메뉴 건너뛰기




Volumn 10, Issue 1, 2011, Pages 98-109

Proteolytic cleavage of covalently linked cell wall proteins by Candida albicans Sap9 and Sap10

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; CHITINASE; FUNGAL PROTEIN; PEPSTATIN; PROTEOME; RECOMBINANT PROTEIN; SAP9 PROTEIN, CANDIDA ALBICANS;

EID: 78651507997     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00210-10     Document Type: Article
Times cited : (83)

References (73)
  • 1
    • 33644861572 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions
    • Albrecht, A., et al. 2006. Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions. J. Biol. Chem. 281:688-694.
    • (2006) J. Biol. Chem , vol.281 , pp. 688-694
    • Albrecht, A.1
  • 2
    • 0041530198 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of the association and dissociation of inhibitors interacting with secreted aspartic acid proteases 1 and 2 from Candida albicans
    • Backman, D., and U. H. Danielson. 2003. Kinetic and mechanistic analysis of the association and dissociation of inhibitors interacting with secreted aspartic acid proteases 1 and 2 from Candida albicans. Biochim. Biophys. Acta 1646:184-195.
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 184-195
    • Backman, D.1    Danielson, U.H.2
  • 3
    • 49649111234 scopus 로고    scopus 로고
    • Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris
    • Bader, O., Y. Krauke, and B. Hube. 2008. Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris. BMC Microbiol. 8:116.
    • (2008) BMC Microbiol , vol.8 , pp. 116
    • Bader, O.1    Krauke, Y.2    Hube, B.3
  • 4
    • 0031971193 scopus 로고    scopus 로고
    • The expression of the secreted aspartyl proteinases Sap4 to Sap6 from Candida albicans in murine macrophages
    • Borg-von Zepelin, M., S. Beggah, K. Boggian, D. Sanglard, and M. Monod. 1998. The expression of the secreted aspartyl proteinases Sap4 to Sap6 from Candida albicans in murine macrophages. Mol. Microbiol. 28:543-554.
    • (1998) Mol. Microbiol , vol.28 , pp. 543-554
    • Borg-Von, Z.M.1    Beggah, S.2    Boggian, K.3    Sanglard, D.4    Monod, M.5
  • 5
    • 4143129869 scopus 로고    scopus 로고
    • Ectopic expression of URA3 can influence the virulence phenotypes and proteome of Candida albicans but can be overcome by targeted reintegration of URA3 at the RPS10 locus
    • Brand, A., D. M. MacCallum, A. J. Brown, N. A. Gow, and F. C. Odds. 2004. Ectopic expression of URA3 can influence the virulence phenotypes and proteome of Candida albicans but can be overcome by targeted reintegration of URA3 at the RPS10 locus. Eukaryot. Cell 3:900-909.
    • (2004) Eukaryot. Cell , vol.3 , pp. 900-909
    • Brand, A.1    Maccallum, D.M.2    Brown, A.J.3    Gow, N.A.4    Odds, F.C.5
  • 6
    • 0033828719 scopus 로고    scopus 로고
    • Identification and characterization of TUP1-regulated genes in Candida albicans
    • Braun, B. R., W. S. Head, M. X. Wang, and A. D. Johnson. 2000. Identification and characterization of TUP1-regulated genes in Candida albicans. Genetics 156:31-44.
    • (2000) Genetics , vol.156 , pp. 31-44
    • Braun, B.R.1    Head, W.S.2    Wang, M.X.3    Johnson, A.D.4
  • 7
    • 0035399946 scopus 로고    scopus 로고
    • Virulence factors of Candida albicans
    • Calderone, R. A., and W. A. Fonzi. 2001. Virulence factors of Candida albicans. Trends Microbiol. 9:327-335.
    • (2001) Trends Microbiol , vol.9 , pp. 327-335
    • Calderone, R.A.1    Fonzi, W.A.2
  • 8
    • 53549117486 scopus 로고    scopus 로고
    • A study of the Candida albicans cell wall proteome
    • Castillo, L., et al. 2008. A study of the Candida albicans cell wall proteome. Proteomics 8:3871-3881.
    • (2008) Proteomics , vol.8 , pp. 3871-3881
    • Castillo, L.1
  • 9
    • 32444438298 scopus 로고    scopus 로고
    • Genomic response programs of Candida albicans following protoplasting and regeneration
    • Castillo, L., et al. 2006. Genomic response programs of Candida albicans following protoplasting and regeneration. Fungal Genet. Biol. 43:124-134.
    • (2006) Fungal Genet. Biol , vol.43 , pp. 124-134
    • Castillo, L.1
  • 10
    • 0037458676 scopus 로고    scopus 로고
    • Synthesis and characterization of the first potent inhibitor of yapsin 1. Implications for the study of yapsin-like enzymes
    • Cawley, N. X., et al. 2003. Synthesis and characterization of the first potent inhibitor of yapsin 1. Implications for the study of yapsin-like enzymes. J. Biol. Chem. 278:5523-5530.
    • (2003) J. Biol. Chem , vol.278 , pp. 5523-5530
    • Cawley, N.X.1
  • 11
    • 51949116049 scopus 로고    scopus 로고
    • Candida albicans cell wall proteins
    • Chaffin, W. L. 2008. Candida albicans cell wall proteins. Microbiol. Mol. Biol. Rev. 72:495-544.
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 495-544
    • Chaffin, W.L.1
  • 12
    • 18844462400 scopus 로고    scopus 로고
    • Exposure of Candida albicans to antifungal agents affects expression of SAP2 and SAP9 secreted proteinase genes
    • Copping, V. M., et al. 2005. Exposure of Candida albicans to antifungal agents affects expression of SAP2 and SAP9 secreted proteinase genes. J. Antimicrob. Chemother. 55:645-654.
    • (2005) J. Antimicrob. Chemother , vol.55 , pp. 645-654
    • Copping, V.M.1
  • 13
    • 0029645880 scopus 로고
    • The crystal structure of a major secreted aspartic roteinase from Candida albicans in complexes with two inhibitors
    • Cutfield, S. M., et al. 1995. The crystal structure of a major secreted aspartic roteinase from Candida albicans in complexes with two inhibitors. Structure: 1261-1271.
    • (1995) Structure , pp. 1261-1271
    • Cutfield, S.M.1
  • 14
    • 77956827211 scopus 로고    scopus 로고
    • The Candida albicans cell wall protein Rhd3/Pga29 is abundant in the yeast form and contributes to virulence
    • de Boer, A. D., et al. 2010. The Candida albicans cell wall protein Rhd3/Pga29 is abundant in the yeast form and contributes to virulence. Yeast 7:611-624.
    • (2010) Yeast , vol.7 , pp. 611-624
    • de Boer, A.D.1
  • 15
    • 4143087024 scopus 로고    scopus 로고
    • Proteomic analysis of Candida albicans cell alls reveals covalently bound carbohydrate-active enzymes and adhesins
    • de Groot, P. W. J., et al. 2004. Proteomic analysis of Candida albicans cell alls reveals covalently bound carbohydrate-active enzymes and adhesins. Eukaryot. Cell 3:955-965.
    • (2004) Eukaryot. Cell , vol.3 , pp. 955-965
    • de Groot, P.W.J.1
  • 17
    • 27544509874 scopus 로고    scopus 로고
    • Candida lbicans CHT3 encodes the functional homolog of the Cts1 chitinase of accharomyces cerevisiae
    • Dünkler, A., A. Walther, C. A. Specht, and J. Wendland. 2005. Candida lbicans CHT3 encodes the functional homolog of the Cts1 chitinase of accharomyces cerevisiae. Fungal Genet. Biol. 42:935-947.
    • (2005) Fungal Genet. Biol , vol.42 , pp. 935-947
    • Dünkler, A.1    Walther, A.2    Specht, C.A.3    Wendland, J.4
  • 18
    • 33744962003 scopus 로고    scopus 로고
    • Pir roteins of Saccharomyces cerevisiae are attached to beta-1,3-glucan by a new rotein-carbohydrate linkage
    • Ecker, M., R. Deutzmann, L. Lehle, V. Mrsa, and W. Tanner. 2006. Pir roteins of Saccharomyces cerevisiae are attached to beta-1,3-glucan by a new rotein-carbohydrate linkage. J. Biol. Chem. 281:11523-11529.
    • (2006) J. Biol. Chem , vol.281 , pp. 11523-11529
    • Ecker, M.1    Deutzmann, R.2    Lehle, L.3    Mrsa, V.4    Tanner, W.5
  • 19
    • 0027192868 scopus 로고
    • Isogenic strain construction and gene apping in Candida albicans
    • Fonzi, W. A., and M. Y. Irwin. 1993. Isogenic strain construction and gene apping in Candida albicans. Genetics 134:717-728.
    • (1993) Genetics , vol.134 , pp. 717-728
    • Fonzi, W.A.1    Irwin, M.Y.2
  • 20
    • 47749133814 scopus 로고    scopus 로고
    • Activation mechanism, functional role and shedding of glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface
    • Gagnon-Arsenault, I., L. Parise, J. Tremblay, and Y. Bourbonnais. 2008. Activation mechanism, functional role and shedding of glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface. Mol. Bicrobiol. 69:982-993.
    • (2008) Mol. Bicrobiol , vol.69 , pp. 982-993
    • Gagnon-Arsenault, I.1    Parise, L.2    Tremblay, J.3    Bourbonnais, Y.4
  • 21
    • 33749991922 scopus 로고    scopus 로고
    • Fungal apsins and cell wall: A unique family of aspartic peptidases for a distinctive ellular function
    • Gagnon-Arsenault, I., J. Tremblay, and Y. Bourbonnais. 2006. Fungal apsins and cell wall: a unique family of aspartic peptidases for a distinctive ellular function. FEMS Yeast Res. 6:966-978.
    • (2006) FEMS Yeast Res , vol.6 , pp. 966-978
    • Gagnon-Arsenault, I.1    Tremblay, J.2    Bourbonnais, Y.3
  • 22
    • 13444274743 scopus 로고    scopus 로고
    • New modules for he repeated internal and N-terminal epitope tagging of genes in Saccharomyces erevisiae
    • Gauss, R., M. Trautwein, T. Sommer, and A. Spang. 2005. New modules for he repeated internal and N-terminal epitope tagging of genes in Saccharomyces erevisiae. Yeast 22:1-12.
    • (2005) Yeast , vol.22 , pp. 1-12
    • Gauss, R.1    Trautwein, M.2    Sommer, T.3    Spang, A.4
  • 23
    • 0021742042 scopus 로고
    • Isolation of the Candida lbicans gene for orotidine-5'-phosphate decarboxylase by complementation f S. cerevisiae ura3 and E. coli pyrF mutations
    • Gillum, A. M., E. Y. Tsay, and D. R. Kirsch. 1984. Isolation of the Candida lbicans gene for orotidine-5'-phosphate decarboxylase by complementation f S. cerevisiae ura3 and E. coli pyrF mutations. Mol. Gen. Genet. 198:179-182.
    • (1984) Mol. Gen. Gene , vol.198 , pp. 179-182
    • Gillum, A.M.1    Tsay, E.Y.2    Kirsch, D.R.3
  • 25
    • 70450225229 scopus 로고    scopus 로고
    • The yeast Candida albicans evades human complement ttack by secretion of aspartic proteases
    • Gropp, K., et al. 2009. The yeast Candida albicans evades human complement ttack by secretion of aspartic proteases. Mol. Immunol. 47:465-475.
    • (2009) Mol. Immunol , vol.47 , pp. 465-475
    • Gropp, K.1
  • 26
    • 72449188627 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol-anchored pro-tease Sap9 odulates the interaction of Candida albicans with human neutrophils
    • Hornbach, A., et al. 2009. The glycosylphosphatidylinositol-anchored pro-tease Sap9 odulates the interaction of Candida albicans with human neutrophils. Infect. Immun. 77:5216-5224.
    • (2009) Infect. Immun , vol.77 , pp. 5216-5224
    • Hornbach, A.1
  • 27
    • 39749164061 scopus 로고    scopus 로고
    • Discovering the ecrets of the Candida albicans agglutinin-like sequence (ALS) gene family-a sticky pursuit
    • Hoyer, L. L., C. B. Green, S. H. Oh, and X. Zhao. 2008. Discovering the ecrets of the Candida albicans agglutinin-like sequence (ALS) gene family-a sticky pursuit. Med. Mycol. 46:1-15.
    • (2008) Med. Mycol , vol.46 , pp. 1-15
    • Hoyer, L.L.1    Green, C.B.2    Oh, S.H.3    Zhao, X.4
  • 28
    • 0033950964 scopus 로고    scopus 로고
    • The cell wall architecture of Candida albicans ild-type cells and cell wall-defective mutants
    • Kapteyn, J. C., et al. 2000. The cell wall architecture of Candida albicans ild-type cells and cell wall-defective mutants. Mol. Microbiol. 35:601-611.
    • (2000) Mol. Microbiol , vol.35 , pp. 601-611
    • Kapteyn, J.C.1
  • 29
    • 34250617570 scopus 로고    scopus 로고
    • A family of glycosylphosphatidylinositol- inked aspartyl proteases is required for virulence of Candida labrata
    • Kaur, R., B. Ma, and B. P. Cormack. 2007. A family of glycosylphosphatidylinositol- inked aspartyl proteases is required for virulence of Candida labrata. Proc. Natl. Acad. Sci. U. S. A. 104:7628-7633.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 7628-7633
    • Kaur, R.1    Ma, B.2    Cormack, B.P.3
  • 30
    • 70350020265 scopus 로고    scopus 로고
    • Covalently inked cell wall proteins of Candida albicans and their role in fitness and irulence
    • Klis, F. M., G. J. Sosinska, P. W. J. de Groot, and S. Brul. 2009. Covalently inked cell wall proteins of Candida albicans and their role in fitness and irulence. FEMS Yeast Res. 9:1013-1028.
    • (2009) FEMS Yeast Res , vol.9 , pp. 1013-1028
    • Klis, F.M.1    Sosinska, G.J.2    de Groot, P.W.J.3    Brul, S.4
  • 31
    • 0034648004 scopus 로고    scopus 로고
    • Enzymic characteristics of secreted aspartic proteases f Candida albicans
    • Koelsch, G., et al. 2000. Enzymic characteristics of secreted aspartic proteases f Candida albicans. Biochim. Biophys. Acta 1480:117-131.
    • (2000) Biochim. Biophys. Acta , vol.1480 , pp. 117-131
    • Koelsch, G.1
  • 32
    • 0033588223 scopus 로고    scopus 로고
    • Purification and characterization of the yeast glycosylphosphatidylinositolanchored, onobasic-specific aspartyl protease yapsin 2 (Mkc7p)
    • Komano, H., N. Rockwell, G. T. Wang, G. A. Krafft, and R. S. Fuller. 1999. Purification and characterization of the yeast glycosylphosphatidylinositolanchored, onobasic-specific aspartyl protease yapsin 2 (Mkc7p). J. Biol. Chem. 274:24431-24437.
    • (1999) J. Biol. Chem , vol.274 , pp. 24431-24437
    • Komano, H.1    Rockwell, N.2    Wang, G.T.3    Krafft, G.A.4    Fuller, R.S.5
  • 33
    • 23844501292 scopus 로고    scopus 로고
    • Yapsins are a family of aspartyl proteases required for cell wall integrity in accharomyces cerevisiae
    • Krysan, D. J., E. L. Ting, C. Abeijon, L. Kroos, and R. S. Fuller. 2005. Yapsins are a family of aspartyl proteases required for cell wall integrity in accharomyces cerevisiae. Eukaryot. Cell 4:1364-1374.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1364-1374
    • Krysan, D.J.1    Ting, E.L.2    Abeijon, C.3    Kroos, L.4    Fuller, R.S.5
  • 34
    • 68549139870 scopus 로고    scopus 로고
    • Trifluoromethanesulfonic cid-based proteomic analysis of cell wall and secreted proteins of the ascomycetous ungi Neurospora crassa and Candida albicans
    • Maddi, A., S. M. Bowman, and S. J. Free. 2009. Trifluoromethanesulfonic cid-based proteomic analysis of cell wall and secreted proteins of the ascomycetous ungi Neurospora crassa and Candida albicans. Fungal Genet. Biol. 6:768-781.
    • (2009) Fungal Genet. Biol , vol.6 , pp. 768-781
    • Maddi, A.1    Bowman, S.M.2    Free, S.J.3
  • 35
    • 6444235913 scopus 로고    scopus 로고
    • Role of Pir1 in the construction of the Candida lbicans cell wall
    • Martínez, A. I., et al. 2004. Role of Pir1 in the construction of the Candida lbicans cell wall. Microbiology 150:3151-3161.
    • (2004) Microbiology , vol.150 , pp. 3151-3161
    • Martínez, A.I.1
  • 36
    • 47249158622 scopus 로고    scopus 로고
    • Immunoproteomic analysis of the protective response obtained from accination with Candida albicans ecm33 cell wall mutant in mice
    • Martínez-López, R., C. Nombela, R. Diez-Orejas, L. Monteoliva, and C. Gil. 2008. Immunoproteomic analysis of the protective response obtained from accination with Candida albicans ecm33 cell wall mutant in mice. Proteomics: 2651-2664.
    • (2008) Proteomics , pp. 2651-2664
    • Martínez-López, R.1    Nombela, C.2    Diez-Orejas, R.3    Monteoliva, L.4    Gil, C.5
  • 37
    • 30944460880 scopus 로고    scopus 로고
    • Candida albicans Ecm33p is important for normal cell wall architecture and nteractions with host cells
    • Martinez-Lopez, R., H. Park, C. L. Myers, C. Gil, and S. G. Filler. 2006. Candida albicans Ecm33p is important for normal cell wall architecture and nteractions with host cells. Eukaryot. Cell 5:140-147.
    • (2006) Eukaryot. Cell , vol.5 , pp. 140-147
    • Martinez-Lopez, R.1    Park, H.2    Myers, C.L.3    Gil, C.4    Filler, S.G.5
  • 38
    • 0026506381 scopus 로고
    • A rapid and sensitive microassay or determination of chitinolytic activity
    • McCreath, K. J., and G. W. Gooday. 1992. A rapid and sensitive microassay or determination of chitinolytic activity. J. Microbiol. Methods 14:229-237.
    • (1992) J. Microbiol. Methods , vol.14 , pp. 229-237
    • McCreath, K.J.1    Gooday, G.W.2
  • 39
    • 0028913997 scopus 로고
    • Molecular cloning nd characterization of chitinase genes from Candida albicans
    • McCreath, K. J., C. A. Specht, and P. W. Robbins. 1995. Molecular cloning nd characterization of chitinase genes from Candida albicans. Proc. Natl. cad. Sci. U. S. A. 92:2544-2548.
    • (1995) Proc. Natl. Cad. Sci. U. S. A , vol.92 , pp. 2544-2548
    • McCreath, K.J.1    Specht, C.A.2    Robbins, P.W.3
  • 40
    • 77950252783 scopus 로고    scopus 로고
    • Contribution of Candida albicans cell wall omponents to recognition by and escape from murine macrophages
    • McKenzie, C. G., et al. 2010. Contribution of Candida albicans cell wall omponents to recognition by and escape from murine macrophages. Infect. mmun. 78:1650-1658.
    • (2010) Infect. Mmun , vol.78 , pp. 1650-1658
    • McKenzie, C.G.1
  • 41
    • 64549125592 scopus 로고    scopus 로고
    • A novel immune evasion strategy of Candida lbicans: Proteolytic cleavage of a salivary antimicrobial peptide
    • Meiller, T. F., et al. 2009. A novel immune evasion strategy of Candida lbicans: proteolytic cleavage of a salivary antimicrobial peptide. PLoS One 4: e5039.
    • (2009) PLoS One , vol.4
    • Meiller, T.F.1
  • 42
    • 33645549216 scopus 로고    scopus 로고
    • The MAP kinase ignal transduction network in Candida albicans
    • Monge, R. A., E. Roman, C. Nombela, and J. Pla. 2006. The MAP kinase ignal transduction network in Candida albicans. Microbiology 152:905-912.
    • (2006) Microbiology , vol.152 , pp. 905-912
    • Monge, R.A.1    Roman, E.2    Nombela, C.3    Pla, J.4
  • 44
    • 0030883927 scopus 로고    scopus 로고
    • Specific labelling of ell wall proteins by biotinylation. Identification of four covalently linked -mannosylated proteins of Saccharomyces cerevisiae
    • Mrsa, V., T. Seidl, M. Gentzsch, and W. Tanner. 1997. Specific labelling of ell wall proteins by biotinylation. Identification of four covalently linked -mannosylated proteins of Saccharomyces cerevisiae. Yeast 13:1145-1154.
    • (1997) Yeast , vol.13 , pp. 1145-1154
    • Mrsa, V.1    Seidl, T.2    Gentzsch, M.3    Tanner, W.4
  • 45
    • 0034653201 scopus 로고    scopus 로고
    • CIp10, an efficient and convenient integrating vector for Candida lbicans
    • Murad, A. M., P. R. Lee, I. D. Broadbent, C. J. Barelle, and A. J. Brown. 2000. CIp10, an efficient and convenient integrating vector for Candida lbicans. Yeast 16:325-327.
    • (2000) Yeast , vol.16 , pp. 325-327
    • Murad A., M.1    Lee, P.R.2    Broadbent, I.D.3    Barelle, C.J.4    Brown, A.J.5
  • 46
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans ecreted aspartyl proteinases in virulence and pathogenesis
    • Naglik, J. R., S. J. Challacombe, and B. Hube. 2003. Candida albicans ecreted aspartyl proteinases in virulence and pathogenesis. Microbiol. Mol. Biol. Rev. 67:400-428.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 47
    • 57349145280 scopus 로고    scopus 로고
    • Quantitative expression of the Candida albicans ecreted aspartyl proteinase gene family in human oral and vaginal candidiasis
    • Naglik, J. R., et al. 2008. Quantitative expression of the Candida albicans ecreted aspartyl proteinase gene family in human oral and vaginal candidiasis. Microbiology 154:3266-3280.
    • (2008) Microbiology , vol.154 , pp. 3266-3280
    • Naglik, J.R.1
  • 48
    • 37349015349 scopus 로고    scopus 로고
    • An ntegrated model of the recognition of Candida albicans by the innate immune system
    • Netea, M. G., G. D. Brown, B. J. Kullberg, and N. A. Gow. 2008. An ntegrated model of the recognition of Candida albicans by the innate immune system. Nat. Rev. Microbiol. 6:67-78.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 67-78
    • Netea, M.G.1    Brown, G.D.2    Kullberg, B.J.3    Gow, N.A.4
  • 49
    • 0030710147 scopus 로고    scopus 로고
    • KEX2 influences Candida albicans proteinase secretion and hyphal formation
    • Newport, G., and N. Agabian. 1997. KEX2 influences Candida albicans proteinase secretion and hyphal formation. J. Biol. Chem. 272:28954-28961.
    • (1997) J. Biol. Chem , vol.272 , pp. 28954-28961
    • Newport, G.1    Agabian, N.2
  • 50
    • 0004246866 scopus 로고
    • Candida and candidosis
    • Baillière Tindall, London, United Kingdom
    • Odds, F. C. 1988. Candida and candidosis. Baillière Tindall, London, United Kingdom.
    • (1988)
    • Odds, F.C.1
  • 51
    • 0033560722 scopus 로고    scopus 로고
    • Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene
    • Olsen, V., N. X. Cawley, J. Brandt, M. Egel-Mitani, and Y. P. Loh. 1999. Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene. Biochem. J. 339(2):407-411.
    • (1999) Biochem. J , vol.339 , Issue.2 , pp. 407-411
    • Olsen, V.1    Cawley, N.X.2    Brandt, J.3    Egel-Mitani, M.4    Loh, Y.P.5
  • 52
    • 0032478123 scopus 로고    scopus 로고
    • Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: Correlation with electronegative active-site pockets predicted by molecular modeling
    • Olsen, V., et al. 1998. Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: correlation with electronegative active-site pockets predicted by molecular modeling. Biochemistry 37:2768-2777.
    • (1998) Biochemistry , vol.37 , pp. 2768-2777
    • Olsen, V.1
  • 53
    • 34249724445 scopus 로고    scopus 로고
    • Nosocomial fungal infections: Epidemiology, diagnosis, and treatment
    • Perlroth, J., B. Choi, and B. Spellberg. 2007. Nosocomial fungal infections: epidemiology, diagnosis, and treatment. Med. Mycol. 45:321-346.
    • (2007) Med. Mycol , vol.45 , pp. 321-346
    • Perlroth, J.1    Choi, B.2    Spellberg, B.3
  • 54
    • 0038631572 scopus 로고    scopus 로고
    • Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome
    • Pitarch, A., M. Sanchez, C. Nombela, and C. Gil. 2002. Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome. Mol. Cell. Proteomics 1:967-982.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 967-982
    • Pitarch, A.1    Sanchez, M.2    Nombela, C.3    Gil, C.4
  • 55
    • 0028070285 scopus 로고
    • Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease
    • Polgar, L., Z. Szeltner, and I. Boros. 1994. Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease. Biochemistry 33:9351-9357.
    • (1994) Biochemistry , vol.33 , pp. 9351-9357
    • Polgar, L.1    Szeltner, Z.2    Boros, I.3
  • 56
    • 0032903637 scopus 로고    scopus 로고
    • The Gas1 glycoprotein, a putative wall polymer cross-linker
    • Popolo, L., and M. Vai. 1999. The Gas1 glycoprotein, a putative wall polymer cross-linker. Biochim. Biophys. Acta 1426:385-400.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 385-400
    • Popolo, L.1    Vai, M.2
  • 57
    • 33847225225 scopus 로고    scopus 로고
    • Comprehensive analysis of glycosylphosphatidylinositol-anchored proteins in Candida albicans
    • Richard, M. L., and A. Plaine. 2007. Comprehensive analysis of glycosylphosphatidylinositol-anchored proteins in Candida albicans. Eukaryot. Cell 6:119-133.
    • (2007) Eukaryot. Cell , vol.6 , pp. 119-133
    • Richard, M.L.1    Plaine, A.2
  • 58
    • 0035200240 scopus 로고    scopus 로고
    • Signaling through adenylyl cyclase is essential for hyphal growth and virulence in the pathogenic fungus Candida albicans
    • Rocha, C. R., et al. 2001. Signaling through adenylyl cyclase is essential for hyphal growth and virulence in the pathogenic fungus Candida albicans. Mol. Biol. Cell 12:3631-3643.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3631-3643
    • Rocha, C.R.1
  • 59
    • 0019503111 scopus 로고
    • Properties of a purified proteinase from the yeast Candida albicans
    • Rüchel, R. 1981. Properties of a purified proteinase from the yeast Candida albicans. Biochim. Biophys. Acta 659:99-113.
    • (1981) Biochim. Biophys. Acta , vol.659 , pp. 99-113
    • Rüchel, R.1
  • 60
    • 0037205508 scopus 로고    scopus 로고
    • Management of mycoses in patients with hematologic disease and cancer-review of the literature
    • Ruhnke, M., and G. Maschmeyer. 2002. Management of mycoses in patients with hematologic disease and cancer-review of the literature. Eur. J. Med. Res. 7:227-235.
    • (2002) Eur. J. Med. Res , vol.7 , pp. 227-235
    • Ruhnke, M.1    Maschmeyer, G.2
  • 61
    • 33645056930 scopus 로고    scopus 로고
    • Molecular organization of the cell wall of Candida albicans and its relation to pathogenicity
    • Ruiz-Herrera, J., M. V. Elorza, E. Valentin, and R. Sentandreu. 2006. Molecular organization of the cell wall of Candida albicans and its relation to pathogenicity. FEMS Yeast Res. 6:14-29.
    • (2006) FEMS Yeast Res , vol.6 , pp. 14-29
    • Ruiz-Herrera, J.1    Elorza, M.V.2    Valentin, E.3    Sentandreu, R.4
  • 62
    • 33644683261 scopus 로고    scopus 로고
    • Hydrolytic enzymes as virulence factors of Candida albicans
    • Schaller, M., C. Borelli, H. C. Korting, and B. Hube. 2005. Hydrolytic enzymes as virulence factors of Candida albicans. Mycoses 48:365-377.
    • (2005) Mycoses , vol.48 , pp. 365-377
    • Schaller, M.1    Borelli, C.2    Korting, H.C.3    Hube, B.4
  • 63
    • 1942505375 scopus 로고    scopus 로고
    • Independent regulation of chitin synthase and chitinase activity in Candida albicans and Saccharomyces cerevisiae
    • Selvaggini, S., C. A. Munro, S. Paschoud, D. Sanglard, and N. A. Gow. 2004. Independent regulation of chitin synthase and chitinase activity in Candida albicans and Saccharomyces cerevisiae. Microbiology 150:921-928.
    • (2004) Microbiology , vol.150 , pp. 921-928
    • Selvaggini, S.1    Munro, C.A.2    Paschoud, S.3    Sanglard, D.4    Gow, N.A.5
  • 64
    • 3142677978 scopus 로고    scopus 로고
    • Functional and structural diversity in the Als protein family of Candida albicans
    • Sheppard, D. C., et al. 2004. Functional and structural diversity in the Als protein family of Candida albicans. J. Biol. Chem. 279:30480-30489.
    • (2004) J. Biol. Chem , vol.279 , pp. 30480-30489
    • Sheppard, D.C.1
  • 65
    • 77956858246 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the secretome of Candida albicans
    • Sorgo, A. G., et al. 2010. Mass spectrometric analysis of the secretome of Candida albicans. Yeast 27:661-672.
    • (2010) Yeast , vol.27 , pp. 661-672
    • Sorgo, A.G.1
  • 66
    • 33751102883 scopus 로고    scopus 로고
    • Proteomics for the analysis of the Candida albicans biofilm lifestyle
    • Thomas, D. P., S. P. Bachmann, and J. L. Lopez-Ribot. 2006. Proteomics for the analysis of the Candida albicans biofilm lifestyle. Proteomics 6:5795-5804.
    • (2006) Proteomics , vol.6 , pp. 5795-5804
    • Thomas, D.P.1    Bachmann, S.P.2    Lopez-Ribot, J.L.3
  • 67
    • 0038018413 scopus 로고    scopus 로고
    • Identification of cell surface determinants in Candida albicans reveals Tsa1p, a protein differentially localized in the cell
    • Urban, C., K. Sohn, F. Lottspeich, H. Brunner, and S. Rupp. 2003. Identification of cell surface determinants in Candida albicans reveals Tsa1p, a protein differentially localized in the cell. FEBS Lett. 544:228-235.
    • (2003) FEBS Lett , vol.544 , pp. 228-235
    • Urban, C.1    Sohn, K.2    Lottspeich, F.3    Brunner, H.4    Rupp, S.5
  • 68
    • 0037354365 scopus 로고    scopus 로고
    • An improved transformation protocol for the human fungal pathogen Candida albicans
    • Walther, A., and J. Wendland. 2003. An improved transformation protocol for the human fungal pathogen Candida albicans. Curr. Genet. 42:339-343.
    • (2003) Curr. Genet , vol.42 , pp. 339-343
    • Walther, A.1    Wendland, J.2
  • 69
    • 4344604358 scopus 로고    scopus 로고
    • A family of Candida cell surface haem-binding proteins involved in haemin and haemoglobin-iron utilization
    • Weissman, Z., and D. Kornitzer. 2004. A family of Candida cell surface haem-binding proteins involved in haemin and haemoglobin-iron utilization. Mol. Microbiol. 53:1209-1220.
    • (2004) Mol. Microbiol , vol.53 , pp. 1209-1220
    • Weissman, Z.1    Kornitzer, D.2
  • 70
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., and U. I. Flugge. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143.
    • (1984) Anal. Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 71
    • 33646242974 scopus 로고    scopus 로고
    • A drug-sensitive genetic network masks fungi from the immune system
    • Wheeler, R. T., and G. R. Fink. 2006. A drug-sensitive genetic network masks fungi from the immune system. PLoS Pathog. 2:e35.
    • (2006) PLoS Pathog , vol.2
    • Wheeler, R.T.1    Fink, G.R.2
  • 72
    • 35848955684 scopus 로고    scopus 로고
    • Morphogenesis in Candida albicans
    • Whiteway, M., and C. Bachewich. 2007. Morphogenesis in Candida albicans. Annu. Rev. Microbiol. 61:529-553.
    • (2007) Annu. Rev. Microbiol , vol.61 , pp. 529-553
    • Whiteway, M.1    Bachewich, C.2
  • 73
    • 67651173120 scopus 로고    scopus 로고
    • Identifying infection-associated genes of Candida albicans in the postgenomic era
    • Wilson, D., et al. 2009. Identifying infection-associated genes of Candida albicans in the postgenomic era. FEMS Yeast Res. 9:688-700.
    • (2009) FEMS Yeast Res , vol.9 , pp. 688-700
    • Wilson, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.