메뉴 건너뛰기




Volumn 13, Issue 8, 2014, Pages 950-957

Interplay between Candida albicans and the antimicrobial peptide armory

Author keywords

[No Author keywords available]

Indexed keywords

CANDIDA ALBICANS;

EID: 84907478489     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00093-14     Document Type: Review
Times cited : (110)

References (90)
  • 1
    • 84860244125 scopus 로고    scopus 로고
    • Interplay between Candida albicans and the mammalian innate host defense
    • Cheng SC, Joosten LA, Kullberg BJ, Netea MG. 2012. Interplay between Candida albicans and the mammalian innate host defense. Infect. Immun. 80:1304-1313. http://dx.doi.org/10.1128/IAI.06146-11.
    • (2012) Infect. Immun. , vol.80 , pp. 1304-1313
    • Cheng, S.C.1    Joosten, L.A.2    Kullberg, B.J.3    Netea, M.G.4
  • 2
    • 4143119933 scopus 로고    scopus 로고
    • From commensal to pathogen: Stage- and tissue-specific gene expression of Candida albicans
    • Hube B. 2004. From commensal to pathogen: stage- and tissue-specific gene expression of Candida albicans. Curr. Opin. Microbiol. 7:336-341. http://dx.doi.org/10.1016/j.mib.2004.06.003.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 336-341
    • Hube, B.1
  • 3
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • Vandamme D, Landuyt B, Luyten W, Schoofs L. 2012. A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell. Immunol. 280:22-35. http://dx.doi.org/10.1016/j.cellimm.2012.11.009.
    • (2012) Cell. Immunol. , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 4
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer RI, Ganz T. 1999. Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11:23-27. http://dx.doi.org/10. 1016/S0952-7915(99)80005-3.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 5
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel A, Sahl HG. 2006. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4:529-536. http://dx.doi.org/10.1038/nrmicro1441.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 7
    • 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. http://dx.doi.org/10.1007/s11302 -006-9040-0.
    • (2007) Purinergic Signal , vol.3 , pp. 91-97
    • Vylkova, S.1    Sun, J.N.2    Edgerton, M.3
  • 8
    • 79251599753 scopus 로고    scopus 로고
    • Host defense peptides and their antimicrobial-immunomodulatory duality
    • Steinstraesser L, Kraneburg U, Jacobsen F, Al-Benna S. 2011. Host defense peptides and their antimicrobial-immunomodulatory duality. Immunobiology 216:322-333. http://dx.doi.org/10.1016/j.imbio.2010.07. 003.
    • (2011) Immunobiology , vol.216 , pp. 322-333
    • Steinstraesser, L.1    Kraneburg, U.2    Jacobsen, F.3    Al-Benna, S.4
  • 9
    • 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, Veerman EC, Nieuw Amerongen AV. 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. http://dx.doi.org/10.1042/BJ20042099.
    • (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    Veerman, E.C.6    Nieuw Amerongen, A.V.7
  • 10
    • 84862967447 scopus 로고    scopus 로고
    • LL37 and hBD-3 elevate the beta-1,3-exoglucanase activity of Candida albicans Xog1p, resulting in reduced fungal adhesion to plastic
    • Chang HT, Tsai PW, Huang HH, Liu YS, Chien TS, Lan CY. 2012. LL37 and hBD-3 elevate the beta-1,3-exoglucanase activity of Candida albicans Xog1p, resulting in reduced fungal adhesion to plastic. Biochem. J. 441: 963-970. http://dx.doi.org/10.1042/BJ20111454.
    • (2012) Biochem. J. , vol.441 , pp. 963-970
    • Chang, H.T.1    Tsai, P.W.2    Huang, H.H.3    Liu, Y.S.4    Chien, T.S.5    Lan, C.Y.6
  • 11
    • 79952679401 scopus 로고    scopus 로고
    • Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates
    • Tsai PW, Yang CY, Chang HT, Lan CY. 2011. Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates. PLoS One 6:e17755. http://dx.doi.org/10. 1371/journal.pone.0017755.
    • (2011) PLoS One , vol.6
    • Tsai, P.W.1    Yang, C.Y.2    Chang, H.T.3    Lan, C.Y.4
  • 12
    • 1342282224 scopus 로고    scopus 로고
    • Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL. 2004. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J. Immunol. 172:3070-3077. http://dx.doi. org/10.4049/jimmunol.172.5.3070.
    • (2004) J. Immunol. , vol.172 , pp. 3070-3077
    • Murakami, M.1    Lopez-Garcia, B.2    Braff, M.3    Dorschner, R.A.4    Gallo, R.L.5
  • 14
    • 79955433491 scopus 로고    scopus 로고
    • Influence of histatin 5 on Candida albicans mitochondrial protein expression assessed by quantitative mass spectrometry
    • Komatsu T, Salih E, Helmerhorst EJ, Offner GD, Oppenheim FG. 2011. Influence of histatin 5 on Candida albicans mitochondrial protein expression assessed by quantitative mass spectrometry. J. Proteome Res. 10:646- 655. http://dx.doi.org/10.1021/pr100861k.
    • (2011) J. Proteome Res. , vol.10 , pp. 646-655
    • Komatsu, T.1    Salih, E.2    Helmerhorst, E.J.3    Offner, G.D.4    Oppenheim, F.G.5
  • 15
    • 55549117176 scopus 로고    scopus 로고
    • Uptake of the antifungal cationic peptide histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain
    • Sun JN, Li W, Jang WS, Nayyar N, Sutton MD, Edgerton M. 2008. Uptake of the antifungal cationic peptide histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain. Mol. Microbiol. 70:1246-1260. http://dx.doi.org/10.1111/j.1365 -2958.2008.06480.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1246-1260
    • Sun, J.N.1    Li, W.2    Jang, W.S.3    Nayyar, N.4    Sutton, M.D.5    Edgerton, M.6
  • 16
    • 83755171493 scopus 로고    scopus 로고
    • Histatin 5 uptake by Candida albicans utilizes polyamine transporters Dur3 and Dur31 proteins
    • Kumar R, Chadha S, Saraswat D, Bajwa JS, Li RA, Conti HR, Edgerton M. 2011. Histatin 5 uptake by Candida albicans utilizes polyamine transporters Dur3 and Dur31 proteins. J. Biol. Chem. 286:43748-43758. http: //dx.doi.org/10.1074/jbc.M111.311175.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43748-43758
    • Kumar, R.1    Chadha, S.2    Saraswat, D.3    Bajwa, J.S.4    Li, R.A.5    Conti, H.R.6    Edgerton, M.7
  • 17
    • 84861205386 scopus 로고    scopus 로고
    • The novel Candida albicans transporter Dur31 is a multi-stage pathogenicity factor
    • Mayer FL, Wilson D, Jacobsen ID, Miramon P, Grosse K, Hube B. 2012. The novel Candida albicans transporter Dur31 is a multi-stage pathogenicity factor. PLoS Pathog. 8:e1002592. http://dx.doi.org/10.1371 /journal.ppat.1002592.
    • (2012) PLoS Pathog. , vol.8
    • Mayer, F.L.1    Wilson, D.2    Jacobsen, I.D.3    Miramon, P.4    Grosse, K.5    Hube, B.6
  • 18
    • 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. http://dx.doi.org/10.1073/pnas.141366998.
    • (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
  • 19
    • 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. http://dx.doi.org/10. 1128/IAI.68.12.6848-6856.2000.
    • (2000) Infect. Immun. , vol.68 , pp. 6848-6856
    • Koshlukova, S.E.1    Araujo, M.W.2    Baev, D.3    Edgerton, M.4
  • 20
    • 84907463396 scopus 로고    scopus 로고
    • How does it kill?: Understanding the candidacidal mechanism of salivary histatin 5
    • Puri S, Edgerton M. 2014. How does it kill?: understanding the candidacidal mechanism of salivary histatin 5. Eukaryot. Cell 13:958-964.
    • (2014) Eukaryot. Cell , vol.13 , pp. 958-964
    • Puri, S.1    Edgerton, M.2
  • 21
    • 0034425535 scopus 로고    scopus 로고
    • Salivary histatin 5 and human neutrophil defensin 1 kill Candida albicans via shared pathways
    • Edgerton M, Koshlukova SE, Araujo MW, Patel RC, Dong J, Bruenn JA. 2000. Salivary histatin 5 and human neutrophil defensin 1 kill Candida albicans via shared pathways. Antimicrob. Agents Chemother. 44:3310- 3316. http://dx.doi.org/10.1128/AAC.44.12.3310-3316.2000.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3310-3316
    • Edgerton, M.1    Koshlukova, S.E.2    Araujo, M.W.3    Patel, R.C.4    Dong, J.5    Bruenn, J.A.6
  • 22
    • 59749096989 scopus 로고    scopus 로고
    • Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3
    • Krishnakumari V, Rangaraj N, Nagaraj R. 2009. Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3. Antimicrob. Agents Chemother. 53:256-260. http://dx.doi. org/10.1128/AAC.00470-08.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 256-260
    • Krishnakumari, V.1    Rangaraj, N.2    Nagaraj, R.3
  • 23
    • 0141919277 scopus 로고    scopus 로고
    • Human salivary MUC7 mucin peptides: Effect of size, charge and cysteine residues on antifungal activity
    • Situ H, Wei G, Smith CJ, Mashhoon S, Bobek LA. 2003. Human salivary MUC7 mucin peptides: effect of size, charge and cysteine residues on antifungal activity. Biochem. J. 375:175-182. http://dx.doi.org/10.1042 /BJ20030779.
    • (2003) Biochem. J. , vol.375 , pp. 175-182
    • Situ, H.1    Wei, G.2    Smith, C.J.3    Mashhoon, S.4    Bobek, L.A.5
  • 24
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder J, Schroder JM. 2002. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277:46779- 46784. http://dx.doi.org/10.1074/jbc.M207587200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46779-46784
    • Harder, J.1    Schroder, J.M.2
  • 25
    • 70349745535 scopus 로고    scopus 로고
    • Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7
    • Abtin A, Eckhart L, Mildner M, Ghannadan M, Harder J, Schroder JM, Tschachler E. 2009. Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7. J. Investig. Dermatol. 129:2193-2201. http://dx.doi. org/10.1038/jid.2009.35.
    • (2009) J. Investig. Dermatol. , vol.129 , pp. 2193-2201
    • Abtin, A.1    Eckhart, L.2    Mildner, M.3    Ghannadan, M.4    Harder, J.5    Schroder, J.M.6    Tschachler, E.7
  • 27
    • 84861371938 scopus 로고    scopus 로고
    • Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans
    • Bolscher J, Nazmi K, van Marle J, van't Hof W, Veerman E. 2012. Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans. Biochem. Cell Biol. 90:378-388. http://dx.doi.org/10.1139/o11-085.
    • (2012) Biochem. Cell Biol. , vol.90 , pp. 378-388
    • Bolscher, J.1    Nazmi, K.2    van Marle, J.3    van't Hof, W.4    Veerman, E.5
  • 30
    • 84866290009 scopus 로고    scopus 로고
    • Natural antimicrobial peptides from bacteria: Characteristics and potential applications to fight against antibiotic resistance
    • Hassan M, Kjos M, Nes IF, Diep DB, Lotfipour F. 2012. Natural antimicrobial peptides from bacteria: characteristics and potential applications to fight against antibiotic resistance. J. Appl. Microbiol. 113:723- 736. http://dx.doi.org/10.1111/j.1365-2672.2012.05338.x.
    • (2012) J. Appl. Microbiol. , vol.113 , pp. 723-736
    • Hassan, M.1    Kjos, M.2    Nes, I.F.3    Diep, D.B.4    Lotfipour, F.5
  • 31
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted ME, Ouellette AJ. 2005. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6:551-557. http://dx.doi.org/10. 1038/ni1206.
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 32
    • 66949176665 scopus 로고    scopus 로고
    • Candida albicans phospholipomannan triggers inflammatory responses of human keratinocytes through Toll-like receptor 2
    • Li M, Chen Q, Shen Y, Liu W. 2009. Candida albicans phospholipomannan triggers inflammatory responses of human keratinocytes through Toll-like receptor 2. Exp. Dermatol. 18:603-610. http://dx.doi.org/10. 1111/j.1600-0625.2008.00832.x.
    • (2009) Exp. Dermatol. , vol.18 , pp. 603-610
    • Li, M.1    Chen, Q.2    Shen, Y.3    Liu, W.4
  • 35
    • 4143095716 scopus 로고    scopus 로고
    • IL-22 increases the innate immunity of tissues
    • Wolk K, Kunz S, Witte E, Friedrich M, Asadullah K, Sabat R. 2004. IL-22 increases the innate immunity of tissues. Immunity 21:241-254. http://dx.doi.org/10.1016/j.immuni.2004.07.007.
    • (2004) Immunity , vol.21 , pp. 241-254
    • Wolk, K.1    Kunz, S.2    Witte, E.3    Friedrich, M.4    Asadullah, K.5    Sabat, R.6
  • 36
    • 4344688669 scopus 로고    scopus 로고
    • IL-17 markedly up-regulates beta-defensin-2 expression in human airway epithelium via JAK and NF-kappaB signaling pathways
    • Kao CY, Chen Y, Thai P, Wachi S, Huang F, Kim C, Harper RW, Wu R. 2004. IL-17 markedly up-regulates beta-defensin-2 expression in human airway epithelium via JAK and NF-kappaB signaling pathways. J. Immunol. 173:3482-3491. http://dx.doi.org/10.4049/jimmunol.173.5.3482.
    • (2004) J. Immunol. , vol.173 , pp. 3482-3491
    • Kao, C.Y.1    Chen, Y.2    Thai, P.3    Wachi, S.4    Huang, F.5    Kim, C.6    Harper, R.W.7    Wu, R.8
  • 37
    • 77951652390 scopus 로고    scopus 로고
    • Lessons from the inflammasome: A molecular sentry linking Candida and Crohn's disease
    • Rehaume LM, Jouault T, Chamaillard M. 2010. Lessons from the inflammasome: a molecular sentry linking Candida and Crohn's disease. Trends Immunol. 31:171-175. http://dx.doi.org/10.1016/j.it.2010.01.007.
    • (2010) Trends Immunol. , vol.31 , pp. 171-175
    • Rehaume, L.M.1    Jouault, T.2    Chamaillard, M.3
  • 38
    • 33747339180 scopus 로고    scopus 로고
    • Hyphal invasion of Candida albicans inhibits the expression of human beta-defensins in experimental oral candidiasis
    • Lu Q, Jayatilake JA, Samaranayake LP, Jin L. 2006. Hyphal invasion of Candida albicans inhibits the expression of human beta-defensins in experimental oral candidiasis. J. Investig. Dermatol. 126:2049-2056. http: //dx.doi.org/10.1038/sj.jid.5700346.
    • (2006) J. Investig. Dermatol. , vol.126 , pp. 2049-2056
    • Lu, Q.1    Jayatilake, J.A.2    Samaranayake, L.P.3    Jin, L.4
  • 40
    • 0036890119 scopus 로고    scopus 로고
    • Expression of functional Toll-like receptor 2 on human epidermal keratinocytes
    • Kawai K, Shimura H, Minagawa M, Ito A, Tomiyama K, Ito M. 2002. Expression of functional Toll-like receptor 2 on human epidermal keratinocytes. J. Dermatol. Sci. 30:185-194. http://dx.doi.org/10.1016/S0923 -1811(02)00105-6.
    • (2002) J. Dermatol. Sci. , vol.30 , pp. 185-194
    • Kawai, K.1    Shimura, H.2    Minagawa, M.3    Ito, A.4    Tomiyama, K.5    Ito, M.6
  • 42
    • 80053134897 scopus 로고    scopus 로고
    • New insights into cathelicidin modulation of adaptive immunity
    • Wuerth K, Hancock RE. 2011. New insights into cathelicidin modulation of adaptive immunity. Eur. J. Immunol. 41:2817-2819. http://dx.doi.org /10.1002/eji.201142055.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 2817-2819
    • Wuerth, K.1    Hancock, R.E.2
  • 43
    • 84870242845 scopus 로고    scopus 로고
    • Regulation of antimicrobial peptide gene expression by nutrients and by-products of microbial metabolism
    • Campbell Y, Fantacone ML, Gombart AF. 2012. Regulation of antimicrobial peptide gene expression by nutrients and by-products of microbial metabolism. Eur. J. Nutr. 51:899-907. http://dx.doi.org/10.1007/s00394 -012-0415-4.
    • (2012) Eur. J. Nutr. , vol.51 , pp. 899-907
    • Campbell, Y.1    Fantacone, M.L.2    Gombart, A.F.3
  • 44
    • 67650069160 scopus 로고    scopus 로고
    • The expression of the beta-defensins hBD-2 and hBD-3 is differentially regulated by NF-kappaB and MAPK/AP-1 pathways in an in vitro model of Candida esophagitis
    • Steubesand N, Kiehne K, Brunke G, Pahl R, Reiss K, Herzig KH, Schubert S, Schreiber S, Folsch UR, Rosenstiel P, Arlt A. 2009. The expression of the beta-defensins hBD-2 and hBD-3 is differentially regulated by NF-kappaB and MAPK/AP-1 pathways in an in vitro model of Candida esophagitis. BMC Immunol. 10:36. http://dx.doi.org/10.1186 /1471-2172-10-36.
    • (2009) BMC Immunol. , vol.10 , pp. 36
    • Steubesand, N.1    Kiehne, K.2    Brunke, G.3    Pahl, R.4    Reiss, K.5    Herzig, K.H.6    Schubert, S.7    Schreiber, S.8    Folsch, U.R.9    Rosenstiel, P.10    Arlt, A.11
  • 45
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen O, Arnljots K, Cowland JB, Bainton DF, Borregaard N. 1997. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90:2796-2803.
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 47
    • 34447525439 scopus 로고    scopus 로고
    • Beneficial suicide: Why neutrophils die to make NETs
    • Brinkmann V, Zychlinsky A. 2007. Beneficial suicide: why neutrophils die to make NETs. Nat. Rev. Microbiol. 5:577-582. http://dx.doi.org/10. 1038/nrmicro1710.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 577-582
    • Brinkmann, V.1    Zychlinsky, A.2
  • 48
    • 79960829290 scopus 로고    scopus 로고
    • Neutrophils in the activation and regulation of innate and adaptive immunity
    • Mantovani A, Cassatella MA, Costantini C, Jaillon S. 2011. Neutrophils in the activation and regulation of innate and adaptive immunity. Nat. Rev. Immunol. 11:519-531. http://dx.doi.org/10.1038/nri3024.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 519-531
    • Mantovani, A.1    Cassatella, M.A.2    Costantini, C.3    Jaillon, S.4
  • 49
    • 0019993528 scopus 로고
    • Skin sensitization by misonidazole: A demonstration of uniform mild hypoxia
    • Stewart FA, Denekamp J, Randhawa VS. 1982. Skin sensitization by misonidazole: a demonstration of uniform mild hypoxia. Br. J. Cancer 45:869-877. http://dx.doi.org/10.1038/bjc.1982.139.
    • (1982) Br. J. Cancer , vol.45 , pp. 869-877
    • Stewart, F.A.1    Denekamp, J.2    Randhawa, V.S.3
  • 51
    • 79952193858 scopus 로고    scopus 로고
    • The antimycotic drugs itraconazole and terbinafine hydrochloride induce the production of human beta-defensin-3 in human keratinocytes
    • Kanda N, Kano R, Ishikawa T, Watanabe S. 2011. The antimycotic drugs itraconazole and terbinafine hydrochloride induce the production of human beta-defensin-3 in human keratinocytes. Immunobiology 216:497- 504. http://dx.doi.org/10.1016/j.imbio.2010.08.008.
    • (2011) Immunobiology , vol.216 , pp. 497-504
    • Kanda, N.1    Kano, R.2    Ishikawa, T.3    Watanabe, S.4
  • 52
    • 0037930850 scopus 로고    scopus 로고
    • SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides
    • Frick IM, Åkesson P, Rasmussen M, Schmidtchen A, Björck L. 2003. SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J. Biol. Chem. 278:16561-16566. http://dx.doi.org/10.1074 /jbc.M301995200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16561-16566
    • Frick, I.M.1    Åkesson, P.2    Rasmussen, M.3    Schmidtchen, A.4    Björck, L.5
  • 53
    • 64549125592 scopus 로고    scopus 로고
    • A novel immune evasion strategy of Candida albicans: Proteolytic cleavage of a salivary antimicrobial peptide
    • Meiller TF, Hube B, Schild L, Shirtliff ME, Scheper MA, Winkler R, Ton A, Jabra-Rizk MA. 2009. A novel immune evasion strategy of Candida albicans: proteolytic cleavage of a salivary antimicrobial peptide. PLoS One 4:e5039. http://dx.doi.org/10.1371/journal.pone.0005039.
    • (2009) PLoS One , vol.4
    • Meiller, T.F.1    Hube, B.2    Schild, L.3    Shirtliff, M.E.4    Scheper, M.A.5    Winkler, R.6    Ton, A.7    Jabra-Rizk, M.A.8
  • 54
    • 84880269447 scopus 로고    scopus 로고
    • Candida albicans mucin Msb2 is a broad-range protectant against antimicrobial peptides
    • Swidergall M, Ernst AM, Ernst JF. 2013. Candida albicans mucin Msb2 is a broad-range protectant against antimicrobial peptides. Antimicrob. Agents Chemother. 57:3917-3922. http://dx.doi.org/10.1128/AAC.00862 -13.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 3917-3922
    • Swidergall, M.1    Ernst, A.M.2    Ernst, J.F.3
  • 56
    • 79951479272 scopus 로고    scopus 로고
    • Interaction between the Candida albicans high-osmolarity glycerol (HOG) pathway and the response to human beta-defensins 2 and 3
    • Argimon S, Fanning S, Blankenship JR, Mitchell AP. 2011. Interaction between the Candida albicans high-osmolarity glycerol (HOG) pathway and the response to human beta-defensins 2 and 3. Eukaryot. Cell 10:272- 275. http://dx.doi.org/10.1128/EC.00133-10.
    • (2011) Eukaryot. Cell , vol.10 , pp. 272-275
    • Argimon, S.1    Fanning, S.2    Blankenship, J.R.3    Mitchell, A.P.4
  • 57
    • 84874522648 scopus 로고    scopus 로고
    • Bcr1 functions downstream of Ssd1 to mediate antimicrobial peptide resistance in Candida albicans
    • Jung SI, Finkel JS, Solis NV, Chaili S, Mitchell AP, Yeaman MR, Filler SG. 2013. Bcr1 functions downstream of Ssd1 to mediate antimicrobial peptide resistance in Candida albicans. Eukaryot. Cell 12:411-419. http: //dx.doi.org/10.1128/EC.00285-12.
    • (2013) Eukaryot. Cell , vol.12 , pp. 411-419
    • Jung, S.I.1    Finkel, J.S.2    Solis, N.V.3    Chaili, S.4    Mitchell, A.P.5    Yeaman, M.R.6    Filler, S.G.7
  • 58
    • 77954521548 scopus 로고    scopus 로고
    • Antimicrobial peptide MUC7 12-mer activates the calcium/calcineurin pathway in Candida albicans
    • Lis M, Liu TT, Barker KS, Rogers PD, Bobek LA. 2010. Antimicrobial peptide MUC7 12-mer activates the calcium/calcineurin pathway in Candida albicans. FEMS Yeast Res. 10:579-586.
    • (2010) FEMS Yeast Res. , vol.10 , pp. 579-586
    • Lis, M.1    Liu, T.T.2    Barker, K.S.3    Rogers, P.D.4    Bobek, L.A.5
  • 59
    • 84872050716 scopus 로고    scopus 로고
    • Secreted aspartic protease cleavage of Candida albicans Msb2 activates Cek1 MAPK signaling affecting biofilm formation and oropharyngeal candidiasis
    • Author Correction, 8:10.1371/annotation /13ef5e14-c192-4bb2-af91-886024500b4b, 2013. http://dx.doi.org/10. 1371/annotation/13ef5e14-c192-4bb2-af91-886024500b4b
    • Puri S, Kumar R, Chadha S, Tati S, Conti HR, Hube B, Cullen PJ, Edgerton M. 2012. Secreted aspartic protease cleavage of Candida albicans Msb2 activates Cek1 MAPK signaling affecting biofilm formation and oropharyngeal candidiasis. PLoS One 7:e46020. http://dx.doi.org/10. 1371/journal.pone.0046020. (Author Correction, 8:10.1371/annotation /13ef5e14-c192-4bb2-af91-886024500b4b, 2013. http://dx.doi.org/10. 1371/annotation/13ef5e14-c192-4bb2-af91-886024500b4b.)
    • (2012) PLoS One , vol.7
    • Puri, S.1    Kumar, R.2    Chadha, S.3    Tati, S.4    Conti, H.R.5    Hube, B.6    Cullen, P.J.7    Edgerton, M.8
  • 60
    • 84875199113 scopus 로고    scopus 로고
    • Candida albicans Flu1-mediated efflux of salivary histatin 5 reduces its cytosolic concentration and fungicidal activity
    • Li R, Kumar R, Tati S, Puri S, Edgerton M. 2013. Candida albicans Flu1-mediated efflux of salivary histatin 5 reduces its cytosolic concentration and fungicidal activity. Antimicrob. Agents Chemother. 57:1832- 1839. http://dx.doi.org/10.1128/AAC.02295-12.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 1832-1839
    • Li, R.1    Kumar, R.2    Tati, S.3    Puri, S.4    Edgerton, M.5
  • 61
    • 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. http://dx.doi.org/10.1128/EC.00039-07.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1876-1888
    • Vylkova, S.1    Jang, W.S.2    Li, W.3    Nayyar, N.4    Edgerton, M.5
  • 62
    • 84880318184 scopus 로고    scopus 로고
    • Identification and mechanism of action of the plant defensin NaD1 as a new member of the antifungal drug arsenal against Candida albicans
    • Hayes BM, Bleackley MR, Wiltshire JL, Anderson MA, Traven A, van der Weerden NL. 2013. Identification and mechanism of action of the plant defensin NaD1 as a new member of the antifungal drug arsenal against Candida albicans. Antimicrob. Agents Chemother. 57:3667-3675. http://dx.doi.org/10.1128/AAC.00365-13.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 3667-3675
    • Hayes, B.M.1    Bleackley, M.R.2    Wiltshire, J.L.3    Anderson, M.A.4    Traven, A.5    van der Weerden, N.L.6
  • 63
    • 62249094620 scopus 로고    scopus 로고
    • The Hog1 MAP kinase controls respiratory metabolism in the fungal pathogen Candida albicans
    • Alonso-Monge R, Carvaihlo S, Nombela C, Rial E, Pla J. 2009. The Hog1 MAP kinase controls respiratory metabolism in the fungal pathogen Candida albicans. Microbiology 155:413-423. http://dx.doi.org/10.1099/mic. 0.023309-0.
    • (2009) Microbiology , vol.155 , pp. 413-423
    • Alonso-Monge, R.1    Carvaihlo, S.2    Nombela, C.3    Rial, E.4    Pla, J.5
  • 67
    • 0038016755 scopus 로고    scopus 로고
    • Calcineurin A of Candida albicans: Involvement in antifungal tolerance, cell morphogenesis and virulence
    • Sanglard D, Ischer F, Marchetti O, Entenza J, Bille J. 2003. Calcineurin A of Candida albicans: involvement in antifungal tolerance, cell morphogenesis and virulence. Mol. Microbiol. 48:959-976. http://dx.doi.org/10. 1046/j.1365-2958.2003.03495.x.
    • (2003) Mol. Microbiol. , vol.48 , pp. 959-976
    • Sanglard, D.1    Ischer, F.2    Marchetti, O.3    Entenza, J.4    Bille, J.5
  • 68
    • 66149141488 scopus 로고    scopus 로고
    • Dissection of the Candida albicans class I chitin synthase promoters
    • Lenardon MD, Lesiak I, Munro CA, Gow NA. 2009. Dissection of the Candida albicans class I chitin synthase promoters. Mol. Genet. Genomics 281:459-471. http://dx.doi.org/10.1007/s00438-009-0423-0.
    • (2009) Mol. Genet. Genomics , vol.281 , pp. 459-471
    • Lenardon, M.D.1    Lesiak, I.2    Munro, C.A.3    Gow, N.A.4
  • 69
    • 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
  • 71
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395. http://dx.doi.org/10.1038/415389a.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 72
    • 70349173209 scopus 로고    scopus 로고
    • Susceptibility relationship between vancomycin and daptomycin in Staphylococcus aureus: Facts and assumptions
    • Moise PA, North D, Steenbergen JN, Sakoulas G. 2009. Susceptibility relationship between vancomycin and daptomycin in Staphylococcus aureus: facts and assumptions. Lancet Infect. Dis. 9:617-624. http://dx.doi. org/10.1016/S1473-3099(09)70200-2.
    • (2009) Lancet Infect. Dis. , vol.9 , pp. 617-624
    • Moise, P.A.1    North, D.2    Steenbergen, J.N.3    Sakoulas, G.4
  • 73
    • 70349099122 scopus 로고    scopus 로고
    • In vitro efficacy of nisin Z against Candida albicans adhesion and transition following contact with normal human gingival cells
    • Akerey B, Le-Lay C, Fliss I, Subirade M, Rouabhia M. 2009. In vitro efficacy of nisin Z against Candida albicans adhesion and transition following contact with normal human gingival cells. J. Appl. Microbiol. 107: 1298-1307. http://dx.doi.org/10.1111/j.1365-2672.2009.04312.x.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 1298-1307
    • Akerey, B.1    Le-Lay, C.2    Fliss, I.3    Subirade, M.4    Rouabhia, M.5
  • 74
    • 70349133953 scopus 로고    scopus 로고
    • Candida albicans and Staphylococcus aureus form polymicrobial biofilms: Effects on antimicrobial resistance
    • Harriott MM, Noverr MC. 2009. Candida albicans and Staphylococcus aureus form polymicrobial biofilms: effects on antimicrobial resistance. Antimicrob. Agents Chemother. 53:3914-3922. http://dx.doi.org/10. 1128/AAC.00657-09.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3914-3922
    • Harriott, M.M.1    Noverr, M.C.2
  • 75
    • 84887286022 scopus 로고    scopus 로고
    • Sensing of the microbial neighborhood by Candida albicans
    • Mallick EM, Bennett RJ. 2013. Sensing of the microbial neighborhood by Candida albicans. PLoS Pathog. 9:e1003661. http://dx.doi.org/10.1371 /journal.ppat.1003661.
    • (2013) PLoS Pathog. , vol.9
    • Mallick, E.M.1    Bennett, R.J.2
  • 76
    • 77956132510 scopus 로고    scopus 로고
    • Ability of Candida albicans mutants to induce Staphylococcus aureus vancomycin resistance during polymicrobial biofilm formation
    • Harriott MM, Noverr MC. 2010. Ability of Candida albicans mutants to induce Staphylococcus aureus vancomycin resistance during polymicrobial biofilm formation. Antimicrob. Agents Chemother. 54:3746-3755. http: //dx.doi.org/10.1128/AAC.00573-10.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 3746-3755
    • Harriott, M.M.1    Noverr, M.C.2
  • 77
    • 77954765564 scopus 로고    scopus 로고
    • Antifungals to treat Candida albicans
    • Moudgal V, Sobel J. 2010. Antifungals to treat Candida albicans. Expert Opin. Pharmacother. 11:2037-2048. http://dx.doi.org/10.1517/14656566. 2010.493875.
    • (2010) Expert Opin. Pharmacother. , vol.11 , pp. 2037-2048
    • Moudgal, V.1    Sobel, J.2
  • 78
    • 33746922380 scopus 로고    scopus 로고
    • Candida albicans and Candida glabrata clinical isolates exhibiting reduced echinocandin susceptibility
    • Katiyar S, Pfaller M, Edlind T. 2006. Candida albicans and Candida glabrata clinical isolates exhibiting reduced echinocandin susceptibility. Antimicrob. Agents Chemother. 50:2892-2894. http://dx.doi.org/10.1128 /AAC.00349-06.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 2892-2894
    • Katiyar, S.1    Pfaller, M.2    Edlind, T.3
  • 79
    • 0036488166 scopus 로고    scopus 로고
    • Resistance of Candida species to antifungal agents: Molecular mechanisms and clinical consequences
    • Sanglard D, Odds FC. 2002. Resistance of Candida species to antifungal agents: molecular mechanisms and clinical consequences. Lancet Infect. Dis. 2:73-85. http://dx.doi.org/10.1016/S1473-3099(02)00181-0.
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 73-85
    • Sanglard, D.1    Odds, F.C.2
  • 80
    • 70350708570 scopus 로고    scopus 로고
    • Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1- 11)
    • Velden WJ, van Iersel TM, Blijlevens NM, Donnelly JP. 2009. Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1- 11). BMC Med. 7:44. http://dx.doi.org/10.1186/1741-7015-7-44.
    • (2009) BMC Med. , vol.7 , pp. 44
    • Velden, W.J.1    van Iersel, T.M.2    Blijlevens, N.M.3    Donnelly, J.P.4
  • 81
    • 79952532377 scopus 로고    scopus 로고
    • Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: Effects of pH, salt and heating
    • Tokle T, McClements DJ. 2011. Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: effects of pH, salt and heating. Food Hydrocolloids 25:976-982. http://dx.doi.org/10.1016/j.foodhyd.2010.09. 012.
    • (2011) Food Hydrocolloids , vol.25 , pp. 976-982
    • Tokle, T.1    McClements, D.J.2
  • 82
    • 51149102074 scopus 로고    scopus 로고
    • Human recombinant lactoferrin acts synergistically with antimicrobials commonly used in neonatal practice against coagulase-negative staphylococci and Candida albicans causing neonatal sepsis
    • Venkatesh MP, Rong L. 2008. Human recombinant lactoferrin acts synergistically with antimicrobials commonly used in neonatal practice against coagulase-negative staphylococci and Candida albicans causing neonatal sepsis. J. Med. Microbiol. 57:1113-1121. http://dx.doi.org/10. 1099/jmm.0.2008/001263-0.
    • (2008) J. Med. Microbiol. , vol.57 , pp. 1113-1121
    • Venkatesh, M.P.1    Rong, L.2
  • 83
    • 84893474208 scopus 로고    scopus 로고
    • Histatin 5-spermidine conjugates have enhanced fungicidal activity and efficacy as a topical therapeutic for oral candidiasis
    • Tati S, Li R, Puri S, Kumar R, Davidow P, Edgerton M. 2014. Histatin 5-spermidine conjugates have enhanced fungicidal activity and efficacy as a topical therapeutic for oral candidiasis. Antimicrob. Agents Chemother. 58:756-766.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 756-766
    • Tati, S.1    Li, R.2    Puri, S.3    Kumar, R.4    Davidow, P.5    Edgerton, M.6
  • 84
    • 77950499848 scopus 로고    scopus 로고
    • Potential therapeutic application of host defense peptides
    • Zhang L, Falla TJ. 2010. Potential therapeutic application of host defense peptides. Methods Mol. Biol. 618:303-327. http://dx.doi.org/10.1007/978 -1-60761-594-1_19.
    • (2010) Methods Mol. Biol. , vol.618 , pp. 303-327
    • Zhang, L.1    Falla, T.J.2
  • 87
    • 84878765907 scopus 로고    scopus 로고
    • Rationally designed transmembrane peptide mimics of the multidrug transporter protein Cdr1 act as antagonists to selectively block drug efflux and chemosensitize azole-resistant clinical isolates of Candida albicans
    • Maurya IK, Thota CK, Verma SD, Sharma J, Rawal MK, Ravikumar B, Sen S, Chauhan N, Lynn AM, Chauhan VS, Prasad R. 2013. Rationally designed transmembrane peptide mimics of the multidrug transporter protein Cdr1 act as antagonists to selectively block drug efflux and chemosensitize azole-resistant clinical isolates of Candida albicans. J. Biol. Chem. 288:16775-16787. http://dx.doi.org/10.1074/jbc.M113.467159.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16775-16787
    • Maurya, I.K.1    Thota, C.K.2    Verma, S.D.3    Sharma, J.4    Rawal, M.K.5    Ravikumar, B.6    Sen, S.7    Chauhan, N.8    Lynn, A.M.9    Chauhan, V.S.10    Prasad, R.11
  • 88
    • 77954352198 scopus 로고    scopus 로고
    • Salivary histatin 5 internalization by translocation, but not endocytosis, is required for fungicidal activity in Candida albicans
    • Jang WS, Bajwa JS, Sun JN, Edgerton M. 2010. Salivary histatin 5 internalization by translocation, but not endocytosis, is required for fungicidal activity in Candida albicans. Mol. Microbiol. 77:354-370. http://dx. doi.org/10.1111/j.1365-2958.2010.07210.x.
    • (2010) Mol. Microbiol. , vol.77 , pp. 354-370
    • Jang, W.S.1    Bajwa, J.S.2    Sun, J.N.3    Edgerton, M.4
  • 89
    • 0034585802 scopus 로고    scopus 로고
    • Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva
    • Edgerton M, Koshlukova SE. 2000. Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva. Adv. Dent. Res. 14: 16-21. http://dx.doi.org/10.1177/08959374000140010201.
    • (2000) Adv. Dent. Res. , vol.14 , pp. 16-21
    • Edgerton, M.1    Koshlukova, S.E.2
  • 90
    • 55849141654 scopus 로고    scopus 로고
    • Human lactoferrin induces apoptosis-like cell death in Candida albicans: Critical role of K+-channelmediated K+ efflux
    • Andres MT, Viejo-Diaz M, Fierro JF. 2008. Human lactoferrin induces apoptosis-like cell death in Candida albicans: critical role of K+-channelmediated K+ efflux. Antimicrob. Agents Chemother. 52:4081-4088. http://dx.doi.org/10.1128/AAC.01597-07.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 4081-4088
    • Andres, M.T.1    Viejo-Diaz, M.2    Fierro, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.