p and Mkc1p signaling pathways. Eukaryot Cell 5: 1252-1265.
    • (2006) Eukaryot Cell , vol.5 , pp. 1252-1265
    • Oberholzer, U.1    Nantel, A.2    Berman, J.3    Whiteway, M.4
  • 34
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55: 27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 37
    • 0029851698 scopus 로고    scopus 로고
    • Candidacidal activity of recombinant human salivary histatin-5 and variants
    • Tsai H, Raj PA, Bobek LA (1996) Candidacidal activity of recombinant human salivary histatin-5 and variants. Infect Immun 64: 5000-5007.
    • (1996) Infect Immun , vol.64 , pp. 5000-5007
    • Tsai, H.1    Raj, P.A.2    Bobek, L.A.3
  • 38
    • 0035413118 scopus 로고    scopus 로고
    • The relevance of pH to gingivitis and periodontitis
    • Galgut PN (2001) The relevance of pH to gingivitis and periodontitis. J Int Acad Periodontol 3: 61-67.
    • (2001) J Int Acad Periodontol , vol.3 , pp. 61-67
    • Galgut, P.N.1
  • 39
    • 0036307472 scopus 로고    scopus 로고
    • Low pH inhibits compensatory endocytosis at a step between depolarization and calcium influx
    • Smith RM, Baibakov B, Lambert NA, Vogel SS (2002) Low pH inhibits compensatory endocytosis at a step between depolarization and calcium influx. Traffic 3: 397-406.
    • (2002) Traffic , vol.3 , pp. 397-406
    • Smith, R.M.1    Baibakov, B.2    Lambert, N.A.3    Vogel, S.S.4
  • 41
    • 23844506833 scopus 로고    scopus 로고
    • Candida glabrata is unusual with respect to its resistance to cationic antifungal proteins
    • Helmerhorst EJ, Venuleo C, Beri A, Oppenheim FG (2005) Candida glabrata is unusual with respect to its resistance to cationic antifungal proteins. Yeast 22: 705-714.
    • (2005) Yeast , vol.22 , pp. 705-714
    • Helmerhorst, E.J.1    Venuleo, C.2    Beri, A.3    Oppenheim, F.G.4
  • 42
    • 13244257191 scopus 로고    scopus 로고
    • Role of oxidative phosphorylation in histatin 5-induced cell death in Saccharomyces cerevisiae
    • De Smet K, Reekmans R, Contreras R (2004) Role of oxidative phosphorylation in histatin 5-induced cell death in Saccharomyces cerevisiae. Biotechnol Lett 26: 1781-1785.
    • (2004) Biotechnol Lett , vol.26 , pp. 1781-1785
    • De Smet, K.1    Reekmans, R.2    Contreras, R.3
  • 43
    • 34447288932 scopus 로고    scopus 로고
    • Histatin-induced alterations in Candida albicans: A microscopic and submicroscopic comparison
    • Isola R, Isola M, Conti G, Lantini MS, Riva A (2007) Histatin-induced alterations in Candida albicans: a microscopic and submicroscopic comparison. Microsc Res Tech 70: 607-616.
    • (2007) Microsc Res Tech , vol.70 , pp. 607-616
    • Isola, R.1    Isola, M.2    Conti, G.3    Lantini, M.S.4    Riva, A.5
  • 44
    • 0018594372 scopus 로고
    • Viability assessment by dye exclusion. A fluorescent method for fungal cells
    • Auger P, Marquis G, Dallaire L (1979) Viability assessment by dye exclusion. A fluorescent method for fungal cells. Arch Dermatol 115: 1195-1196.
    • (1979) Arch Dermatol , vol.115 , pp. 1195-1196
    • Auger, P.1    Marquis, G.2    Dallaire, L.3
  • 46
    • 0030600473 scopus 로고    scopus 로고
    • Candidacidal activity of human salivary histatin recombinant variants produced by site-directed mutagenesis
    • Driscoll J, Duan C, Zuo Y, Xu T, Troxler R, et al. (1996) Candidacidal activity of human salivary histatin recombinant variants produced by site-directed mutagenesis. Gene 177: 29-34.
    • (1996) Gene , vol.177 , pp. 29-34
    • Driscoll, J.1    Duan, C.2    Zuo, Y.3    Xu, T.4    Troxler, R.5
  • 48
    • 0141789783 scopus 로고    scopus 로고
    • CaSPA2 is important for polarity establishment and maintenance in Candida albicans
    • Zheng XD, Wang YM, Wang Y (2003) CaSPA2 is important for polarity establishment and maintenance in Candida albicans. Mol Microbiol 49: 1391-1405.
    • (2003) Mol Microbiol , vol.49 , pp. 1391-1405
    • Zheng, X.D.1    Wang, Y.M.2    Wang, Y.3
  • 49
    • 0034442695 scopus 로고    scopus 로고
    • Released ATP is an extracellular cytotoxic mediator in salivary histatin 5-induced killing of Candida albicans
    • Koshlukova SE, Araujo MW, Baev D, Edgerton M (2000) Released ATP is an extracellular cytotoxic mediator in salivary histatin 5-induced killing of Candida albicans. Infect Immun 68: 6848-6856.
    • (2000) Infect Immun , vol.68 , pp. 6848-6856
    • Koshlukova, S.E.1    Araujo, M.W.2    Baev, D.3    Edgerton, M.4
  • 50
    • 0035215744 scopus 로고    scopus 로고
    • Genetically engineered human salivary histatin genes are functional in Candida albicans: Development of a new system for studying histatin candidacidal activity
    • Baev D, Li X, Edgerton M (2001) Genetically engineered human salivary histatin genes are functional in Candida albicans: development of a new system for studying histatin candidacidal activity. Microbiology 147: 3323-3334.
    • (2001) Microbiology , vol.147 , pp. 3323-3334
    • Baev, D.1    Li, X.2    Edgerton, M.3
  • 51
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe M, Nikolenko H, Meyer J, Beyermann M, Bienert M (2001) Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett 501: 146-150.
    • (2001) FEBS Lett , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 52
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki K, Sugishita K, Fujii N, Miyajima K (1995) Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry 34: 3423-3429.
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 53
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • Yeaman MR, Bayer AS, Koo SP, Foss W, Sullam PM (1998) Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action. J Clin Invest 101: 178-187.
    • (1998) J Clin Invest , vol.101 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.P.3    Foss, W.4    Sullam, P.M.5
  • 54
    • 0019394881 scopus 로고
    • Membrane potentials in yeast cells measured by direct and indirect methods
    • Vacata V, Kotyk A, Sigler K (1981) Membrane potentials in yeast cells measured by direct and indirect methods. Biochim Biophys Acta 643: 265-268.
    • (1981) Biochim Biophys Acta , vol.643 , pp. 265-268
    • Vacata, V.1    Kotyk, A.2    Sigler, K.3
  • 55
    • 0023045554 scopus 로고
    • Tetraphenylphosphonium is an indicator of negative membrane potential in Candida albicans
    • Prasad R, Hofer M (1986) Tetraphenylphosphonium is an indicator of negative membrane potential in Candida albicans. Biochim Biophys Acta 861: 377-380.
    • (1986) Biochim Biophys Acta , vol.861 , pp. 377-380
    • Prasad, R.1    Hofer, M.2
  • 56
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann S (2002) Osmotic stress signaling and osmoadaptation in yeasts. Microbiol Mol Biol Rev 66: 300-372.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 57
    • 0031716170 scopus 로고    scopus 로고
    • Inhibitory action of a truncated derivative of the amphibian skin peptide dermaseptin s3 on Saccharomyces cerevisiae
    • Coote PJ, Holyoak CD, Bracey D, Ferdinando DP, Pearce JA (1998) Inhibitory action of a truncated derivative of the amphibian skin peptide dermaseptin s3 on Saccharomyces cerevisiae. Antimicrob Agents Chemother 42: 2160-2170.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2160-2170
    • Coote, P.J.1    Holyoak, C.D.2    Bracey, D.3    Ferdinando, D.P.4    Pearce, J.A.5
  • 58
    • 0242690221 scopus 로고    scopus 로고
    • Respiratory inhibition of isolated mammalian mitochondria by salivary antifungal peptide histatin-5
    • Petruzzelli R, Clementi ME, Marini S, Coletta M, Di Stasio E, et al. (2003) Respiratory inhibition of isolated mammalian mitochondria by salivary antifungal peptide histatin-5. Biochem Biophys Res Commun 311: 1034-1040.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 1034-1040
    • Petruzzelli, R.1    Clementi, M.E.2    Marini, S.3    Coletta, M.4    Di Stasio, E.5
  • 60
    • 0038333259 scopus 로고    scopus 로고
    • Rvs161p and sphingolipids are required for actin repolarization following salt stress
    • Balguerie A, Bagnat M, Bonneu M, Aigle M, Breton AM (2002) Rvs161p and sphingolipids are required for actin repolarization following salt stress. Eukaryot Cell 1: 1021-1031.
    • (2002) Eukaryot Cell , vol.1 , pp. 1021-1031
    • Balguerie, A.1    Bagnat, M.2    Bonneu, M.3    Aigle, M.4    Breton, A.M.5
  • 61
    • 0032908687 scopus 로고    scopus 로고
    • Role of the mitogen-activated protein kinase Hog1p in morphogenesis and virulence of Candida albicans
    • Alonso-Monge R, Navarro-Garcia F, Molero G, Diez-Orejas R, Gustin M, et al. (1999) Role of the mitogen-activated protein kinase Hog1p in morphogenesis and virulence of Candida albicans. J Bacteriol 181: 3058-3068.
    • (1999) J Bacteriol , vol.181 , pp. 3058-3068
    • Alonso-Monge, R.1    Navarro-Garcia, F.2    Molero, G.3    Diez-Orejas, R.4    Gustin, M.5
  • 62
    • 0038735200 scopus 로고    scopus 로고
    • The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans
    • Alonso-Monge R, Navarro-Garcia F, Roman E, Negredo AI, Eisman B, et al. (2003) The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans. Eukaryot Cell 2: 351-361.
    • (2003) Eukaryot Cell , vol.2 , pp. 351-361
    • Alonso-Monge, R.1    Navarro-Garcia, F.2    Roman, E.3    Negredo, A.I.4    Eisman, B.5
  • 63
    • 10144237210 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
    • San Jose C, Alonso R, Perez-Diaz RM, Pla J, Nombela C (1996) The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans. Journal of Bacteriology 178: 5850-5852.
    • (1996) Journal of Bacteriology , vol.178 , pp. 5850-5852
    • San Jose, C.1    Alonso, R.2    Perez-Diaz, R.M.3    Pla, J.4    Nombela, C.5
  • 64
    • 0038153182 scopus 로고    scopus 로고
    • Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure
    • Reiser V, Raitt DC, Saito H (2003) Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. J Cell Biol 161: 1035-1040.
    • (2003) J Cell Biol , vol.161 , pp. 1035-1040
    • Reiser, V.1    Raitt, D.C.2    Saito, H.3
  • 66
    • 30344443097 scopus 로고    scopus 로고
    • Antimicrobial peptides enhance the candidacidal activity of antifungal drugs by promoting the efflux of ATP from Candida cells
    • Tanida T, Okamoto T, Ueta E, Yamamoto T, Osaki T (2006) Antimicrobial peptides enhance the candidacidal activity of antifungal drugs by promoting the efflux of ATP from Candida cells. J Antimicrob Chemother 57: 94-103.
    • (2006) J Antimicrob Chemother , vol.57 , pp. 94-103
    • Tanida, T.1    Okamoto, T.2    Ueta, E.3    Yamamoto, T.4    Osaki, T.5
  • 67
    • 9444284398 scopus 로고    scopus 로고
    • Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans
    • Xu W, Smith FJ Jr, Subaran R, Mitchell AP (2004) Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans. Mol Biol Cell 15: 5528-5537.
    • (2004) Mol Biol Cell , vol.15 , pp. 5528-5537
    • Xu, W.1    Smith Jr, F.J.2    Subaran, R.3    Mitchell, A.P.4
  • 70
    • 26944476331 scopus 로고    scopus 로고
    • Regulated cell-to-cell variation in a cell-fate decision system
    • Colman-Lerner A, Gordon A, Serra E, Chin T, Resnekov O, et al. (2005) Regulated cell-to-cell variation in a cell-fate decision system. Nature 437: 699-706.
    • (2005) Nature , vol.437 , pp. 699-706
    • Colman-Lerner, A.1    Gordon, A.2    Serra, E.3    Chin, T.4    Resnekov, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.