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Volumn 17, Issue 2, 2004, Pages 281-310

Surface Glycans of Candida albicans and Other Pathogenic Fungi: Physiological Roles, Clinical Uses, and Experimental Challenges

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE DERIVATIVE; CHITIN; DNA; GLUCAN; GLYCAN DERIVATIVE; GLYCOPROTEIN; MANNAN; RNA; SIALIC ACID DERIVATIVE;

EID: 2042489656     PISSN: 08938512     EISSN: None     Source Type: Journal    
DOI: 10.1128/CMR.17.2.281-310.2004     Document Type: Review
Times cited : (150)

References (325)
  • 1
    • 0026474072 scopus 로고
    • Stimulation of human monocyte β-glucan receptors by glucan particles induces production of TNF-α and IL-1β
    • Abel, G., and J. K. Czop. 1992. Stimulation of human monocyte β-glucan receptors by glucan particles induces production of TNF-α and IL-1β. Int. J. Immunopharmacol. 14:1363-1373.
    • (1992) Int. J. Immunopharmacol. , vol.14 , pp. 1363-1373
    • Abel, G.1    Czop, J.K.2
  • 3
    • 33746387830 scopus 로고    scopus 로고
    • Involvement of the major glycopotein (gp43) of Paracoccidioides brasiliensis in attachment to macrophages
    • Almeida, S. R., C. S. Unterkircher, and Z. P. Camargo. 1998. Involvement of the major glycopotein (gp43) of Paracoccidioides brasiliensis in attachment to macrophages. Med. Mycol. 36:405-411.
    • (1998) Med. Mycol. , vol.36 , pp. 405-411
    • Almeida, S.R.1    Unterkircher, C.S.2    Camargo, Z.P.3
  • 7
    • 0036668543 scopus 로고    scopus 로고
    • Role of Paracoccidioides brasiliensis cell wall fraction containing β-glucan in tumor necrosis factor-alpha production by human monocytes: Correlation with fungicidal activity
    • Anjos, A. R., S. A. Calvi, R. Ferracini, M. T. S. Peraçoli, C. L. Silva, and A. M. V. C. Soares. 2002. Role of Paracoccidioides brasiliensis cell wall fraction containing β-glucan in tumor necrosis factor-alpha production by human monocytes: Correlation with fungicidal activity. Med. Mycol. 40:377-382.
    • (2002) Med. Mycol. , vol.40 , pp. 377-382
    • Anjos, A.R.1    Calvi, S.A.2    Ferracini, R.3    Peraçoli, M.T.S.4    Silva, C.L.5    Soares, A.M.V.C.6
  • 8
    • 0031820069 scopus 로고    scopus 로고
    • High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid
    • Anumula, K. R., and S. T. Dhume. 1998. High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid. Glycobiology 8:685-694.
    • (1998) Glycobiology , vol.8 , pp. 685-694
    • Anumula, K.R.1    Dhume, S.T.2
  • 10
    • 0001151876 scopus 로고
    • Pectins, plant gums, and other plant polysaccharides
    • W. Pigman and D. Horton (ed.). Academic Press, Inc., New York, N.Y.
    • Aspinall, G. O. 1970. Pectins, plant gums, and other plant polysaccharides, p. 515-568. In W. Pigman and D. Horton (ed.), The carbohydrates. Chemistry and biochemistry, 2nd ed., vol. IIB. Academic Press, Inc., New York, N.Y.
    • (1970) The Carbohydrates. Chemistry and Biochemistry, 2nd Ed. , vol.2 B , pp. 515-568
    • Aspinall, G.O.1
  • 11
    • 0022497937 scopus 로고
    • Coagglutination reactions between Candida albicans and oral bacteria
    • Bagg, J., and R. W. Silverwood. 1986. Coagglutination reactions between Candida albicans and oral bacteria. J. Med. Microbiol. 22:165-169.
    • (1986) J. Med. Microbiol. , vol.22 , pp. 165-169
    • Bagg, J.1    Silverwood, R.W.2
  • 12
    • 0037195371 scopus 로고    scopus 로고
    • Change of cell wall chitin content in amphotericin B resistant Kluyveromyces strains
    • Bahmed, K., R. Bonaly, M. Wathier, B. Pucci, and J. Coulon. 2002. Change of cell wall chitin content in amphotericin B resistant Kluyveromyces strains. FEMS Microbiol. Lett. 216:99-103.
    • (2002) FEMS Microbiol. Lett. , vol.216 , pp. 99-103
    • Bahmed, K.1    Bonaly, R.2    Wathier, M.3    Pucci, B.4    Coulon, J.5
  • 13
    • 0002180797 scopus 로고
    • Yeast cell wall and cell surface
    • J. N. Strathern, E. W. Jones, and J. R. Broach (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Ballou, C. E. 1982. Yeast cell wall and cell surface, p. 335-360. In J. N. Strathern, E. W. Jones, and J. R. Broach (ed.), The molecular biology of the yeast Saccharomyces. Metabolism and gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1982) The Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression , pp. 335-360
    • Ballou, C.E.1
  • 14
    • 0015789513 scopus 로고
    • Genetic control of yeast mannan structure
    • Ballou, C. E., K. A. Kern, and W. C. Raschke. 1973. Genetic control of yeast mannan structure. J. Biol. Chem. 248:4667-4673.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4667-4673
    • Ballou, C.E.1    Kern, K.A.2    Raschke, W.C.3
  • 16
    • 0020618703 scopus 로고
    • Host-parasite interactions in the pathogenesis of experimental renal candidiasis
    • Barnes, J. L., R. W. Osgood, J. C. Lee, R. D. King, and J. H. Stein. 1983. Host-parasite interactions in the pathogenesis of experimental renal candidiasis. Lab. Investig. 49:460-467.
    • (1983) Lab. Investig. , vol.49 , pp. 460-467
    • Barnes, J.L.1    Osgood, R.W.2    Lee, J.C.3    King, R.D.4    Stein, J.H.5
  • 17
    • 0027511893 scopus 로고
    • Secular trends in the epidemiology of nosocomial fungal infections in the United States, 1980-1990
    • Beck-Sagué, C. M., W. R. Jarvis, and National Nosocomial Infections Surveillance System. 1993. Secular trends in the epidemiology of nosocomial fungal infections in the United States, 1980-1990. J. Infect. Dis. 167:1247-1251.
    • (1993) J. Infect. Dis. , vol.167 , pp. 1247-1251
    • Beck-Sagué, C.M.1    Jarvis, W.R.2
  • 19
    • 0022495801 scopus 로고
    • Ultrastructural localization of glycoconjugates in the fungus Ascocalyx abietina, the scleroderris canker agent of conifers, using lectin-gold complexes
    • Benhamou, N., and G. B. Ouellette. 1986. Ultrastructural localization of glycoconjugates in the fungus Ascocalyx abietina, the scleroderris canker agent of conifers, using lectin-gold complexes. J. Histochem. Cytochem. 34:855-867.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 855-867
    • Benhamou, N.1    Ouellette, G.B.2
  • 20
    • 0029065495 scopus 로고
    • Regulation of yeast Golgi glycosylation. Guanosine diphosphatase functions as a homodimer in the membrane
    • Berninsone, P., Z.-Y. Lin, E. Kempner, and C. B. Hirschberg. 1995. Regulation of yeast Golgi glycosylation. Guanosine diphosphatase functions as a homodimer in the membrane. J. Biol. Chem. 270:14564-14567.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14564-14567
    • Berninsone, P.1    Lin, Z.-Y.2    Kempner, E.3    Hirschberg, C.B.4
  • 21
    • 0343853185 scopus 로고
    • The cell wall polysaccharides of Candida albicans: Glucan, mannan, and chitin
    • Bishop, C. T., F. Blank, and P. E. Gardner. 1960. The cell wall polysaccharides of Candida albicans: glucan, mannan, and chitin. Can. J. Chem. 38:869-881.
    • (1960) Can. J. Chem. , vol.38 , pp. 869-881
    • Bishop, C.T.1    Blank, F.2    Gardner, P.E.3
  • 22
  • 24
    • 0036784710 scopus 로고    scopus 로고
    • Interplay between protective and inhibitory antibodies dictates the outcome of experimentally disseminated candidiasis in recipients of a Candida albicans vaccine
    • Bromuro, C., A. Torosantucci, P. Chiani, S. Conti, L. Polonelli, and A. Cassone. 2002. Interplay between protective and inhibitory antibodies dictates the outcome of experimentally disseminated candidiasis in recipients of a Candida albicans vaccine. Infect. Immun. 70:5462-5470.
    • (2002) Infect. Immun. , vol.70 , pp. 5462-5470
    • Bromuro, C.1    Torosantucci, A.2    Chiani, P.3    Conti, S.4    Polonelli, L.5    Cassone, A.6
  • 26
    • 0031049158 scopus 로고    scopus 로고
    • Vaginal colonization or infection with Candida albicans in human immunodeficiency virus-infected women during pregnancy and during the postpartum period
    • Burns, D. N., R. Tuomala, B.-H. Chang, R. Hershow, H. Minkoff, E. Rodriguez, C. Zorrilla, H. Hammill, J. Regan, and Women and Infants Transmission Study Group. 1997. Vaginal colonization or infection with Candida albicans in human immunodeficiency virus-infected women during pregnancy and during the postpartum period. Clin. Infect. Dis. 24:201-210.
    • (1997) Clin. Infect. Dis. , vol.24 , pp. 201-210
    • Burns, D.N.1    Tuomala, R.2    Chang, B.-H.3    Hershow, R.4    Minkoff, H.5    Rodriguez, E.6    Zorrilla, C.7    Hammill, H.8    Regan, J.9
  • 27
    • 0032560548 scopus 로고    scopus 로고
    • Molecular analysis of CaMnt1p, a mannosyl transferase important for adhesion and virulence of Candida albicans
    • Buurman, E. T., C. Westwater, B. Hube, A. J. P. Brown, F. C. Odds, and N. A. R. Gow. 1998. Molecular analysis of CaMnt1p, a mannosyl transferase important for adhesion and virulence of Candida albicans. Proc. Natl. Acad. Sci. USA 95:7670-7675.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7670-7675
    • Buurman, E.T.1    Westwater, C.2    Hube, B.3    Brown, A.J.P.4    Odds, F.C.5    Gow, N.A.R.6
  • 28
    • 0037415423 scopus 로고    scopus 로고
    • Candida albicans mannan-protein conjugate as vaccine candidate
    • Bystricky, S., E. Paulovicová, and E. Machová. 2003. Candida albicans mannan-protein conjugate as vaccine candidate. Immunol. Lett. 85:251-255.
    • (2003) Immunol. Lett. , vol.85 , pp. 251-255
    • Bystricky, S.1    Paulovicová, E.2    Machová, E.3
  • 29
    • 0035827639 scopus 로고    scopus 로고
    • The yeast cell wall and septum as paradigms of cell growth and morphogenesis
    • Cabib, E., D.-H. Roh, M. Schmidt, L. B. Crotti, and A. Varma. 2001. The yeast cell wall and septum as paradigms of cell growth and morphogenesis. J. Biol. Chem. 276:19679-19682.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19679-19682
    • Cabib, E.1    Roh, D.-H.2    Schmidt, M.3    Crotti, L.B.4    Varma, A.5
  • 30
    • 0030813822 scopus 로고    scopus 로고
    • A monoclonal antibody to Candida albicans enhances mouse neutrophil candidacidal activity
    • Caesar-TonThat, T.-C., and J. E. Cutler. 1997. A monoclonal antibody to Candida albicans enhances mouse neutrophil candidacidal activity. Infect. Immun. 65:5354-5357.
    • (1997) Infect. Immun. , vol.65 , pp. 5354-5357
    • Caesar-TonThat, T.-C.1    Cutler, J.E.2
  • 32
    • 0011091789 scopus 로고    scopus 로고
    • Host recognition by Candida species
    • R. A. Calderone (ed.). ASM Press, Washington, D.C.
    • Calderone, R., and N. A. R. Gow. 2002. Host recognition by Candida species, p. 67-86. In R. A. Calderone (ed.), Candida and candidiasis. ASM Press, Washington, D.C.
    • (2002) Candida and Candidiasis , pp. 67-86
    • Calderone, R.1    Gow, N.A.R.2
  • 35
    • 0027222876 scopus 로고
    • Recognition between Candida albicans and host cells
    • Calderone, R. A. 1993. Recognition between Candida albicans and host cells. Trends Microbiol. 1:55-58.
    • (1993) Trends Microbiol. , vol.1 , pp. 55-58
    • Calderone, R.A.1
  • 36
    • 0026061798 scopus 로고
    • Adherence and receptor relationships of Candida albicans
    • Calderone, R. A., and P. C. Braun. 1991. Adherence and receptor relationships of Candida albicans. Microbiol. Rev. 55:1-20.
    • (1991) Microbiol. Rev. , vol.55 , pp. 1-20
    • Calderone, R.A.1    Braun, P.C.2
  • 37
    • 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
  • 38
    • 0034948464 scopus 로고    scopus 로고
    • Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment
    • Callewaert, N., S. Geysens, F. Molemans, and R. Contreras. 2001. Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment. Glycobiology 11:275-281.
    • (2001) Glycobiology , vol.11 , pp. 275-281
    • Callewaert, N.1    Geysens, S.2    Molemans, F.3    Contreras, R.4
  • 41
    • 0029060899 scopus 로고
    • Rats clearing a vaginal infection by Candida albicans acquire specific, antibody-mediated resistance to vaginal reinfection
    • Cassone, A., M. Boccanera, D. Adriani, G. Santoni, and F. De Bernadis. 1995. Rats clearing a vaginal infection by Candida albicans acquire specific, antibody-mediated resistance to vaginal reinfection. Infect. Immun. 63:2619-2624.
    • (1995) Infect. Immun. , vol.63 , pp. 2619-2624
    • Cassone, A.1    Boccanera, M.2    Adriani, D.3    Santoni, G.4    De Bernadis, F.5
  • 42
    • 0017885362 scopus 로고
    • Agglutination of blastospores of Candida albicans by concanavalin A and its relationship with the distribution of mannan polymers and the ultrastructure of the cell wall
    • Cassone, A., E. Mattia, and L. Boldrini. 1978. Agglutination of blastospores of Candida albicans by concanavalin A and its relationship with the distribution of mannan polymers and the ultrastructure of the cell wall. J. Gen. Microbiol. 105:263-273.
    • (1978) J. Gen. Microbiol. , vol.105 , pp. 263-273
    • Cassone, A.1    Mattia, E.2    Boldrini, L.3
  • 43
    • 0015791826 scopus 로고
    • Ultrastructural changes in the wall during germ-tube formation from blastospores of Candida albicans
    • Cassone, A., N. Simonetti, and V. Strippoli. 1973. Ultrastructural changes in the wall during germ-tube formation from blastospores of Candida albicans. J. Gen. Microbiol. 77:417-426.
    • (1973) J. Gen. Microbiol. , vol.77 , pp. 417-426
    • Cassone, A.1    Simonetti, N.2    Strippoli, V.3
  • 44
    • 0002545471 scopus 로고
    • Immunological moieties of the cell wall
    • R. Prasad (ed.). Candida albicans. Springer-Verlag, New York, N.Y.
    • Cassone, A., and A. Torosantucci. 1991. Immunological moieties of the cell wall, p. 89-107. In R. Prasad (ed.), Candida albicans. Cellular and molecular biology. Springer-Verlag, New York, N.Y.
    • (1991) Cellular and Molecular Biology , pp. 89-107
    • Cassone, A.1    Torosantucci, A.2
  • 45
    • 0027930720 scopus 로고
    • Candida albicans stimulates arachidonic acid liberation from alveolar macrophages through α-mannan and β-glucan cell wall components
    • Castro, M., N. V. C. Ralston, T. I. Morgenthaler, M. S. Rohrbach, and A. H. Limper. 1994. Candida albicans stimulates arachidonic acid liberation from alveolar macrophages through α-mannan and β-glucan cell wall components. Infect. Immun. 62:3138-3145.
    • (1994) Infect. Immun. , vol.62 , pp. 3138-3145
    • Castro, M.1    Ralston, N.V.C.2    Morgenthaler, T.I.3    Rohrbach, M.S.4    Limper, A.H.5
  • 46
    • 0037136409 scopus 로고    scopus 로고
    • Lectin activities of cytokines: Functions and putative carbohydrate-recognition domains
    • Cebo, C., G. Vergoten, and J.-P. Zanetta. 2002. Lectin activities of cytokines: functions and putative carbohydrate-recognition domains. Biochim. Biophys. Acta 1572:422-434.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 422-434
    • Cebo, C.1    Vergoten, G.2    Zanetta, J.-P.3
  • 47
    • 0020683790 scopus 로고
    • Modulation of Candida albicans attachment to human epithelial cells by bacteria and carbohydrates
    • Centeno, A., C. P. Davis, M. S. Cohen, and M. M. Warren. 1983. Modulation of Candida albicans attachment to human epithelial cells by bacteria and carbohydrates. Infect. Immun. 39:1354-1360.
    • (1983) Infect. Immun. , vol.39 , pp. 1354-1360
    • Centeno, A.1    Davis, C.P.2    Cohen, M.S.3    Warren, M.M.4
  • 48
    • 0002504789 scopus 로고
    • Monosaccharides
    • M. F. Chaplin, and J. F. Kennedy (ed.). IRL Press, Washington, D.C.
    • Chaplin, M. F. 1986. Monosaccharides, p. 1-36. In M. F. Chaplin, and J. F. Kennedy (ed.), Carbohydrate analysis: a practical approach. IRL Press, Washington, D.C.
    • (1986) Carbohydrate Analysis: A Practical Approach , pp. 1-36
    • Chaplin, M.F.1
  • 49
    • 16744363444 scopus 로고    scopus 로고
    • Economic consequences of invasive aspergillosis due to Aspergillus or to other filamentous fungal infection in patients treated for acute myeloid leukemia and preventative treatments modeling
    • Chapuis, F., A. Thiebaut, A. Bataillard, M. A. Piens, A. Lafuma, M. C. Nicolle, and J. P. Auray. 2001. Economic consequences of invasive aspergillosis due to Aspergillus or to other filamentous fungal infection in patients treated for acute myeloid leukemia and preventative treatments modeling. J. Mycol. Med. 11:67-72.
    • (2001) J. Mycol. Med. , vol.11 , pp. 67-72
    • Chapuis, F.1    Thiebaut, A.2    Bataillard, A.3    Piens, M.A.4    Lafuma, A.5    Nicolle, M.C.6    Auray, J.P.7
  • 50
    • 0014290672 scopus 로고
    • Cell wall composition of the mycelial and blastospore forms of Candida albicans
    • Chattaway, F. W., M. R. Holmes, and J. E. Barlow. 1968. Cell wall composition of the mycelial and blastospore forms of Candida albicans. J. Gen. Microbiol. 51:367-376.
    • (1968) J. Gen. Microbiol. , vol.51 , pp. 367-376
    • Chattaway, F.W.1    Holmes, M.R.2    Barlow, J.E.3
  • 51
    • 0029081915 scopus 로고
    • Analysis of mono- and oligosaccharide isomers derivatized with 9-aminopyrene-1,4,6-trisulfonate by capillary electrophoresis with laser-induced fluorescence
    • Chen, F. A., and R. A. Evangelista. 1995. Analysis of mono- and oligosaccharide isomers derivatized with 9-aminopyrene-1,4,6-trisulfonate by capillary electrophoresis with laser-induced fluorescence. Anal. Biochem. 230:273-280.
    • (1995) Anal. Biochem. , vol.230 , pp. 273-280
    • Chen, F.A.1    Evangelista, R.A.2
  • 52
    • 0028216864 scopus 로고
    • Polysaccharide antigens of the capsule of Cryptococcus neoformans
    • Cherniak, R., and J. B. Sundstrom. 1994. Polysaccharide antigens of the capsule of Cryptococcus neoformans. Infect. Immun. 62:1507-1512.
    • (1994) Infect. Immun. , vol.62 , pp. 1507-1512
    • Cherniak, R.1    Sundstrom, J.B.2
  • 53
    • 0027321312 scopus 로고
    • Capillary zone electrophoresis of malto-oligosaccharides derivatized with 8-aminonaphthalene-1,3,6-trisulfonic acid
    • Chiesa, C., and C. Horváth. 1993. Capillary zone electrophoresis of malto-oligosaccharides derivatized with 8-aminonaphthalene-1,3,6-trisulfonic acid. J. Chromatogr. 645:337-352.
    • (1993) J. Chromatogr. , vol.645 , pp. 337-352
    • Chiesa, C.1    Horváth, C.2
  • 55
    • 0034801559 scopus 로고    scopus 로고
    • 3 subunit of the antigenic polysaccharides from Leptospira biflexa and the octameric (1→2)-linked β-D-mannan of the Candida albicans phospholipomannan. X-ray crystal structure of the protected tetramer
    • 3 subunit of the antigenic polysaccharides from Leptospira biflexa and the octameric (1→2)-linked β-D-mannan of the Candida albicans phospholipomannan. X-ray crystal structure of the protected tetramer. J. Am. Chem. Soc. 123:5826-5828.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5826-5828
    • Crich, D.1    Li, H.2    Yao, Q.3    Wink, D.J.4    Sommer, R.D.5    Rheingold, A.L.6
  • 56
    • 0029032512 scopus 로고
    • Ingestion of acapsular Cryptococcus neoformans occurs via mannose and β-glucan receptors, resulting in cytokine production and increased phagocytosis of the encapsulated form
    • Cross, C. E., and G. J. Bancroft. 1995. Ingestion of acapsular Cryptococcus neoformans occurs via mannose and β-glucan receptors, resulting in cytokine production and increased phagocytosis of the encapsulated form. Infect. Immun. 63:2604-2611.
    • (1995) Infect. Immun. , vol.63 , pp. 2604-2611
    • Cross, C.E.1    Bancroft, G.J.2
  • 57
    • 0032077836 scopus 로고    scopus 로고
    • The Candida albicans phosphomannan complex in Candida-host interactions
    • Cutler, J. E. 1998. The Candida albicans phosphomannan complex in Candida-host interactions. Res. Immunol. 149:299-308.
    • (1998) Res. Immunol. , vol.149 , pp. 299-308
    • Cutler, J.E.1
  • 58
    • 0035659728 scopus 로고    scopus 로고
    • N-Glycosylation of yeast, with emphasis on Candida albicans
    • Cutler, J. E. 2001. N-Glycosylation of yeast, with emphasis on Candida albicans. Med. Mycol. 39:75-86.
    • (2001) Med. Mycol. , vol.39 , pp. 75-86
    • Cutler, J.E.1
  • 59
    • 0025989934 scopus 로고
    • Putative virulence factors of Candida albicans
    • Cutler, J. E. 1991. Putative virulence factors of Candida albicans. Annu. Rev. Microbiol. 45:187-218.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 187-218
    • Cutler, J.E.1
  • 60
    • 0021925713 scopus 로고
    • Generation of leukotrienes by human monocytes upon stimulation of their β-glucan receptor during phagocytosis
    • Czop, J. K., and K. F. Austen. 1985. Generation of leukotrienes by human monocytes upon stimulation of their β-glucan receptor during phagocytosis. Proc. Natl. Acad. Sci. USA 82:2751-2755.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2751-2755
    • Czop, J.K.1    Austen, K.F.2
  • 61
    • 0025292155 scopus 로고
    • Production and isolation of rabbit anti-idiotypic antibodies directed against the human monocyte receptor for yeast β-glucans
    • Czop, J. K., M. F. Gurish, and J. L. Kadish. 1990. Production and isolation of rabbit anti-idiotypic antibodies directed against the human monocyte receptor for yeast β-glucans. J. Immunol. 145:995-1001.
    • (1990) J. Immunol. , vol.145 , pp. 995-1001
    • Czop, J.K.1    Gurish, M.F.2    Kadish, J.L.3
  • 62
    • 0023161259 scopus 로고
    • Separation of benzoylated oligosaccharides by reversed-phase high-pressure liquid chromatography: Application to high-mannose type oligosaccharides
    • Daniel, P. F. 1987. Separation of benzoylated oligosaccharides by reversed-phase high-pressure liquid chromatography: application to high-mannose type oligosaccharides. Methods Enzymol. 138:94-117.
    • (1987) Methods Enzymol. , vol.138 , pp. 94-117
    • Daniel, P.F.1
  • 63
    • 0001756052 scopus 로고
    • Quantitative microanalysis of oligosaccharides by high-performance liquid chromatography
    • Daniel, P. F., D. F. De Feudis, I. T. Lott, and R. H. McCluer. 1981. Quantitative microanalysis of oligosaccharides by high-performance liquid chromatography. Carbohydr. Res. 97:161-180.
    • (1981) Carbohydr. Res. , vol.97 , pp. 161-180
    • Daniel, P.F.1    De Feudis, D.F.2    Lott, I.T.3    McCluer, R.H.4
  • 64
    • 0032938979 scopus 로고    scopus 로고
    • Asparagine-linked glycosylation in the yeast Golgi
    • Dean, N. 1999. Asparagine-linked glycosylation in the yeast Golgi. Biochim. Biophys. Acta 1426:309-322.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 309-322
    • Dean, N.1
  • 66
    • 0026550939 scopus 로고
    • Flow cytometric analyses of lectin binding to Pneumocystis carinii surface carbohydrates
    • De Stefano, J. A., L. S. Trinkle, P. D. Walzer, and M. T. Cushion. 1992. Flow cytometric analyses of lectin binding to Pneumocystis carinii surface carbohydrates. J. Parasitol. 78:271-280.
    • (1992) J. Parasitol. , vol.78 , pp. 271-280
    • De Stefano, J.A.1    Trinkle, L.S.2    Walzer, P.D.3    Cushion, M.T.4
  • 67
    • 0000701007 scopus 로고
    • On the composition of zymosan
    • Di Carlo, F. J., and J. V. Fiore. 1958. On the composition of zymosan. Science 127:756-757.
    • (1958) Science , vol.127 , pp. 756-757
    • Di Carlo, F.J.1    Fiore, J.V.2
  • 69
    • 0027185637 scopus 로고
    • Allergens of Pityrosporon ovale and Candida albicans. II. Physicochemical characterization
    • Doekes, G., M. J. H. Kaal, and A. G. van Ieperen-van Dijk. 1993. Allergens of Pityrosporon ovale and Candida albicans. II. Physicochemical characterization. Allergy 48:401-408.
    • (1993) Allergy , vol.48 , pp. 401-408
    • Doekes, G.1    Kaal, M.J.H.2    Van Ieperen-Van Dijk, A.G.3
  • 70
    • 0024369367 scopus 로고
    • Candida cell wall mannan: A polysaccharide with diverse immunologic properties
    • Domer, J. E. 1989. Candida cell wall mannan: a polysaccharide with diverse immunologic properties. Crit. Rev. Microbiol. 17:33-51.
    • (1989) Crit. Rev. Microbiol. , vol.17 , pp. 33-51
    • Domer, J.E.1
  • 72
    • 0023104068 scopus 로고
    • Galactomannan antigenemia and antigenuria in aspergillosis: Studies in patients and experimentally infected rabbits
    • Dupont, B., M. Huber, S. J. Kim, and J. E. Bennett. 1987. Galactomannan antigenemia and antigenuria in aspergillosis: studies in patients and experimentally infected rabbits. J. Infect. Dis. 155:1-11.
    • (1987) J. Infect. Dis. , vol.155 , pp. 1-11
    • Dupont, B.1    Huber, M.2    Kim, S.J.3    Bennett, J.E.4
  • 75
    • 0029996036 scopus 로고    scopus 로고
    • Recent advances in capillary electrophoresis of carbohydrates
    • El Rassi, Z., and Y. Mechref. 1996. Recent advances in capillary electrophoresis of carbohydrates. Electrophoresis 17:275-301.
    • (1996) Electrophoresis , vol.17 , pp. 275-301
    • El Rassi, Z.1    Mechref, Y.2
  • 76
    • 0000985549 scopus 로고
    • The antigenic composition of Cryptococcus neoformans. II. Serologic studies with the capsular polysaccharide
    • Evans, E. E., and J. F. Kessel. 1951. The antigenic composition of Cryptococcus neoformans. II. Serologic studies with the capsular polysaccharide. J. Immunol. 67:109-114.
    • (1951) J. Immunol. , vol.67 , pp. 109-114
    • Evans, E.E.1    Kessel, J.F.2
  • 77
    • 0028880654 scopus 로고
    • Purification of 2-aminopyridine derivatives of oligosaccharides and related compounds by cation-exchange chromatography
    • Fan, J.-Q., L. H. Huynh, and Y. C. Lee. 1995. Purification of 2-aminopyridine derivatives of oligosaccharides and related compounds by cation-exchange chromatography. Anal. Biochem. 232:65-68.
    • (1995) Anal. Biochem. , vol.232 , pp. 65-68
    • Fan, J.-Q.1    Huynh, L.H.2    Lee, Y.C.3
  • 78
    • 0026732921 scopus 로고
    • A comparison of specific IgG antibody levels to the cell wall mannan of Candida albicans in normal individuals and in patients with primary antibody deficiency
    • Faux, J. A., A. E. Agbarakwe, S. A. Misbah, and H. M. Chapel. 1992. A comparison of specific IgG antibody levels to the cell wall mannan of Candida albicans in normal individuals and in patients with primary antibody deficiency. J. Immunol. Methods 153:167-172.
    • (1992) J. Immunol. Methods , vol.153 , pp. 167-172
    • Faux, J.A.1    Agbarakwe, A.E.2    Misbah, S.A.3    Chapel, H.M.4
  • 79
    • 0027171741 scopus 로고
    • Tumour necrosis factor production in vivo and in vitro in response to Paracoccidioides brasiliensis and the cell wall fractions thereof
    • Figueiredo, F., L. M. C. Alves, and C. L. Silva. 1993. Tumour necrosis factor production in vivo and in vitro in response to Paracoccidioides brasiliensis and the cell wall fractions thereof. Clin. Exp. Immunol. 93:189-194.
    • (1993) Clin. Exp. Immunol. , vol.93 , pp. 189-194
    • Figueiredo, F.1    Alves, L.M.C.2    Silva, C.L.3
  • 80
    • 0027192868 scopus 로고
    • Isogenic strain construction and gene mapping in Candida albicans
    • Fonzi, W. A., and M. Y. Irwin. 1993. Isogenic strain construction and gene mapping in Candida albicans. Genetics 134:717-728.
    • (1993) Genetics , vol.134 , pp. 717-728
    • Fonzi, W.A.1    Irwin, M.Y.2
  • 81
    • 0036157962 scopus 로고    scopus 로고
    • Lymphocyte adhesion to Candida albicans
    • Forsyth, C. B., and H. L. Matthews. 2002. Lymphocyte adhesion to Candida albicans. Infect. Immun. 70:517-527.
    • (2002) Infect. Immun. , vol.70 , pp. 517-527
    • Forsyth, C.B.1    Matthews, H.L.2
  • 83
    • 0033914833 scopus 로고    scopus 로고
    • β-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
    • Fradin, C., D. Poulain, and T. Jouault. 2000. β-1,2-Linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3. Infect. Immun. 68:4391-4398.
    • (2000) Infect. Immun. , vol.68 , pp. 4391-4398
    • Fradin, C.1    Poulain, D.2    Jouault, T.3
  • 84
    • 0032191166 scopus 로고    scopus 로고
    • The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity
    • Fraser, I. P., H. Koziel, and R. A. B. Ezekowitz. 1998. The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. Semin. Immunol. 10:363-372.
    • (1998) Semin. Immunol. , vol.10 , pp. 363-372
    • Fraser, I.P.1    Koziel, H.2    Ezekowitz, R.A.B.3
  • 85
    • 0037231976 scopus 로고    scopus 로고
    • Alternative sources of reagents and supplies for fluorophore-assisted carbohydrate electrophoresis (FACE)
    • Gao, N., and M. A. Lehrman. 2003. Alternative sources of reagents and supplies for fluorophore-assisted carbohydrate electrophoresis (FACE). Glycobiology 13:1G-3G.
    • (2003) Glycobiology , vol.13
    • Gao, N.1    Lehrman, M.A.2
  • 86
    • 0029909326 scopus 로고    scopus 로고
    • Intravenous injection of Candida-derived mannan results in elevated tumor necrosis factor alpha levels in serum
    • Garner, R. E., and J. A. Hudson. 1996. Intravenous injection of Candida-derived mannan results in elevated tumor necrosis factor alpha levels in serum. Infect. Immun. 64:4561-4566.
    • (1996) Infect. Immun. , vol.64 , pp. 4561-4566
    • Garner, R.E.1    Hudson, J.A.2
  • 87
    • 0028012419 scopus 로고
    • Secretion of TNF-α by alveolar macrophages in response to Candida albicans mannan
    • Garner, R. E., K. Rubanowice, R. T. Sawyer, and J. A. Hudson. 1994. Secretion of TNF-α by alveolar macrophages in response to Candida albicans mannan. J. Leukoc. Biol. 55:161-168.
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 161-168
    • Garner, R.E.1    Rubanowice, K.2    Sawyer, R.T.3    Hudson, J.A.4
  • 88
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmill, T. R., and R. B. Trimble. 1999. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426:227-237.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 91
    • 0030001592 scopus 로고    scopus 로고
    • Cost analysis of Candida infection among surgical intensive care unit patients
    • Goff, D. A., S. J. Sierawski, and R. J. Fass. 1996. Cost analysis of Candida infection among surgical intensive care unit patients. Clin. Drug Investig. 12:176-180.
    • (1996) Clin. Drug Investig. , vol.12 , pp. 176-180
    • Goff, D.A.1    Sierawski, S.J.2    Fass, R.J.3
  • 92
    • 0033903216 scopus 로고    scopus 로고
    • Relative abundance of oligosaccharides in Candida species as determined by fluorophore-assisted carbohydrate electrophoresis
    • Goins, T. L., and J. E. Cutler. 2000. Relative abundance of oligosaccharides in Candida species as determined by fluorophore-assisted carbohydrate electrophoresis. J. Clin. Microbiol. 38:2862-2869.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 2862-2869
    • Goins, T.L.1    Cutler, J.E.2
  • 93
    • 0001866587 scopus 로고
    • Protein-carbohydrate interaction. I. The interaction of polysaccharides with concanavalin A
    • Goldstein, I. J., C. E. Hollerman, and J. M. Merrick. 1965. Protein-carbohydrate interaction. I. The interaction of polysaccharides with concanavalin A. Biochim. Biophys. Acta 97:68-76.
    • (1965) Biochim. Biophys. Acta , vol.97 , pp. 68-76
    • Goldstein, I.J.1    Hollerman, C.E.2    Merrick, J.M.3
  • 94
    • 2042509519 scopus 로고
    • The structure and resistance to methylation of 1,2-β-glucans from species of agrobacteria
    • Gorin, P. A. J., J. F. T. Spencer, and D. W. S. Westlake. 1961. The structure and resistance to methylation of 1,2-β-glucans from species of agrobacteria. Can. J. Chem. 39:1067-1073.
    • (1961) Can. J. Chem. , vol.39 , pp. 1067-1073
    • Gorin, P.A.J.1    Spencer, J.F.T.2    Westlake, D.W.S.3
  • 95
    • 0031658804 scopus 로고    scopus 로고
    • Heterogeneity of glycans at each N-glycosylation site of horseradish peroxidase
    • Gray, J. S. S., B. Y. Yang, and R. Montgomery. 1998. Heterogeneity of glycans at each N-glycosylation site of horseradish peroxidase. Carbohydr. Res. 311:61-69.
    • (1998) Carbohydr. Res. , vol.311 , pp. 61-69
    • Gray, J.S.S.1    Yang, B.Y.2    Montgomery, R.3
  • 96
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile, G. R., P. M. Rudd, D. R. Wing, S. B. Prime, and R. A. Dwek. 1996. A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 240:210-226.
    • (1996) Anal. Biochem. , vol.240 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 97
    • 0028884861 scopus 로고
    • Capillary gel electrophoresis separation of high-mannose type oligosaccharides derivatized by 1-amino-3,6,8-trisulfonic acid
    • Guttman, A., and T. Pritchett. 1995. Capillary gel electrophoresis separation of high-mannose type oligosaccharides derivatized by 1-amino-3,6,8-trisulfonic acid. Electrophoresis 16:1906-1911.
    • (1995) Electrophoresis , vol.16 , pp. 1906-1911
    • Guttman, A.1    Pritchett, T.2
  • 98
    • 0037449795 scopus 로고    scopus 로고
    • Pneumocystis carinii cell wall β-glucan induces release of macrophage inflammatory protein-2 from alveolar epithelial cells via a lactosylceramide-mediated mechanism
    • Hahn, P. Y., S. E. Evans, T. J. Kottom, J. E. Standing, R. E. Pagano, and A. H. Limper. 2003. Pneumocystis carinii cell wall β-glucan induces release of macrophage inflammatory protein-2 from alveolar epithelial cells via a lactosylceramide-mediated mechanism. J. Biol. Chem. 278:2043-2050.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2043-2050
    • Hahn, P.Y.1    Evans, S.E.2    Kottom, T.J.3    Standing, J.E.4    Pagano, R.E.5    Limper, A.H.6
  • 99
    • 0021193309 scopus 로고
    • Structure of cell wall and extracellular mannans from Saccharomyces rouxii and their relationship to a high concentration of NaCl in the growth medium
    • Hamada, T., F. Noda, and K. Hayashi. 1984. Structure of cell wall and extracellular mannans from Saccharomyces rouxii and their relationship to a high concentration of NaCl in the growth medium. Appl. Environ. Microbiol. 50:708-712.
    • (1984) Appl. Environ. Microbiol. , vol.50 , pp. 708-712
    • Hamada, T.1    Noda, F.2    Hayashi, K.3
  • 100
    • 0029033902 scopus 로고
    • Antibody response that protects against disseminated candidiasis
    • Han, Y., and J. E. Cutler. 1995. Antibody response that protects against disseminated candidiasis. Infect. Immun. 63:2714-2719.
    • (1995) Infect. Immun. , vol.63 , pp. 2714-2719
    • Han, Y.1    Cutler, J.E.2
  • 101
    • 0030863412 scopus 로고    scopus 로고
    • Biochemical characterization of Candida albicans epitopes that can elicit protective and nonprotective antibodies
    • Han, Y., T. Kanbe, R. Cherniak, and J. E. Cutler. 1997. Biochemical characterization of Candida albicans epitopes that can elicit protective and nonprotective antibodies. Infect. Immun. 65:4100-4107.
    • (1997) Infect. Immun. , vol.65 , pp. 4100-4107
    • Han, Y.1    Kanbe, T.2    Cherniak, R.3    Cutler, J.E.4
  • 102
    • 0033983051 scopus 로고    scopus 로고
    • Protection against candidiasis by an immunoglobulin G3 (IgG3) monoclonal antibody specific for the same mannotriose as an IgM protective antibody
    • Han, Y., M. H. Riesselman, and J. E. Cutler. 2000. Protection against candidiasis by an immunoglobulin G3 (IgG3) monoclonal antibody specific for the same mannotriose as an IgM protective antibody. Infect. Immun. 68:1649-1654.
    • (2000) Infect. Immun. , vol.68 , pp. 1649-1654
    • Han, Y.1    Riesselman, M.H.2    Cutler, J.E.3
  • 103
    • 0032995552 scopus 로고    scopus 로고
    • Candida albicans mannan extract-protein conjugates induce a protective immune response against experimental candidiasis
    • Han, Y., M. A. Ulrich, and J. E. Cutler. 1999. Candida albicans mannan extract-protein conjugates induce a protective immune response against experimental candidiasis. J. Infect. Dis. 179:1477-1484.
    • (1999) J. Infect. Dis. , vol.179 , pp. 1477-1484
    • Han, Y.1    Ulrich, M.A.2    Cutler, J.E.3
  • 104
    • 0034924383 scopus 로고    scopus 로고
    • Facile sequencing of oligosaccharides by matrix-assisted laser desorption/ionisation on a hybrid quadrupole orthogonal acceleration time-of-flight mass spectrometer
    • Hanrahan, S., J. Charlwood, R. Tyldesley, J. Langridge, R. Bordoli, R. Bateman, and P. Camilleri. 2001. Facile sequencing of oligosaccharides by matrix-assisted laser desorption/ionisation on a hybrid quadrupole orthogonal acceleration time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 15:1141-1151.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1141-1151
    • Hanrahan, S.1    Charlwood, J.2    Tyldesley, R.3    Langridge, J.4    Bordoli, R.5    Bateman, R.6    Camilleri, P.7
  • 105
    • 73049138243 scopus 로고
    • Antigenic studies of Candida. I. Observation of two antigenic groups in Candida albicans
    • Hasenclever, H. F., and W. O. Mitchell. 1961. Antigenic studies of Candida. I. Observation of two antigenic groups in Candida albicans. J. Bacteriol. 82:570-573.
    • (1961) J. Bacteriol. , vol.82 , pp. 570-573
    • Hasenclever, H.F.1    Mitchell, W.O.2
  • 106
    • 0005921015 scopus 로고
    • Relationship of cell surface hydrophobicity to morphology of monomorphic and dimorphic fungi
    • Hazen, B. W., R. E. Liebert, and K. C. Hazen. 1988. Relationship of cell surface hydrophobicity to morphology of monomorphic and dimorphic fungi. Mycologia 80:348-355.
    • (1988) Mycologia , vol.80 , pp. 348-355
    • Hazen, B.W.1    Liebert, R.E.2    Hazen, K.C.3
  • 107
    • 0002470020 scopus 로고
    • Cell surface hydrophobicity of medically important fungi, especially Candida albicans
    • R. J. Doyle and M. Rosenberg (ed.). American Society for Microbiology, Washington, D.C.
    • Hazen, K. C. 1990. Cell surface hydrophobicity of medically important fungi, especially Candida albicans, p. 249-295. In R. J. Doyle and M. Rosenberg (ed.), Microbial cell surface hydrophobicity. American Society for Microbiology, Washington, D.C.
    • (1990) Microbial Cell Surface Hydrophobicity , pp. 249-295
    • Hazen, K.C.1
  • 108
    • 0026504439 scopus 로고
    • Hydrophobic surface protein masking by the opportunistic fungal pathogen Candida albicans
    • Hazen, K. C., and B. W. Hazen. 1992. Hydrophobic surface protein masking by the opportunistic fungal pathogen Candida albicans. Infect. Immun. 60:1499-1508.
    • (1992) Infect. Immun. , vol.60 , pp. 1499-1508
    • Hazen, K.C.1    Hazen, B.W.2
  • 109
    • 84907128665 scopus 로고
    • Identification of Candida albicans cell wall antigens lost during subculture in synthetic media
    • Hernando, F. L., J. J. Estevez, M. Cebrian, D. Poulain, and J. Ponton. 1993. Identification of Candida albicans cell wall antigens lost during subculture in synthetic media. J. Med. Vet. Mycol. 31:227-237.
    • (1993) J. Med. Vet. Mycol. , vol.31 , pp. 227-237
    • Hernando, F.L.1    Estevez, J.J.2    Cebrian, M.3    Poulain, D.4    Ponton, J.5
  • 110
    • 0036616606 scopus 로고    scopus 로고
    • The Golgi GDPase of the fungal pathogen Candida albicans affects morphogenesis, glycosylation, and cell wall properties
    • Herrero, A., B., D. Uccelletti, C. B. Hirschberg, A. Dominguez, and C. Abeijon. 2002. The Golgi GDPase of the fungal pathogen Candida albicans affects morphogenesis, glycosylation, and cell wall properties. Eukaryotic Cell 1:420-431.
    • (2002) Eukaryotic Cell , vol.1 , pp. 420-431
    • Herrero, A.1    Uccelletti, D.2    Hirschberg, C.B.3    Dominguez, A.4    Abeijon, C.5
  • 111
    • 0027279655 scopus 로고
    • Fungal β-glucans modulate macrophage release of tumor necrosis factor-α in response to bacterial lipopolysaccharide
    • Hoffman, O. A., E. J. Olson, and A. H. Limper. 1993. Fungal β-glucans modulate macrophage release of tumor necrosis factor-α in response to bacterial lipopolysaccharide. Immunol. Lett. 37:19-25.
    • (1993) Immunol. Lett. , vol.37 , pp. 19-25
    • Hoffman, O.A.1    Olson, E.J.2    Limper, A.H.3
  • 112
    • 0000527108 scopus 로고
    • Influence of borate complexation on the electrophoretic behavior of carbohydrates in capillary electrophoresis
    • Hofstetter-Kuhn, S., A. Paulus, E. Gassmann, and H. M. Widmer. 1991. Influence of borate complexation on the electrophoretic behavior of carbohydrates in capillary electrophoresis. Anal. Chem. 63:1541-1547.
    • (1991) Anal. Chem. , vol.63 , pp. 1541-1547
    • Hofstetter-Kuhn, S.1    Paulus, A.2    Gassmann, E.3    Widmer, H.M.4
  • 113
    • 0024355993 scopus 로고
    • High-performance liquid chromatography of reducing carbohydrates as strongly ultraviolet-absorbing and electrochemically sensitive 1-phenyl-3-methyl-5-pyrolazone derivatives
    • Honda, S., E. Akao, S. Suzuki, M. Okuda, K. Kakehi, and J. Nakamura. 1989. High-performance liquid chromatography of reducing carbohydrates as strongly ultraviolet-absorbing and electrochemically sensitive 1-phenyl-3-methyl-5-pyrolazone derivatives. Anal. Biochem. 180:351-357.
    • (1989) Anal. Biochem. , vol.180 , pp. 351-357
    • Honda, S.1    Akao, E.2    Suzuki, S.3    Okuda, M.4    Kakehi, K.5    Nakamura, J.6
  • 114
    • 0024534028 scopus 로고
    • Simultaneous determination of reducing monosaccharides by capillary zone electrophoresis as a borate complex of n-2-pyridylglycamines
    • Honda, S., S. Iwase, A. Makino, and S. Fujiwara. 1989. Simultaneous determination of reducing monosaccharides by capillary zone electrophoresis as a borate complex of n-2-pyridylglycamines. Anal. Biochem. 176:72-77.
    • (1989) Anal. Biochem. , vol.176 , pp. 72-77
    • Honda, S.1    Iwase, S.2    Makino, A.3    Fujiwara, S.4
  • 115
    • 0028098182 scopus 로고
    • Adhesins and ligands involved in the interaction of Candida spp. with epithelial and endothelial surfaces
    • Hostetter, M. K. 1994. Adhesins and ligands involved in the interaction of Candida spp. with epithelial and endothelial surfaces. Clin. Microbiol. Rev. 7:29-42.
    • (1994) Clin. Microbiol. Rev. , vol.7 , pp. 29-42
    • Hostetter, M.K.1
  • 116
    • 0031624098 scopus 로고    scopus 로고
    • Characterization of protein glycosylation
    • E. F. Hounsell (ed.). Humana Press, Totowa, N.J.
    • Hounsell, E. F. 1998. Characterization of protein glycosylation, p. 1-18. In E. F. Hounsell (ed.), Glycoanalysis protocols, 2nd ed. Humana Press, Totowa, N.J.
    • (1998) Glycoanalysis Protocols, 2nd Ed. , pp. 1-18
    • Hounsell, E.F.1
  • 118
    • 0034683072 scopus 로고    scopus 로고
    • High resolution of oligosaccharide mixtures by ultrahigh voltage micellar electrokinetic capillary chromatography
    • Hutterer, K. M., H. Birrell, P. Camilleri, and J. W. Jorgenson. 2000. High resolution of oligosaccharide mixtures by ultrahigh voltage micellar electrokinetic capillary chromatography. J. Chromatogr. 745:365-272.
    • (2000) J. Chromatogr. , vol.745 , pp. 365-272
    • Hutterer, K.M.1    Birrell, H.2    Camilleri, P.3    Jorgenson, J.W.4
  • 119
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali, B., and S. E. O'Connor. 1999. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3:643-649.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 120
    • 0035993213 scopus 로고    scopus 로고
    • Relationship between the physical properties of Candida albicans cell wall β-glucan and activation of leukocytes in vitro
    • Ishibashi, K.-I., N. N. Miura, Y. Adachi, N. Ogura, H. Tamura, S. Tanaka, and N. Ohno. 2002. Relationship between the physical properties of Candida albicans cell wall β-glucan and activation of leukocytes in vitro. Int. Immunopharmacol. 2:1109-1122.
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1109-1122
    • Ishibashi, K.-I.1    Miura, N.N.2    Adachi, Y.3    Ogura, N.4    Tamura, H.5    Tanaka, S.6    Ohno, N.7
  • 122
    • 0035012169 scopus 로고    scopus 로고
    • New assay for measuring cell surface hydrophobicities of Candida dubliniensis and Candida albicans
    • Jabra-Rizk, M. A., W. A. Falkler, Jr., W. G. Merz, and T. F. Meiller. 2001. New assay for measuring cell surface hydrophobicities of Candida dubliniensis and Candida albicans. Clin. Diagn. Lab. Immunol. 8:585-587.
    • (2001) Clin. Diagn. Lab. Immunol. , vol.8 , pp. 585-587
    • Jabra-Rizk, M.A.1    Falkler Jr., W.A.2    Merz, W.G.3    Meiller, T.F.4
  • 123
    • 0028327131 scopus 로고
    • The analysis of fluorophore-labeled glycans by high-resolution polyacrylamide gel electrophoresis
    • Jackson, P. 1994. The analysis of fluorophore-labeled glycans by high-resolution polyacrylamide gel electrophoresis. Anal. Biochem. 216:243-252.
    • (1994) Anal. Biochem. , vol.216 , pp. 243-252
    • Jackson, P.1
  • 124
    • 0028294887 scopus 로고
    • High-resolution polyacrylamide gel electrophoresis of fluorophore-labeled reducing saccharides
    • Jackson, P. 1994. High-resolution polyacrylamide gel electrophoresis of fluorophore-labeled reducing saccharides. Methods Enzymol. 230:250-265.
    • (1994) Methods Enzymol. , vol.230 , pp. 250-265
    • Jackson, P.1
  • 125
    • 0025708306 scopus 로고
    • The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1,3,6-trisulphonic acid
    • Jackson, P. 1990. The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1,3,6-trisulphonic acid. Biochem. J. 270:705-713.
    • (1990) Biochem. J. , vol.270 , pp. 705-713
    • Jackson, P.1
  • 126
    • 0028147836 scopus 로고
    • The use of polyacrylamide gel electrophoresis for the analysis of acidic glycans labeled with the fluorophore 2-aminoacridone
    • Jackson, P., M. G. Pluskal, and W. Skea. 1994. The use of polyacrylamide gel electrophoresis for the analysis of acidic glycans labeled with the fluorophore 2-aminoacridone. Electrophoresis 15:896-902.
    • (1994) Electrophoresis , vol.15 , pp. 896-902
    • Jackson, P.1    Pluskal, M.G.2    Skea, W.3
  • 127
    • 0026023303 scopus 로고
    • Polyacrylamide gel electrophoresis of reducing saccharides labeled with the fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid: Application to the enzymological structural analysis of oligosaccharides
    • Jackson, P., and G. R. Williams. 1991. Polyacrylamide gel electrophoresis of reducing saccharides labeled with the fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid: Application to the enzymological structural analysis of oligosaccharides. Electrophoresis 12:94-96.
    • (1991) Electrophoresis , vol.12 , pp. 94-96
    • Jackson, P.1    Williams, G.R.2
  • 128
    • 0031791617 scopus 로고    scopus 로고
    • Nature of Candida albicans-derived carbohydrate antigen recognized by a monoclonal antibody in patient sera and distribution over Candida species
    • Jacquinot, P. M., Y. Plancke, B. Sendid, G. Strecker, and D. Poulain. 1998. Nature of Candida albicans-derived carbohydrate antigen recognized by a monoclonal antibody in patient sera and distribution over Candida species. FEMS Microbiol. Lett. 169:131-138.
    • (1998) FEMS Microbiol. Lett. , vol.169 , pp. 131-138
    • Jacquinot, P.M.1    Plancke, Y.2    Sendid, B.3    Strecker, G.4    Poulain, D.5
  • 130
    • 0023245729 scopus 로고
    • Lysosomal enzyme release from human monocytes by particulate activators is mediated by β-glucan inhibitable receptors
    • Janusz, M. J., K. F. Austen, and J. K. Czop. 1987. Lysosomal enzyme release from human monocytes by particulate activators is mediated by β-glucan inhibitable receptors. J. Immunol. 138:3897-3901.
    • (1987) J. Immunol. , vol.138 , pp. 3897-3901
    • Janusz, M.J.1    Austen, K.F.2    Czop, J.K.3
  • 131
    • 0026579896 scopus 로고
    • Predominant pathogens in hospital infections
    • Jarvis, W. R., and W. J. Martone. 1992. Predominant pathogens in hospital infections. J. Antimicrob. Chemother. 29:19-24.
    • (1992) J. Antimicrob. Chemother. , vol.29 , pp. 19-24
    • Jarvis, W.R.1    Martone, W.J.2
  • 132
    • 0034731821 scopus 로고    scopus 로고
    • A mannose-binding protein from the cell surface of flocculent Saccharomyces cereivsiae (NCIM 3528): Its role in flocculation
    • Javadekar, V. S., H. Sivaraman, R. Sainkar, and M. I. Khan. 2000. A mannose-binding protein from the cell surface of flocculent Saccharomyces cereivsiae (NCIM 3528): its role in flocculation. Yeast 16:99-110.
    • (2000) Yeast , vol.16 , pp. 99-110
    • Javadekar, V.S.1    Sivaraman, H.2    Sainkar, R.3    Khan, M.I.4
  • 133
    • 0025275210 scopus 로고
    • Coaggregation of Streptococcus sanguis and other streptococci with Candida albicans
    • Jenkinson, H. F., H. C. Lala, and M. G. Shepherd. 1990. Coaggregation of Streptococcus sanguis and other streptococci with Candida albicans. Infect. Immun. 58:1429-1436.
    • (1990) Infect. Immun. , vol.58 , pp. 1429-1436
    • Jenkinson, H.F.1    Lala, H.C.2    Shepherd, M.G.3
  • 134
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft, N. 1990. Why are proteins O-glycosylated? Trends Biol. Sci. 15:291-294.
    • (1990) Trends Biol. Sci. , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 135
    • 0345211500 scopus 로고    scopus 로고
    • Flocculation of Saccharomyces cerevisiae
    • Jin, Y.-L., and R. A. Speers. 1999. Flocculation of Saccharomyces cerevisiae. Food Res. Int. 31:421-440.
    • (1999) Food Res. Int. , vol.31 , pp. 421-440
    • Jin, Y.-L.1    Speers, R.A.2
  • 136
    • 0015686877 scopus 로고
    • Acute hematogenous pyelonephritis induced in the rabbit with Saccharomyces cerevisiae
    • Johnston, W. H., and H. Latta. 1973. Acute hematogenous pyelonephritis induced in the rabbit with Saccharomyces cerevisiae. Lab. Investig. 29:495-505.
    • (1973) Lab. Investig. , vol.29 , pp. 495-505
    • Johnston, W.H.1    Latta, H.2
  • 137
    • 0014409077 scopus 로고
    • Isolation of an α-mannosidase which hydrolyzes yeast mannan
    • Jones, G. H., and C. E. Ballou. 1968. Isolation of an α-mannosidase which hydrolyzes yeast mannan. J. Biol. Chem. 243:2442-2446.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2442-2446
    • Jones, G.H.1    Ballou, C.E.2
  • 138
    • 0014669410 scopus 로고
    • Studies on the structure of yeast mannan. I. Purification and some properties of an α-mannosidase from an Arthrobacter species
    • Jones, G. H., and C. E. Ballou. 1969. Studies on the structure of yeast mannan. I. Purification and some properties of an α-mannosidase from an Arthrobacter species. J. Biol. Chem. 244:1043-1051.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1043-1051
    • Jones, G.H.1    Ballou, C.E.2
  • 139
    • 0014669440 scopus 로고
    • Studies on the structure of yeast mannan. II. Mode of action of the Arthrobacter α-mannosidase on yeast mannan
    • Jones, G. H., and C. E. Ballou. 1969. Studies on the structure of yeast mannan. II. Mode of action of the Arthrobacter α-mannosidase on yeast mannan. J. Biol. Chem. 244:1052-1059.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1052-1059
    • Jones, G.H.1    Ballou, C.E.2
  • 140
    • 0013685071 scopus 로고
    • Use of a real-time fluorescent probe to study the electrostatic properties of the cell surface of Candida albicans
    • Jones, L., C. Hobden, and P. O'Shea. 1995. Use of a real-time fluorescent probe to study the electrostatic properties of the cell surface of Candida albicans. Mycol. Res. 99:969-976.
    • (1995) Mycol. Res. , vol.99 , pp. 969-976
    • Jones, L.1    Hobden, C.2    O'Shea, P.3
  • 141
    • 0031655385 scopus 로고    scopus 로고
    • Early signal transduction induced by Candida albicans in macrophages through shedding of a glycolipid
    • Jouault, T., C. Fradin, P.-A. Trinel, A. Bernigaud, and D. Poulain. 1998. Early signal transduction induced by Candida albicans in macrophages through shedding of a glycolipid. J. Infect. Dis. 178:792-802.
    • (1998) J. Infect. Dis. , vol.178 , pp. 792-802
    • Jouault, T.1    Fradin, C.2    Trinel, P.-A.3    Bernigaud, A.4    Poulain, D.5
  • 142
    • 0033979231 scopus 로고    scopus 로고
    • Candida albicans-derived β-1,2-linked mannooligosaccharides induce desensitization of macrophages
    • Jouault, T., C. Fradin, P.-A. Trinel, and D. Poulain. 2000. Candida albicans-derived β-1,2-linked mannooligosaccharides induce desensitization of macrophages. Infect. Immun. 68:965-968.
    • (2000) Infect. Immun. , vol.68 , pp. 965-968
    • Jouault, T.1    Fradin, C.2    Trinel, P.-A.3    Poulain, D.4
  • 144
    • 0028299782 scopus 로고
    • Evidence for adhesin activity in the acid-stable moiety of the phosphomannoprotein cell wall complex of Candida albicans
    • Kanbe, T., and J. E. Cutler. 1994. Evidence for adhesin activity in the acid-stable moiety of the phosphomannoprotein cell wall complex of Candida albicans. Infect. Immun. 62:1662-1668.
    • (1994) Infect. Immun. , vol.62 , pp. 1662-1668
    • Kanbe, T.1    Cutler, J.E.2
  • 145
    • 0031741913 scopus 로고    scopus 로고
    • Minimum chemical requirements for adhesion activity of the acid-stable part of Candida albicans cell wall phosphomannoprotein complex
    • Kanbe, T., and J. E. Cutler. 1998. Minimum chemical requirements for adhesion activity of the acid-stable part of Candida albicans cell wall phosphomannoprotein complex. Infect. Immun. 66:5812-5818.
    • (1998) Infect. Immun. , vol.66 , pp. 5812-5818
    • Kanbe, T.1    Cutler, J.E.2
  • 146
    • 0027223406 scopus 로고
    • Evidence that mannans of Candida albicans are responsible for adherence of yeast forms to spleen and lymph node tissue
    • Kanbe, T., Y. Han, B. Redgrave, M. H. Riesselman, and J. E. Cutler. 1993. Evidence that mannans of Candida albicans are responsible for adherence of yeast forms to spleen and lymph node tissue. Infect. Immun. 61:2578-2584.
    • (1993) Infect. Immun. , vol.61 , pp. 2578-2584
    • Kanbe, T.1    Han, Y.2    Redgrave, B.3    Riesselman, M.H.4    Cutler, J.E.5
  • 147
    • 0026762956 scopus 로고
    • Evidence that Candida albicans binds via a unique adhesion system on phagocytic cells in the marginal zone of the mouse spleen
    • Kanbe, T., M. A. Jutila, and J. E. Cutler. 1992. Evidence that Candida albicans binds via a unique adhesion system on phagocytic cells in the marginal zone of the mouse spleen. Infect. Immun. 60:1972-1978.
    • (1992) Infect. Immun. , vol.60 , pp. 1972-1978
    • Kanbe, T.1    Jutila, M.A.2    Cutler, J.E.3
  • 148
    • 0014759913 scopus 로고
    • Cell wall glucans of the yeast and mycelial forms of Paracoccidioides brasiliensis
    • Kanetsuna, F., and L. M. Carbonell. 1970. Cell wall glucans of the yeast and mycelial forms of Paracoccidioides brasiliensis. J. Bacteriol. 101:675-680.
    • (1970) J. Bacteriol. , vol.101 , pp. 675-680
    • Kanetsuna, F.1    Carbonell, L.M.2
  • 149
    • 0014478815 scopus 로고
    • Cell wall composition of the yeast and mycelial forms of Paracoccidioides brasiliensis
    • Kanetsuna, F., L. M. Carbonell, R. E. Moreno, and J. Rodriguez. 1969. Cell wall composition of the yeast and mycelial forms of Paracoccidioides brasiliensis. J. Bacteriol. 97:1036-1041.
    • (1969) J. Bacteriol. , vol.97 , pp. 1036-1041
    • Kanetsuna, F.1    Carbonell, L.M.2    Moreno, R.E.3    Rodriguez, J.4
  • 151
    • 0028980292 scopus 로고
    • Covalent association of β-1,3-glucan with β-1,6-glucosylated mannoproteins in cell walls of Candida albicans
    • Kapteyn, J. C., R. C. Montijn, G. J. P. Dijkgraaf, H. Van den Ende, and F. M. Klis. 1995. Covalent association of β-1,3-glucan with β-1,6-glucosylated mannoproteins in cell walls of Candida albicans. J. Bacteriol. 177:3788-3792.
    • (1995) J. Bacteriol. , vol.177 , pp. 3788-3792
    • Kapteyn, J.C.1    Montijn, R.C.2    Dijkgraaf, G.J.P.3    Van Den Ende, H.4    Klis, F.M.5
  • 152
  • 153
    • 0030844713 scopus 로고    scopus 로고
    • Altered extent of cross-linking of β1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall β1,3-glucan content
    • Kapteyn, J. C., A. F. J. Ram, E. M. Groos, R. Kollar, R. C. Montijn, H. van den Ende, A. Llobell, E. Cabib, and F. M. Klis. 1997. Altered extent of cross-linking of β1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall β1,3-glucan content. J. Bacteriol. 179:6279-6284.
    • (1997) J. Bacteriol. , vol.179 , pp. 6279-6284
    • Kapteyn, J.C.1    Ram, A.F.J.2    Groos, E.M.3    Kollar, R.4    Montijn, R.C.5    Van Den Ende, H.6    Llobell, A.7    Cabib, E.8    Klis, F.M.9
  • 154
    • 0037184115 scopus 로고    scopus 로고
    • Activation of macrophages by linear (1-3)-β-D-glucans. Implications for the recognition of fungi by innate immunity
    • Kataoka, K., T. Muta, S. Yamazaki, and K. Takeshige. 2002. Activation of macrophages by linear (1-3)-β-D-glucans. Implications for the recognition of fungi by innate immunity. J. Biol. Chem. 277:36825-36831.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36825-36831
    • Kataoka, K.1    Muta, T.2    Yamazaki, S.3    Takeshige, K.4
  • 155
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Kelm, S., and R. Schauer. 1997. Sialic acids in molecular and cellular interactions. Int. Rev. Cytol. 175:137-240.
    • (1997) Int. Rev. Cytol. , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 156
    • 0022729223 scopus 로고
    • Reconstitution of the masking effect of sialic acid groups on sialidase-treated erythrocytes by the action of sialyltransferases
    • Kelm, S., A. K. Shukla, J. C. Paulson, and R. Schauer. 1986. Reconstitution of the masking effect of sialic acid groups on sialidase-treated erythrocytes by the action of sialyltransferases. Carbohydr. Res. 149:59-64.
    • (1986) Carbohydr. Res. , vol.149 , pp. 59-64
    • Kelm, S.1    Shukla, A.K.2    Paulson, J.C.3    Schauer, R.4
  • 158
    • 0011948092 scopus 로고
    • Glucomannan-protein complexes from cell walls of yeast
    • Kessler, G., and W. J. Nickerson. 1959. Glucomannan-protein complexes from cell walls of yeast. J. Biol. Chem. 234:2281-2285.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2281-2285
    • Kessler, G.1    Nickerson, W.J.2
  • 159
    • 0036711405 scopus 로고    scopus 로고
    • Maturation of dendritic cells induced by Candida β-D-glucan
    • Kikuchi, T., N. Ohno, and T. Ohno. 2002. Maturation of dendritic cells induced by Candida β-D-glucan. Int. Immunopharmacol. 2:1503-1508.
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1503-1508
    • Kikuchi, T.1    Ohno, N.2    Ohno, T.3
  • 160
    • 0035812415 scopus 로고    scopus 로고
    • 2-(hydroxycarbonyl)benzyl glycosides: A novel type of glycosyl donors for highly efficient β-mannopyranosylation and oligosaccharide synthesis by latent-active glycosylation
    • Kim, K. S., J. H. Kim, Y. J. Lee, Y. J. Lee, and J. Park. 2001. 2-(Hydroxycarbonyl)benzyl glycosides: a novel type of glycosyl donors for highly efficient β-mannopyranosylation and oligosaccharide synthesis by latent-active glycosylation. J. Am. Chem. Soc. 123:8477-8481.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8477-8481
    • Kim, K.S.1    Kim, J.H.2    Lee, Y.J.3    Lee, Y.J.4    Park, J.5
  • 161
    • 0035659952 scopus 로고    scopus 로고
    • Molecular organization of the cell wall of Candida albicans
    • Klis, F. M., P. de Groot, and K. Hellingwerf. 2001. Molecular organization of the cell wall of Candida albicans. Med. Mycol. 39:1-8.
    • (2001) Med. Mycol. , vol.39 , pp. 1-8
    • Klis, F.M.1    De Groot, P.2    Hellingwerf, K.3
  • 165
    • 0026639283 scopus 로고
    • Structural study of a cell wall mannan-protein complex of the pathogenic yeast Candida glabrata IFO 0622 strain
    • Kobayashi, H., H. Mitobe, K. Takahashi, T. Yamamoto, N. Shibata, and S. Suzuki. 1992. Structural study of a cell wall mannan-protein complex of the pathogenic yeast Candida glabrata IFO 0622 strain. Arch. Biochem. Biophys. 294:662-669.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 662-669
    • Kobayashi, H.1    Mitobe, H.2    Takahashi, K.3    Yamamoto, T.4    Shibata, N.5    Suzuki, S.6
  • 166
    • 0024720498 scopus 로고
    • Structural study of phosphomannan of yeast-form cells of Candida albicans J-1012 strain with special reference to application of mild acetolysis
    • Kobayashi, H., N. Shibata, H. Mitobe, Y. Ohkubo, and S. Suzuki. 1989. Structural study of phosphomannan of yeast-form cells of Candida albicans J-1012 strain with special reference to application of mild acetolysis. Arch. Biochem. Biophys. 272:364-375.
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 364-375
    • Kobayashi, H.1    Shibata, N.2    Mitobe, H.3    Ohkubo, Y.4    Suzuki, S.5
  • 169
    • 0027957269 scopus 로고
    • Structural modification of cell wall mannans of Candida albicans serotype A strains grown in yeast extract-Sabouraud liquid medium under acidic conditions
    • Kobayashi, H., S. Takahashi, N. Shibata, M. Miyauchi, M. Ishida, J. Sato, K. Maeda, and S. Suzuki. 1994. Structural modification of cell wall mannans of Candida albicans serotype A strains grown in yeast extract-Sabouraud liquid medium under acidic conditions. Infect. Immun. 62:968-973.
    • (1994) Infect. Immun. , vol.62 , pp. 968-973
    • Kobayashi, H.1    Takahashi, S.2    Shibata, N.3    Miyauchi, M.4    Ishida, M.5    Sato, J.6    Maeda, K.7    Suzuki, S.8
  • 170
    • 0037292538 scopus 로고    scopus 로고
    • Candida albicans cell wall antigens for serological diagnosis of candademia
    • Kondori, N., L. Edebo, and I. Mattsby-Baltzer. 2003. Candida albicans cell wall antigens for serological diagnosis of candademia. Med. Mycol. 41:21-30.
    • (2003) Med. Mycol. , vol.41 , pp. 21-30
    • Kondori, N.1    Edebo, L.2    Mattsby-Baltzer, I.3
  • 171
    • 0036151240 scopus 로고    scopus 로고
    • Comparison of biofilms formed by Candida albicans and Candida parapsilosis on bioprosthetic surfaces
    • Kuhn, D. M., J. Chandra, P. K. Mukherjee, and M. A. Ghannoum. 2002. Comparison of biofilms formed by Candida albicans and Candida parapsilosis on bioprosthetic surfaces. Infect. Immun. 70:878-888.
    • (2002) Infect. Immun. , vol.70 , pp. 878-888
    • Kuhn, D.M.1    Chandra, J.2    Mukherjee, P.K.3    Ghannoum, M.A.4
  • 172
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
    • Küster, B., S. F. Wheeler, A. P. Hunter, R. A. Dwek, and D. J. Harvey. 1997. Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal. Biochem. 250:82-101.
    • (1997) Anal. Biochem. , vol.250 , pp. 82-101
    • Küster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 173
    • 0038783497 scopus 로고    scopus 로고
    • Derivatization of carbohydrates for chromatographic, electrophoretic and mass spectrometric structure analysis
    • Lamari, F. N., R. Kuhn, and N. K. Karamanos. 2003. Derivatization of carbohydrates for chromatographic, electrophoretic and mass spectrometric structure analysis. J. Chromatogr. Ser. B 793:15-36.
    • (2003) J. Chromatogr. Ser. B , vol.793 , pp. 15-36
    • Lamari, F.N.1    Kuhn, R.2    Karamanos, N.K.3
  • 176
    • 0041589276 scopus 로고    scopus 로고
    • Pneumocystis carinii cell wall β-glucans initiate macrophage inflammatory responses through NF-κB activation
    • Lebron, F., R. Vassallo, V. Puri, and A. H. Limper. 2003. Pneumocystis carinii cell wall β-glucans initiate macrophage inflammatory responses through NF-κB activation. J. Biol. Chem. 278:25001-25008.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25001-25008
    • Lebron, F.1    Vassallo, R.2    Puri, V.3    Limper, A.H.4
  • 177
    • 0024986576 scopus 로고
    • Influence of sialic acids on the galactose-recognizing receptor of rat peritoneal macrophages
    • Lee, H., S. Kelm, J.-C. Michalski, and R. Schauer. 1990. Influence of sialic acids on the galactose-recognizing receptor of rat peritoneal macrophages. Biol. Chem. Hoppe-Seyler 371:307-316.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 307-316
    • Lee, H.1    Kelm, S.2    Michalski, J.-C.3    Schauer, R.4
  • 178
    • 0036741450 scopus 로고    scopus 로고
    • Systemic candidiasis in intensive care units: A multicenter, matched-cohort study
    • Leleu, G., P. Aegerter, and B. Guidet. 2002. Systemic candidiasis in intensive care units: a multicenter, matched-cohort study. J. Crit. Care 17:168-175.
    • (2002) J. Crit. Care , vol.17 , pp. 168-175
    • Leleu, G.1    Aegerter, P.2    Guidet, B.3
  • 179
    • 0027290863 scopus 로고
    • Chemical definition of an epitope/adhesion molecule on Candida albicans
    • Li, R.-K., and J. E. Cutler. 1993. Chemical definition of an epitope/adhesion molecule on Candida albicans. J. Biol. Chem. 268:18293-18299.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18293-18299
    • Li, R.-K.1    Cutler, J.E.2
  • 180
    • 0014199519 scopus 로고
    • Studies on the glycosidases in Jack Bean meal. I. Isolation and properties of α-mannosidase
    • Li, Y.-T. 1967. Studies on the glycosidases in Jack Bean meal. I. Isolation and properties of α-mannosidase. J. Biol. Chem. 242:5474-5480.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5474-5480
    • Li, Y.-T.1
  • 181
    • 0031830365 scopus 로고    scopus 로고
    • Cell wall architecture in yeast: New structure and new challenges
    • Lipke, P. N., and R. Ovalle. 1998. Cell wall architecture in yeast: new structure and new challenges. J. Bacteriol. 180:3735-3740.
    • (1998) J. Bacteriol. , vol.180 , pp. 3735-3740
    • Lipke, P.N.1    Ovalle, R.2
  • 182
    • 0027519943 scopus 로고
    • Protein glycosylation
    • Lis, H., and N. Sharon. 1993. Protein glycosylation. Eur. J. Biochem. 218:1-27.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 183
    • 0028809398 scopus 로고
    • Preliminary characterization of the material released to the culture medium by Candida albicans yeast and mycelial cells
    • López-Ribot, J. L., D. Gozalbo, P. Sepúlveda, M. Casanova, and J. P. Martínez. 1995. Preliminary characterization of the material released to the culture medium by Candida albicans yeast and mycelial cells. Antonie Leeuwenhoek 68:195-201.
    • (1995) Antonie Leeuwenhoek , vol.68 , pp. 195-201
    • López-Ribot, J.L.1    Gozalbo, D.2    Sepúlveda, P.3    Casanova, M.4    Martínez, J.P.5
  • 184
    • 0019523437 scopus 로고
    • Role of surface mannans in the adherence of Candida albicans to fibrin-platelet clots formed in vitro
    • Maisch, P. A., and R. A. Calderone. 1981. Role of surface mannans in the adherence of Candida albicans to fibrin-platelet clots formed in vitro. Infect. Immun. 32:92-97.
    • (1981) Infect. Immun. , vol.32 , pp. 92-97
    • Maisch, P.A.1    Calderone, R.A.2
  • 185
    • 0037087305 scopus 로고    scopus 로고
    • Optimal T cell responses to Cryptococcus neoformans mannoprotein are dependent on recognition of conjugated carbohydrates by mannose receptors
    • Mansour, M. K., L. S. Schlesinger, and S. M. Levitz. 2002. Optimal T cell responses to Cryptococcus neoformans mannoprotein are dependent on recognition of conjugated carbohydrates by mannose receptors. J. Immunol. 168:2872-2879.
    • (2002) J. Immunol. , vol.168 , pp. 2872-2879
    • Mansour, M.K.1    Schlesinger, L.S.2    Levitz, S.M.3
  • 186
    • 0021265218 scopus 로고
    • Ultrastructure of Candida parapsilosis endocarditis
    • Marrie, T. J., J. H. Cooper, and J. W. Costerton. 1984. Ultrastructure of Candida parapsilosis endocarditis. Infect. Immun. 45:390-398.
    • (1984) Infect. Immun. , vol.45 , pp. 390-398
    • Marrie, T.J.1    Cooper, J.H.2    Costerton, J.W.3
  • 187
    • 0021352336 scopus 로고
    • Scanning and transmission electron microscopy of in situ bacterial colonization of intravenous and intraarterial catheters
    • Marrie, T. J., and J. W. Costerton. 1984. Scanning and transmission electron microscopy of in situ bacterial colonization of intravenous and intraarterial catheters. J. Clin. Microbiol. 19:687-693.
    • (1984) J. Clin. Microbiol. , vol.19 , pp. 687-693
    • Marrie, T.J.1    Costerton, J.W.2
  • 188
    • 0019644145 scopus 로고
    • The ultrastructure of Candida albicans infections
    • Marrie, T. J., and J. W. Costerton. 1981. The ultrastructure of Candida albicans infections. Can. J. Microbiol. 27:1156-1164.
    • (1981) Can. J. Microbiol. , vol.27 , pp. 1156-1164
    • Marrie, T.J.1    Costerton, J.W.2
  • 189
    • 0031984061 scopus 로고    scopus 로고
    • Serologic response to cell wall mannoproteins and proteins of Candida albicans
    • Martínez, J. P., M. L. Gil, J. L. López-Ribot, and W. L. Chaffin. 1998. Serologic response to cell wall mannoproteins and proteins of Candida albicans. Clin. Microbiol. Rev. 11:121-141.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 121-141
    • Martínez, J.P.1    Gil, M.L.2    López-Ribot, J.L.3    Chaffin, W.L.4
  • 190
    • 0034278282 scopus 로고    scopus 로고
    • The aman6 gene encoding a yeast mannan backbone degrading 1,6-α-D-mannanase in Bacillus circulans: Cloning, sequence analysis, and expression
    • Maruyama, Y., and T. Nakajima. 2000. The aman6 gene encoding a yeast mannan backbone degrading 1,6-α-D-mannanase in Bacillus circulans: cloning, sequence analysis, and expression. Biosci. Biotechnol. Biochem. 64:2018-2020.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2018-2020
    • Maruyama, Y.1    Nakajima, T.2
  • 191
    • 0030763261 scopus 로고    scopus 로고
    • Cell wall mannosylation determines Candida albicans cell surface hydrophobicity
    • Masuoka, J., and K. C. Hazen. 1997. Cell wall mannosylation determines Candida albicans cell surface hydrophobicity. Microbiology 143:3015-3021.
    • (1997) Microbiology , vol.143 , pp. 3015-3021
    • Masuoka, J.1    Hazen, K.C.2
  • 192
    • 0038442248 scopus 로고    scopus 로고
    • Orthoester-based strategy for efficient synthesis of virulent antigenic-1,2-linked oligomannans of Candida albicans
    • Mathew, F., M. Mach, K. C. Hazen, and B. Fraser-Reid. 2003. Orthoester-based strategy for efficient synthesis of virulent antigenic-1,2-linked oligomannans of Candida albicans. Synlett 2003:1319-1322.
    • (2003) Synlett , vol.2003 , pp. 1319-1322
    • Mathew, F.1    Mach, M.2    Hazen, K.C.3    Fraser-Reid, B.4
  • 195
    • 0026729502 scopus 로고
    • Role of specific determinants in mannan of Candida albicans serotype A in adherence to human buccal epithelial cells
    • Miyakawa, Y., T. Kuribayashi, K. Kagaya, M. Suzuki, T. Nakase, and Y. Fukazawa. 1992. Role of specific determinants in mannan of Candida albicans serotype A in adherence to human buccal epithelial cells. Infect. Immun. 60:2493-2499.
    • (1992) Infect. Immun. , vol.60 , pp. 2493-2499
    • Miyakawa, Y.1    Kuribayashi, T.2    Kagaya, K.3    Suzuki, M.4    Nakase, T.5    Fukazawa, Y.6
  • 196
    • 0026675438 scopus 로고
    • G test, a new direct method for diagnosis of Candida infection: Comparison with assays for beta-glucan and mannan antigen in a rabbit model of systemic candidiasis
    • Miyazaki, T., S. Kohno, H. Koga, M. Kaku, K. Mitsutake, S. Maesaki, A. Yasuoka, K. Hara, S. Tanaka, and H. Tamura. 1992. G test, a new direct method for diagnosis of Candida infection: comparison with assays for beta-glucan and mannan antigen in a rabbit model of systemic candidiasis. J. Clin. Lab. Anal. 6:315-318.
    • (1992) J. Clin. Lab. Anal. , vol.6 , pp. 315-318
    • Miyazaki, T.1    Kohno, S.2    Koga, H.3    Kaku, M.4    Mitsutake, K.5    Maesaki, S.6    Yasuoka, A.7    Hara, K.8    Tanaka, S.9    Tamura, H.10
  • 197
    • 0038752760 scopus 로고    scopus 로고
    • Lectin typing of five medically important Candida species
    • Muñoz, A., B. Alonso, O. Alvarez, and J. Llovo. 2001. Lectin typing of five medically important Candida species. Mycoses 46:85-89.
    • (2001) Mycoses , vol.46 , pp. 85-89
    • Muñoz, A.1    Alonso, B.2    Alvarez, O.3    Llovo, J.4
  • 198
    • 0027281060 scopus 로고
    • CR3 (CD11b/CD18) expressed by cytotoxic T cells and natural killer cells is upregulated in a manner similar to neutrophil CR3 following stimulation with various agents
    • Muto, S., V. Vetvicka, and G. D. Ross. 1993. CR3 (CD11b/CD18) expressed by cytotoxic T cells and natural killer cells is upregulated in a manner similar to neutrophil CR3 following stimulation with various agents. J. Clin. Immunol. 13:175-184.
    • (1993) J. Clin. Immunol. , vol.13 , pp. 175-184
    • Muto, S.1    Vetvicka, V.2    Ross, G.D.3
  • 199
    • 0017302630 scopus 로고
    • An endo-α1-6-D-mannanase from a soil bacterium
    • Nakajima, T., S. K. Maitra, and C. E. Ballou. 1976. An endo-α1-6-D-mannanase from a soil bacterium. J. Biol. Chem. 251:174-181.
    • (1976) J. Biol. Chem. , vol.251 , pp. 174-181
    • Nakajima, T.1    Maitra, S.K.2    Ballou, C.E.3
  • 200
    • 0037089473 scopus 로고    scopus 로고
    • Analysis of oligosaccharide structures of glycoproteins in polyacrylamide gel
    • Nakakita, S., D. Ama, S. Natsuka, and S. Hase. 2002. Analysis of oligosaccharide structures of glycoproteins in polyacrylamide gel. Anal. Biochem. 303:206-209.
    • (2002) Anal. Biochem. , vol.303 , pp. 206-209
    • Nakakita, S.1    Ama, D.2    Natsuka, S.3    Hase, S.4
  • 201
    • 0028331701 scopus 로고
    • Quantitative assay of (1-3)-β-D-glucan in culture media of Candida albicans using the G-test
    • Nakao, A., H. Kato, T. Kanbe, K. Tanaka, H. Tamura, S. Tanaka, and H. Takagi. 1994. Quantitative assay of (1-3)-β-D-glucan in culture media of Candida albicans using the G-test. Eur. Surg. Res. 26:194-200.
    • (1994) Eur. Surg. Res. , vol.26 , pp. 194-200
    • Nakao, A.1    Kato, H.2    Kanbe, T.3    Tanaka, K.4    Tamura, H.5    Tanaka, S.6    Takagi, H.7
  • 202
    • 0026021979 scopus 로고
    • Candida mannan: Chemistry, supression of cell-mediated immunity, and possible mechanism of action
    • Nelson, R. D., N. Shibata, R. P. Podzorski, and M. J. Herron. 1991. Candida mannan: chemistry, supression of cell-mediated immunity, and possible mechanism of action. Clin. Microbiol. Rev. 4:1-19.
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 1-19
    • Nelson, R.D.1    Shibata, N.2    Podzorski, R.P.3    Herron, M.J.4
  • 203
    • 0030026474 scopus 로고    scopus 로고
    • A comparison of the development of antibody responses to the polysaccharide antigen (Candida albicans mannan) in atopic and healthy infants and children
    • Nermes, M., K. Fälth-Magnusson, J. Savolainen, M. Viander, and B. Björkstén. 1996. A comparison of the development of antibody responses to the polysaccharide antigen (Candida albicans mannan) in atopic and healthy infants and children. Clin. Exp. Allergy 26:164-170.
    • (1996) Clin. Exp. Allergy , vol.26 , pp. 164-170
    • Nermes, M.1    Fälth-Magnusson, K.2    Savolainen, J.3    Viander, M.4    Björkstén, B.5
  • 204
    • 0033547946 scopus 로고    scopus 로고
    • Facile syntheses of a hexasaccharide and a nonasaccharide related to the cell wall D-mannan of yeast Candida albicans
    • Ning, J., and F. Kong. 1999. Facile syntheses of a hexasaccharide and a nonasaccharide related to the cell wall D-mannan of yeast Candida albicans. Tetrahedron Lett. 40:1357-1360.
    • (1999) Tetrahedron Lett. , vol.40 , pp. 1357-1360
    • Ning, J.1    Kong, F.2
  • 205
    • 0035861619 scopus 로고    scopus 로고
    • Synthesis of di- to hexasaccharide 1,2-linked β3-mannopyranan oligomers, a terminal S-linked tetrasaccharide congener and the corresponding BSA glycoconjugates
    • Nitz, M., and D. R. Bundle. 2001. Synthesis of di- to hexasaccharide 1,2-linked β3-mannopyranan oligomers, a terminal S-linked tetrasaccharide congener and the corresponding BSA glycoconjugates. J. Org. Chem. 66:8411-8423.
    • (2001) J. Org. Chem. , vol.66 , pp. 8411-8423
    • Nitz, M.1    Bundle, D.R.2
  • 206
    • 0034699271 scopus 로고    scopus 로고
    • Synthesis of a β1,2-mannopyranosyl tetrasaccharide found in the phosphomannan antigen of Candida albicans
    • Nitz, M., B. W. Purse, and D. R. Bundle. 2000. Synthesis of a β1,2-mannopyranosyl tetrasaccharide found in the phosphomannan antigen of Candida albicans. Org. Lett. 2:2939-2942.
    • (2000) Org. Lett. , vol.2 , pp. 2939-2942
    • Nitz, M.1    Purse, B.W.2    Bundle, D.R.3
  • 207
    • 0020657614 scopus 로고
    • Ingestion of yeast forms of Sporothrix schenckii by mouse peritoneal macrophages
    • Oda, L. M., C. F. Kubelka, C. S. Alviano, and L. R. Travassos. 1893. Ingestion of yeast forms of Sporothrix schenckii by mouse peritoneal macrophages. Infect. Immun. 39:497-504.
    • (1893) Infect. Immun. , vol.39 , pp. 497-504
    • Oda, L.M.1    Kubelka, C.F.2    Alviano, C.S.3    Travassos, L.R.4
  • 208
    • 0004246866 scopus 로고
    • University Park Press, Baltimore, Md.
    • Odds, F. C. 1979. Candida and candidosis. University Park Press, Baltimore, Md.
    • (1979) Candida and Candidosis
    • Odds, F.C.1
  • 210
    • 0019639665 scopus 로고
    • Immunochemical study on bakers' yeast mannan prepared by fractional precipitation with cetylmethylammonium bromide
    • Okubo, Y., N. Shibata, T. Ichikawa, S. Chaki, and S. Suzuki. 1981. Immunochemical study on bakers' yeast mannan prepared by fractional precipitation with cetylmethylammonium bromide. Arch. Biochem. Biophys. 212: 204-215.
    • (1981) Arch. Biochem. Biophys. , vol.212 , pp. 204-215
    • Okubo, Y.1    Shibata, N.2    Ichikawa, T.3    Chaki, S.4    Suzuki, S.5
  • 211
    • 0342424714 scopus 로고    scopus 로고
    • The mnn2 mutant of Saccharomyces cerevisiae is affected in phosphorylation of N-linked oligosaccharides
    • Olivero, I., P. Mañas, and L. M. Hernández. 2000. The mnn2 mutant of Saccharomyces cerevisiae is affected in phosphorylation of N-linked oligosaccharides. FEBS Lett. 475:111-116.
    • (2000) FEBS Lett. , vol.475 , pp. 111-116
    • Olivero, I.1    Mañas, P.2    Hernández, L.M.3
  • 212
    • 0029849098 scopus 로고    scopus 로고
    • Fungal β-glucan interacts with vitronectin and stimulates tumor necrosis factor alpha release from macrophages
    • Olson, E. J., J. E. Standing, N. Griego-Harper, O. A. Hoffman, and A. H. Limper. 1996. Fungal β-glucan interacts with vitronectin and stimulates tumor necrosis factor alpha release from macrophages. Infect. Immun. 64:3548-3554.
    • (1996) Infect. Immun. , vol.64 , pp. 3548-3554
    • Olson, E.J.1    Standing, J.E.2    Griego-Harper, N.3    Hoffman, O.A.4    Limper, A.H.5
  • 213
    • 0032053318 scopus 로고    scopus 로고
    • The ultrastructure of yeast: Cell wall structure and formation
    • Osumi, M. 1998. The ultrastructure of yeast: cell wall structure and formation. Micron 29:207-233.
    • (1998) Micron , vol.29 , pp. 207-233
    • Osumi, M.1
  • 214
    • 0029143283 scopus 로고
    • Molecular and biochemical characterization of a Coccidioides immitis-specific antigen
    • Pan, S., and G. T. Cole. 1995. Molecular and biochemical characterization of a Coccidioides immitis-specific antigen. Infect. Immun. 63:3994-4002.
    • (1995) Infect. Immun. , vol.63 , pp. 3994-4002
    • Pan, S.1    Cole, G.T.2
  • 215
    • 0028325770 scopus 로고
    • Release of oligosaccharides from glycoproteins by hydrazinolysis
    • Patel, T. P., and R. B. Parekh. 1994. Release of oligosaccharides from glycoproteins by hydrazinolysis. Methods Enzymol. 230:57-66.
    • (1994) Methods Enzymol. , vol.230 , pp. 57-66
    • Patel, T.P.1    Parekh, R.B.2
  • 216
    • 0001998071 scopus 로고
    • Neutral polysaccharides
    • M. F. Chaplin and J. F. Kennedy (ed.). IRL Press, Washington, D.C.
    • Pazur, J. H. 1986. Neutral polysaccharides, p. 55-96. In M. F. Chaplin and J. F. Kennedy (ed.), Carbohydrate analysis: a practical approach. IRL Press, Washington, D.C.
    • (1986) Carbohydrate Analysis: A Practical Approach , pp. 55-96
    • Pazur, J.H.1
  • 217
    • 37049042230 scopus 로고
    • Polysaccharides of baker's yeast. IV. Mannan
    • Peat, S., W. J. Whelan, and T. E. Edwards. 1961. Polysaccharides of baker's yeast. IV. Mannan. J. Chem. Soc. 1961:29-34.
    • (1961) J. Chem. Soc. , vol.1961 , pp. 29-34
    • Peat, S.1    Whelan, W.J.2    Edwards, T.E.3
  • 218
    • 0028997468 scopus 로고
    • Adherence of Candida albicans to host cells
    • Pendrak, M. L., and S. A. Klotz. 1995. Adherence of Candida albicans to host cells. FEMS Microbiol. Lett. 129:103-114.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 103-114
    • Pendrak, M.L.1    Klotz, S.A.2
  • 219
    • 0036792188 scopus 로고    scopus 로고
    • Role of sentinel surveillance of candidemia: Trends in species distribution and antifungal susceptibility
    • Pfaller, M. A., and D. J. Diekema. 2002. Role of sentinel surveillance of candidemia: trends in species distribution and antifungal susceptibility. J. Clin. Microbiol. 40:3551-3557.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 3551-3557
    • Pfaller, M.A.1    Diekema, D.J.2
  • 220
    • 0031939508 scopus 로고    scopus 로고
    • National surveillance of nosocomial blood stream infection due to species of Candida other than Candida albicans: Frequency of occurrence and antifungal susceptibility in the SCOPE program
    • Pfaller, M. A., R. N. Jones, S. A. Messer, M. B. Edmond, R. P. Wenzel, and SCOPE Participant Group. 1998. National surveillance of nosocomial blood stream infection due to species of Candida other than Candida albicans: frequency of occurrence and antifungal susceptibility in the SCOPE program. Diagn. Microbiol. Infect. Dis. 30:121-129.
    • (1998) Diagn. Microbiol. Infect. Dis. , vol.30 , pp. 121-129
    • Pfaller, M.A.1    Jones, R.N.2    Messer, S.A.3    Edmond, M.B.4    Wenzel, R.P.5
  • 221
    • 0034931506 scopus 로고    scopus 로고
    • Spatial and temporal sequence of capsule construction in Cryptococcus neoformans
    • Pierini, L. M., and T. L. Doering. 2001. Spatial and temporal sequence of capsule construction in Cryptococcus neoformans. Mol. Microbiol. 41:105-115.
    • (2001) Mol. Microbiol. , vol.41 , pp. 105-115
    • Pierini, L.M.1    Doering, T.L.2
  • 222
    • 0001284072 scopus 로고
    • Anticomplementary factor in fresh yeast
    • Pillemer, L., and E. E. Ecker. 1941. Anticomplementary factor in fresh yeast. J. Biol. Chem. 137:139-142.
    • (1941) J. Biol. Chem. , vol.137 , pp. 139-142
    • Pillemer, L.1    Ecker, E.E.2
  • 223
    • 0031550280 scopus 로고    scopus 로고
    • Capillary zone electrophoresis of oligosaccharides derivatized with n-(4-aminobenzoyl)-1-glutamic acid for ultraviolet absorbance detection
    • Plocek, J., and M. V. Novotny. 1997. Capillary zone electrophoresis of oligosaccharides derivatized with n-(4-aminobenzoyl)-1-glutamic acid for ultraviolet absorbance detection. J. Chromatogr. Ser. A 757:215-223.
    • (1997) J. Chromatogr. Ser. A , vol.757 , pp. 215-223
    • Plocek, J.1    Novotny, M.V.2
  • 224
    • 0025014787 scopus 로고
    • Different effects of native Candida albicans mannan and mannan-derived oligosaccharides on antigen-stimulated lymphoproliferation in vitro
    • Podzorski, R. P., G. R. Gray, and R. D. Nelson. 1990. Different effects of native Candida albicans mannan and mannan-derived oligosaccharides on antigen-stimulated lymphoproliferation in vitro. J. Immunol. 144:707-716.
    • (1990) J. Immunol. , vol.144 , pp. 707-716
    • Podzorski, R.P.1    Gray, G.R.2    Nelson, R.D.3
  • 228
    • 0034255107 scopus 로고    scopus 로고
    • Electrophoretic methods for the analysis of N-linked oligosaccharides
    • Raju, T. S. 2000. Electrophoretic methods for the analysis of N-linked oligosaccharides. Anal. Biochem. 283:125-132.
    • (2000) Anal. Biochem. , vol.283 , pp. 125-132
    • Raju, T.S.1
  • 230
    • 0032788359 scopus 로고    scopus 로고
    • National epidemiology of mycoses survey (NEMIS): Variations in rates of bloodstream infections due to Candida species in seven surgical intensive care units and six neonatal intensive care units
    • Rangel-Frausto, M. S., T. Wiblin, H. M. Blumberg, L. Saiman, J. Patterson, M. Rinaldi, M. Pfaller, J. E. Edwards, Jr., W. Jarvis, J. Dawson, R. P. Wenzel, and NEMIS Group. 1999. National epidemiology of mycoses survey (NEMIS): variations in rates of bloodstream infections due to Candida species in seven surgical intensive care units and six neonatal intensive care units. Clin. Infect. Dis. 29:253-258.
    • (1999) Clin. Infect. Dis. , vol.29 , pp. 253-258
    • Rangel-Frausto, M.S.1    Wiblin, T.2    Blumberg, H.M.3    Saiman, L.4    Patterson, J.5    Rinaldi, M.6    Pfaller, M.7    Edwards Jr., J.E.8    Jarvis, W.9    Dawson, J.10    Wenzel, R.P.11
  • 231
    • 37049134708 scopus 로고
    • Polysaccharide conformation. VI. Computer model-building for linear and branched pyranoglycans. Correlations with biological function. Preliminary assessment of inter-residue forces in aqueous solution. Further interpretation of optical rotation in terms of chain conformation
    • Rees, D. A., and W. E. Scott. 1971. Polysaccharide conformation. VI. Computer model-building for linear and branched pyranoglycans. Correlations with biological function. Preliminary assessment of inter-residue forces in aqueous solution. Further interpretation of optical rotation in terms of chain conformation. J. Chem. Soc. Ser. B 1971:469-479.
    • (1971) J. Chem. Soc. Ser. B , vol.1971 , pp. 469-479
    • Rees, D.A.1    Scott, W.E.2
  • 234
    • 2442740075 scopus 로고    scopus 로고
    • The impact of candidemia on length of hospital stay, outcome, and overall cost of illness
    • Rentz, A. M., M. T. Halpern, and R. Bowden. 1998. The impact of candidemia on length of hospital stay, outcome, and overall cost of illness. Clin. Infect. Dis. 27:781-788.
    • (1998) Clin. Infect. Dis. , vol.27 , pp. 781-788
    • Rentz, A.M.1    Halpern, M.T.2    Bowden, R.3
  • 235
    • 0038494613 scopus 로고    scopus 로고
    • Cross-reactivity of the PLATELIA Candida antigen detection enzyme immunoassay with fungal antigen extracts
    • Rimek, D., J. Singh, and R. Kappe. 2003. Cross-reactivity of the PLATELIA Candida antigen detection enzyme immunoassay with fungal antigen extracts. J. Clin. Microbiol. 41:3395-3398.
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 3395-3398
    • Rimek, D.1    Singh, J.2    Kappe, R.3
  • 237
    • 0030840333 scopus 로고    scopus 로고
    • Identification of N-acetylneuraminic acid and its 9-O-acetylated derivative on the cell surface of Cryptococcus neoformans: Influence on fungal pathogenesis
    • Rodrigues, M. L., S. Rozental, J. N. S. S. Couceiro, J. Angluster, C. S. Alviano, and L. R. Travassos. 1997. Identification of N-acetylneuraminic acid and its 9-O-acetylated derivative on the cell surface of Cryptococcus neoformans: influence on fungal pathogenesis. Infect. Immun. 65:4937-4942.
    • (1997) Infect. Immun. , vol.65 , pp. 4937-4942
    • Rodrigues, M.L.1    Rozental, S.2    Couceiro, J.N.S.S.3    Angluster, J.4    Alviano, C.S.5    Travassos, L.R.6
  • 238
    • 0022003293 scopus 로고
    • 3) has lectin-like properties analagous to bovine conglutinin and functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for iC3b
    • 3) has lectin-like properties analagous to bovine conglutinin and functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for iC3b. J. Immunol. 135:3307-3315.
    • (1985) J. Immunol. , vol.135 , pp. 3307-3315
    • Ross, G.D.1    Cain, J.A.2    Lachmann, P.J.3
  • 244
    • 0023232165 scopus 로고
    • Studies on cell adhesion and concanavalin A-induced agglutination of Candida albicans after mannan extraction
    • Sandin, R. L. 1987. Studies on cell adhesion and concanavalin A-induced agglutination of Candida albicans after mannan extraction. J. Med. Microbiol. 24:145-150.
    • (1987) J. Med. Microbiol. , vol.24 , pp. 145-150
    • Sandin, R.L.1
  • 245
    • 0020052669 scopus 로고
    • Evidence for mannose-mediated adherence of Candida albicans to human buccal cells in vitro
    • Sandin, R. L., A. L. Rogers, R. J. Patterson, and E. S. Beneke. 1982. Evidence for mannose-mediated adherence of Candida albicans to human buccal cells in vitro. Infect. Immun. 35:79-85.
    • (1982) Infect. Immun. , vol.35 , pp. 79-85
    • Sandin, R.L.1    Rogers, A.L.2    Patterson, R.J.3    Beneke, E.S.4
  • 246
    • 0025309182 scopus 로고
    • Passive immunization against Cryptococcus neoformans with an isotype-switch family of monoclonal antibodies reactive with cryptococcal polysaccharide
    • Sanford, J. E., D. M. Lupan, A. M. Schlageter, and T. R. Kozel. 1990. Passive immunization against Cryptococcus neoformans with an isotype-switch family of monoclonal antibodies reactive with cryptococcal polysaccharide. Infect. Immun. 58:1919-1923.
    • (1990) Infect. Immun. , vol.58 , pp. 1919-1923
    • Sanford, J.E.1    Lupan, D.M.2    Schlageter, A.M.3    Kozel, T.R.4
  • 247
    • 0034654599 scopus 로고    scopus 로고
    • Microsequencing of glycans using 2-aminobenzamide and MALDI-TOF mass spectrometry: Occurrence of unique linkage-dependent fragmentation
    • Sato, Y., M. Suzuki, T. Nirasawa, A. Suzuki, and T. Endo. 2000. Microsequencing of glycans using 2-aminobenzamide and MALDI-TOF mass spectrometry: occurrence of unique linkage-dependent fragmentation. Anal. Chem. 72:1207-1216.
    • (2000) Anal. Chem. , vol.72 , pp. 1207-1216
    • Sato, Y.1    Suzuki, M.2    Nirasawa, T.3    Suzuki, A.4    Endo, T.5
  • 249
    • 0032997521 scopus 로고    scopus 로고
    • Candida albicans mannan- and protein-induced humoral, cellular and cytokine responses in atopic dermatitis patients
    • Savolainen, J., J. Kosonen, P. Lintu, M. Viander, J. Pène, K. Kalimo, E. O. Terho, and J. Bousquet. 1999. Candida albicans mannan- and protein-induced humoral, cellular and cytokine responses in atopic dermatitis patients. Clin. Exp. Allergy 29:824-831.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 824-831
    • Savolainen, J.1    Kosonen, J.2    Lintu, P.3    Viander, M.4    Pène, J.5    Kalimo, K.6    Terho, E.O.7    Bousquet, J.8
  • 250
    • 0025145435 scopus 로고
    • Altered hepatic clearance and killing of Candida albicans in the isolated perfused mouse liver model
    • Sawyer, R. T., M. N. Horst, R. E. Garner, J. Hudson, P. R. Jenkins, and A. L. Richardson. 1990. Altered hepatic clearance and killing of Candida albicans in the isolated perfused mouse liver model. Infect. Immun. 58: 2869-2874.
    • (1990) Infect. Immun. , vol.58 , pp. 2869-2874
    • Sawyer, R.T.1    Horst, M.N.2    Garner, R.E.3    Hudson, J.4    Jenkins, P.R.5    Richardson, A.L.6
  • 251
    • 0023880444 scopus 로고
    • Cell wall components of Candida albicans as immunomodulators: Induction of natural killer and macrophage-mediated peritoneal cell cytotoxicity in mice by mannoprotein and glucan fractions
    • Scaringi, L., P. Marconi, M. Boccanera, L. Tissi, F. Bistoni, and A. Cassone. 1988. Cell wall components of Candida albicans as immunomodulators: induction of natural killer and macrophage-mediated peritoneal cell cytotoxicity in mice by mannoprotein and glucan fractions. J. Gen. Microbiol. 134:1265-1274.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1265-1274
    • Scaringi, L.1    Marconi, P.2    Boccanera, M.3    Tissi, L.4    Bistoni, F.5    Cassone, A.6
  • 252
    • 77956696032 scopus 로고    scopus 로고
    • Chemistry, biochemistry and biology of sialic acids
    • J. Montreuil, J. F. G. Vliegenthart, and H. Schacter (ed.). Elsevier, New York, N.Y.
    • Schauer, R., and J. P. Kamerling. 1997. Chemistry, biochemistry and biology of sialic acids, p. 243-402. In J. Montreuil, J. F. G. Vliegenthart, and H. Schacter (ed.), Glycoproteins II. Elsevier, New York, N.Y.
    • (1997) Glycoproteins II , pp. 243-402
    • Schauer, R.1    Kamerling, J.P.2
  • 253
    • 0022329619 scopus 로고
    • Microbial adhesion to fibronectin in vitro correlates with production of endocarditis in rabbits
    • Scheld, W. M., R. W. Strunk, G. Balian, and R. A. Calderone. 1985. Microbial adhesion to fibronectin in vitro correlates with production of endocarditis in rabbits. Proc. Soc. Exp. Biol. Med. 180:474-482.
    • (1985) Proc. Soc. Exp. Biol. Med. , vol.180 , pp. 474-482
    • Scheld, W.M.1    Strunk, R.W.2    Balian, G.3    Calderone, R.A.4
  • 255
    • 0020077773 scopus 로고
    • Adherence of Candida albicans to human vaginal epithelial cells: Inhibition by amino sugars
    • Segal, E., N. Lehrer, and I. Ofek. 1982. Adherence of Candida albicans to human vaginal epithelial cells: Inhibition by amino sugars. Exp. Cell Biol. 50:13-17.
    • (1982) Exp. Cell Biol. , vol.50 , pp. 13-17
    • Segal, E.1    Lehrer, N.2    Ofek, I.3
  • 256
    • 0036235863 scopus 로고    scopus 로고
    • Combined detection of mannanaemia and anti-mannan antibodies as a strategy for the diagnosis of systemic infection caused by pathogenic Candida species
    • Sendid, B., J. L. Poirot, M. Tabouret, A. Bonnin, D. Caillot, D. Camus, and D. Poulain. 2002. Combined detection of mannanaemia and anti-mannan antibodies as a strategy for the diagnosis of systemic infection caused by pathogenic Candida species. J. Med. Microbiol. 51:433-442.
    • (2002) J. Med. Microbiol. , vol.51 , pp. 433-442
    • Sendid, B.1    Poirot, J.L.2    Tabouret, M.3    Bonnin, A.4    Caillot, D.5    Camus, D.6    Poulain, D.7
  • 257
    • 0032897577 scopus 로고    scopus 로고
    • New enzyme immunoassays for sensitive detection of circulating Candida albicans mannan and antimannan antibodies: Useful combined test for diagnosis of systemic candidiasis
    • Sendid, B., M. Tabouret, J. L. Poirot, D. Mathieu, J. Fruit, and D. Poulain. 1999. New enzyme immunoassays for sensitive detection of circulating Candida albicans mannan and antimannan antibodies: useful combined test for diagnosis of systemic candidiasis. J. Clin. Microbiol. 37:1510-1517.
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 1510-1517
    • Sendid, B.1    Tabouret, M.2    Poirot, J.L.3    Mathieu, D.4    Fruit, J.5    Poulain, D.6
  • 258
    • 0027339137 scopus 로고
    • Carbohydrates in cell recognition
    • Sharon, N., and H. Lis. 1993. Carbohydrates in cell recognition. Sci. Am. 268:82-89.
    • (1993) Sci. Am. , vol.268 , pp. 82-89
    • Sharon, N.1    Lis, H.2
  • 259
    • 0032527169 scopus 로고    scopus 로고
    • Structural characterization of carbohydrate sequence, linkage, and branching in a quadrupole ion trap mass spectrometer: Neutral oligosaccharides and N-linked glycans
    • Sheeley, D. M., and V. N. Reinhold. 1998. Structural characterization of carbohydrate sequence, linkage, and branching in a quadrupole ion trap mass spectrometer: neutral oligosaccharides and N-linked glycans. Anal. Chem. 70:3053-3059.
    • (1998) Anal. Chem. , vol.70 , pp. 3053-3059
    • Sheeley, D.M.1    Reinhold, V.N.2
  • 260
    • 0023493828 scopus 로고
    • Cell envelope of Candida albicans
    • Shepherd, M. G. 1987. Cell envelope of Candida albicans. Crit. Rev. Microbiol. 15:7-25.
    • (1987) Crit. Rev. Microbiol. , vol.15 , pp. 7-25
    • Shepherd, M.G.1
  • 261
    • 15844429888 scopus 로고    scopus 로고
    • Existence of novel branched side chains containing β-1,2 and α-1,6 linkages corresponding to antigenic factor 9 in the mannan of Candida guilliermondii
    • Shibata, N., R. Akagi, T. Hosoya, K. Kawahara, A. Suzuki, K. Ikuta, H. Kobayashi, K. Hisamichi, Y. Okawa, and S. Suzuki. 1996. Existence of novel branched side chains containing β-1,2 and α-1,6 linkages corresponding to antigenic factor 9 in the mannan of Candida guilliermondii. J. Biol. Chem. 271:9259-9266.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9259-9266
    • Shibata, N.1    Akagi, R.2    Hosoya, T.3    Kawahara, K.4    Suzuki, A.5    Ikuta, K.6    Kobayashi, H.7    Hisamichi, K.8    Okawa, Y.9    Suzuki, S.10
  • 262
    • 0026723084 scopus 로고
    • Structural identification of an epitope of antigenic factor 5 in mannans of Candida albicans NIH B-792 (serotype B) and J-1012 (serotype A) as α-1,2-linked oligomannosyl residues
    • Shibata, N., M. Arai, E. Haga, T. Kikuchi, M. Najima, T. Satoh, H. Kobayashi, and S. Suzuki. 1992. Structural identification of an epitope of antigenic factor 5 in mannans of Candida albicans NIH B-792 (serotype B) and J-1012 (serotype A) as α-1,2-linked oligomannosyl residues. Infect. Immun. 60:4100-4110.
    • (1992) Infect. Immun. , vol.60 , pp. 4100-4110
    • Shibata, N.1    Arai, M.2    Haga, E.3    Kikuchi, T.4    Najima, M.5    Satoh, T.6    Kobayashi, H.7    Suzuki, S.8
  • 263
    • 0024970256 scopus 로고
    • Structural analysis of phospho-D-mannan-protein complexes isolated from yeast and mold from cells of Candida albicans NIH A-207 serotype A strain
    • Shibata, N., S. Fukasawa, H. Kobayashi, M. Tojo, T. Yonezu, A. Ambo, Y. Ohkubo, and S. Suzuki. 1989. Structural analysis of phospho-D-mannan-protein complexes isolated from yeast and mold from cells of Candida albicans NIH A-207 serotype A strain. Carbohydr. Res. 187:239-253.
    • (1989) Carbohydr. Res. , vol.187 , pp. 239-253
    • Shibata, N.1    Fukasawa, S.2    Kobayashi, H.3    Tojo, M.4    Yonezu, T.5    Ambo, A.6    Ohkubo, Y.7    Suzuki, S.8
  • 265
    • 0026093891 scopus 로고
    • Structural study on a phosphorylated mannotetraose obtained from the phosphomannan of Candida albicans NIH B-792 strain by acetolysis
    • Shibata, N., H. Kobayashi, S. Takahashi, Y. Okawa, K. Hisamichi, and S. Suzuki. 1991. Structural study on a phosphorylated mannotetraose obtained from the phosphomannan of Candida albicans NIH B-792 strain by acetolysis. Arch. Biochem. Biophys. 290:535-542.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 535-542
    • Shibata, N.1    Kobayashi, H.2    Takahashi, S.3    Okawa, Y.4    Hisamichi, K.5    Suzuki, S.6
  • 266
    • 0030473158 scopus 로고    scopus 로고
    • Structure and antigenicity of the mannans of Candida famata and Candida saitoana: Comparative study with the mannan of Candida guilliermondii
    • Shibata, N., M. Onozawa, N. Tadano, Y. Hinosawa, A. Suzuki, K. Ikuta, H. Kobayashi, S. Suzuki, and Y. Okawa. 1996. Structure and antigenicity of the mannans of Candida famata and Candida saitoana: comparative study with the mannan of Candida guilliermondii. Arch. Biochem. Biophys. 336:49-58.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 49-58
    • Shibata, N.1    Onozawa, M.2    Tadano, N.3    Hinosawa, Y.4    Suzuki, A.5    Ikuta, K.6    Kobayashi, H.7    Suzuki, S.8    Okawa, Y.9
  • 267
    • 0035875372 scopus 로고    scopus 로고
    • Rapid and simple preparation of N-linked oligosaccharides by cellulose-column chromatography
    • Shimizu, Y., M. Nakata, Y. Kuroda, F. Tsutsumi, N. Kojima, and T. Mizuochi. 2001. Rapid and simple preparation of N-linked oligosaccharides by cellulose-column chromatography. Carbohydr. Res. 332:381-388.
    • (2001) Carbohydr. Res. , vol.332 , pp. 381-388
    • Shimizu, Y.1    Nakata, M.2    Kuroda, Y.3    Tsutsumi, F.4    Kojima, N.5    Mizuochi, T.6
  • 268
    • 0019430241 scopus 로고
    • Comparative evaluation of the latron serological Candida Check kit and the API 20C kit for identification of medically important Candida species
    • Shinoda, T., L. Kaufman, and A. A. Padhye. 1981. Comparative evaluation of the latron serological Candida Check kit and the API 20C kit for identification of medically important Candida species. J. Clin. Microbiol. 13:513-518.
    • (1981) J. Clin. Microbiol. , vol.13 , pp. 513-518
    • Shinoda, T.1    Kaufman, L.2    Padhye, A.A.3
  • 270
    • 0027449993 scopus 로고
    • Identification of sialic acids on the cell surface of hyphae and yeast forms of the human pathogen Paracoccidioides brasiliensis
    • Soares, R. M. A., C. S. Alviano, J. Angluster, and L. R. Travassos. 1993. Identification of sialic acids on the cell surface of hyphae and yeast forms of the human pathogen Paracoccidioides brasiliensis. FEMS Microbiol. Lett. 108:31-34.
    • (1993) FEMS Microbiol. Lett. , vol.108 , pp. 31-34
    • Soares, R.M.A.1    Alviano, C.S.2    Angluster, J.3    Travassos, L.R.4
  • 271
    • 2642676854 scopus 로고    scopus 로고
    • Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis
    • Soares, R. M. A., F. Costa e Silva-Filho, S. Rozental, J. Angluster, W. de Souza, C. S. Alviano, and L. R. Travassos. 1998. Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis. Microbiology 144:309-314.
    • (1998) Microbiology , vol.144 , pp. 309-314
    • Soares, R.M.A.1    Costa E Silva-Filho, F.2    Rozental, S.3    Angluster, J.4    De Souza, W.5    Alviano, C.S.6    Travassos, L.R.7
  • 273
    • 0021816099 scopus 로고
    • Epidemiology and pathogenesis of recurrent vulvovaginal candidiasis
    • Sobel, J. D. 1985. Epidemiology and pathogenesis of recurrent vulvovaginal candidiasis. Am. J. Obstet. Gynecol. 152:924-935.
    • (1985) Am. J. Obstet. Gynecol. , vol.152 , pp. 924-935
    • Sobel, J.D.1
  • 274
    • 0019448924 scopus 로고
    • Adherence of Candida albicans to human vaginal and buccal epithelial cells
    • Sobel, J. D., P. G. Myers, D. Kaye, and M. E. Levison. 1981. Adherence of Candida albicans to human vaginal and buccal epithelial cells. J. Infect. Dis. 143:76-82.
    • (1981) J. Infect. Dis. , vol.143 , pp. 76-82
    • Sobel, J.D.1    Myers, P.G.2    Kaye, D.3    Levison, M.E.4
  • 275
    • 0022411410 scopus 로고
    • Phagocytosis of unopsonized zymosan by human monocyte-derived macrophages: Maturation and inhibition by mannan
    • Speert, D. P., and S. C. Silverstein. 1985. Phagocytosis of unopsonized zymosan by human monocyte-derived macrophages: maturation and inhibition by mannan. J. Leukoc. Biol. 38:655-658.
    • (1985) J. Leukoc. Biol. , vol.38 , pp. 655-658
    • Speert, D.P.1    Silverstein, S.C.2
  • 276
    • 0028568541 scopus 로고
    • The emerging fungal threat
    • Sternberg, S. 1994. The emerging fungal threat. Science 266:1632-1634.
    • (1994) Science , vol.266 , pp. 1632-1634
    • Sternberg, S.1
  • 278
    • 0023893745 scopus 로고
    • Evidence for a glycosidic linkage between chitin and glucan in the cell wall of Candida albicans
    • Surarit, R., P. K. Gopal, and M. G. Shepherd. 1988. Evidence for a glycosidic linkage between chitin and glucan in the cell wall of Candida albicans. J. Gen. Microbiol. 134:1723-1730.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1723-1730
    • Surarit, R.1    Gopal, P.K.2    Shepherd, M.G.3
  • 279
    • 0021221857 scopus 로고
    • Protecting effect of chitin and chitosan on experimentally induced murine candidiasis
    • Suzuki, K., Y. Okawa, K. Hashimoto, S. Suzuki, and M. Suzuki. 1984. Protecting effect of chitin and chitosan on experimentally induced murine candidiasis. Microbiol. Immunol. 28:903-912.
    • (1984) Microbiol. Immunol. , vol.28 , pp. 903-912
    • Suzuki, K.1    Okawa, Y.2    Hashimoto, K.3    Suzuki, S.4    Suzuki, M.5
  • 280
    • 0023260089 scopus 로고
    • Candidacidal effect of peritoneal exudate cells in mice administered with chitin or chitosan: The role of seriene protease on the mechanism of oxygen-independent candidacidal effect
    • Suzuki, K., Y. Okawa, S. Suzuki, and M. Suzuki. 1987. Candidacidal effect of peritoneal exudate cells in mice administered with chitin or chitosan: the role of seriene protease on the mechanism of oxygen-independent candidacidal effect. Microbiol. Immunol. 31:375-379.
    • (1987) Microbiol. Immunol. , vol.31 , pp. 375-379
    • Suzuki, K.1    Okawa, Y.2    Suzuki, S.3    Suzuki, M.4
  • 281
    • 0020318122 scopus 로고
    • Immunochemical characterization of Candida albicans cell wall antigens: Specific determinant of Candida albicans serotype A mannan
    • Suzuki, M., and Y. Fukazawa. 1982. Immunochemical characterization of Candida albicans cell wall antigens: specific determinant of Candida albicans serotype A mannan. Microbiol. Immunol. 26:387-402.
    • (1982) Microbiol. Immunol. , vol.26 , pp. 387-402
    • Suzuki, M.1    Fukazawa, Y.2
  • 282
    • 0031304610 scopus 로고    scopus 로고
    • Immunochemical study on mannans of genus Candida. I. Structural investigation of antigenic factors 1, 4, 5, 6, 8, 9, 11, 13, 13b and 34
    • Suzuki, S. 1997. Immunochemical study on mannans of genus Candida. I. Structural investigation of antigenic factors 1, 4, 5, 6, 8, 9, 11, 13, 13b and 34. Curr. Top. Med. Mycol. 8:57-70.
    • (1997) Curr. Top. Med. Mycol. , vol.8 , pp. 57-70
    • Suzuki, S.1
  • 283
    • 0036841442 scopus 로고    scopus 로고
    • Primary dendritic cells phagocytose Cryptococcus neoformans via mannose receptors and Fcγ receptor II for presentation to T lymphocytes
    • Syme, R. M., J. C. L. Spurrell, E. K. Amankwah, F. H. Y. Green, and C. H. Mody. 2002. Primary dendritic cells phagocytose Cryptococcus neoformans via mannose receptors and Fcγ receptor II for presentation to T lymphocytes. Infect. Immun. 70:5972-5981.
    • (2002) Infect. Immun. , vol.70 , pp. 5972-5981
    • Syme, R.M.1    Spurrell, J.C.L.2    Amankwah, E.K.3    Green, F.H.Y.4    Mody, C.H.5
  • 284
    • 0028931998 scopus 로고
    • Biochemical properties of the ligand-binding 20-kDa subunit of the β-glucan receptor on human mononuclear phagocytes
    • Szabó, T., J. L. Kadish, and J. K. Czop. 1995. Biochemical properties of the ligand-binding 20-kDa subunit of the β-glucan receptor on human mononuclear phagocytes. J. Biol. Chem. 270:2145-2151.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2145-2151
    • Szabó, T.1    Kadish, J.L.2    Czop, J.K.3
  • 285
    • 0036170913 scopus 로고    scopus 로고
    • The direct costs of nosocomial catheter-associated urinary tract infection in the era of managed care
    • Tambyah, P. A., V. Knasinski, and D. G. Maki. 2002. The direct costs of nosocomial catheter-associated urinary tract infection in the era of managed care. Infect. Control Hosp. Epidemiol. 23:27-31.
    • (2002) Infect. Control Hosp. Epidemiol. , vol.23 , pp. 27-31
    • Tambyah, P.A.1    Knasinski, V.2    Maki, D.G.3
  • 286
    • 0024778571 scopus 로고
    • Enzymatic approaches for studying the structure, synthesis, and processing of glycoproteins
    • A. M. Tartakoff (ed.). Academic Press, Inc., San Diego, Calif.
    • Tarentino, A. L., R. B. Trimble, and T. H. Plummer, Jr. 1989. Enzymatic approaches for studying the structure, synthesis, and processing of glycoproteins, p. 111-139. In A. M. Tartakoff (ed.), Vesicular transport, part B. Academic Press, Inc., San Diego, Calif.
    • (1989) Vesicular Transport, Part B , pp. 111-139
    • Tarentino, A.L.1    Trimble, R.B.2    Plummer Jr., T.H.3
  • 287
    • 0026766923 scopus 로고
    • Analysis of carbohydrate-mediated heterogeneity and characterization of N-linked oligosaccharides of glycoproteins by high performance capillary electrophoresis
    • Taverna, M., A. Baillet, D. Biou, M. Schlüter, R. Werner, and D. Ferrier. 1992. Analysis of carbohydrate-mediated heterogeneity and characterization of N-linked oligosaccharides of glycoproteins by high performance capillary electrophoresis. Electrophoresis 13:359-366.
    • (1992) Electrophoresis , vol.13 , pp. 359-366
    • Taverna, M.1    Baillet, A.2    Biou, D.3    Schlüter, M.4    Werner, R.5    Ferrier, D.6
  • 288
    • 0022992575 scopus 로고
    • Ultrastructure of outermost layer of cell wall in Candida albicans observed by rapid-freezing technique
    • Tokunaga, M., M. Kusamichi, and H. Koike. 1986. Ultrastructure of outermost layer of cell wall in Candida albicans observed by rapid-freezing technique. J. Electron Microsc. 35:237-246.
    • (1986) J. Electron Microsc. , vol.35 , pp. 237-246
    • Tokunaga, M.1    Kusamichi, M.2    Koike, H.3
  • 289
    • 0035183690 scopus 로고    scopus 로고
    • Application of Candida solubilized cell wall β-glucan in antitumor immunotherapy against P815 mastocytoma in mice
    • Tokunaka, K., N. Ohno, Y. Adachi, K. Miura, and T. Yadomae. 2002. Application of Candida solubilized cell wall β-glucan in antitumor immunotherapy against P815 mastocytoma in mice. Int. Immunopharmacol. 2:59-67.
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 59-67
    • Tokunaka, K.1    Ohno, N.2    Adachi, Y.3    Miura, K.4    Yadomae, T.5
  • 290
    • 0034191883 scopus 로고    scopus 로고
    • Immunopharmacological and immunotoxicological activities of a water soluble (1→3)-β-D-glucan, CSBG from Candida spp.
    • Tokunaka, K., N. Ohno, Y. Adachi, S. Tanaka, H. Tamura, and T. Yadomae. 2000. Immunopharmacological and immunotoxicological activities of a water soluble (1→3)-β-D-glucan, CSBG from Candida spp. Int. J. Immunopharmacol. 22:383-394.
    • (2000) Int. J. Immunopharmacol. , vol.22 , pp. 383-394
    • Tokunaka, K.1    Ohno, N.2    Adachi, Y.3    Tanaka, S.4    Tamura, H.5    Yadomae, T.6
  • 291
    • 0033664620 scopus 로고    scopus 로고
    • Differential chemokine response of human monocytes to yeast and hyphal forms of Candida albicans and its relation to the β-1,6 glucan of the fungal cell wall
    • Torosantucci, A., P. Chiani, and A. Cassone. 2000. Differential chemokine response of human monocytes to yeast and hyphal forms of Candida albicans and its relation to the β-1,6 glucan of the fungal cell wall. J. Leukoc. Biol. 68:923-932.
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 923-932
    • Torosantucci, A.1    Chiani, P.2    Cassone, A.3
  • 292
    • 0027485158 scopus 로고
    • Isolation and preliminary characterization of the 14- to 18-kilodalton Candida albicans antigen as a phospholipomannan containing β-1,2-linked oligomannosides
    • Trinel, P.-A., M. Borg-von-Zepelin, G. Lepage, T. Jouault, D. Mackenzie, and D. Poulain. 1993. Isolation and preliminary characterization of the 14- to 18-kilodalton Candida albicans antigen as a phospholipomannan containing β-1,2-linked oligomannosides. Infect. Immun. 61:4398-4405.
    • (1993) Infect. Immun. , vol.61 , pp. 4398-4405
    • Trinel, P.-A.1    Borg-Von-Zepelin, M.2    Lepage, G.3    Jouault, T.4    Mackenzie, D.5    Poulain, D.6
  • 293
    • 0030734676 scopus 로고    scopus 로고
    • Definitive chemical evidence for the constitutive ability of Candida albicans serotype A strains to synthesize β-1,2 linked oligomannosides containing up to 14 mannose residues
    • Trinel, P. A., G. Lepage, T. Jouault, G. Strecker, and D. Poulain. 1997. Definitive chemical evidence for the constitutive ability of Candida albicans serotype A strains to synthesize β-1,2 linked oligomannosides containing up to 14 mannose residues. FEBS Lett. 416:203-206.
    • (1997) FEBS Lett. , vol.416 , pp. 203-206
    • Trinel, P.A.1    Lepage, G.2    Jouault, T.3    Strecker, G.4    Poulain, D.5
  • 294
    • 0019457906 scopus 로고
    • Cytochemical and ultrastructural studies of Candida albicans II. Evidence for a cell wall coat using concanavalin A
    • Tronchin, G., D. Poulain, J. Herbaut, and J. Biguet. 1981. Cytochemical and ultrastructural studies of Candida albicans II. Evidence for a cell wall coat using concanavalin A. J. Ultrastruct. Res. 75:50-59.
    • (1981) J. Ultrastruct. Res. , vol.75 , pp. 50-59
    • Tronchin, G.1    Poulain, D.2    Herbaut, J.3    Biguet, J.4
  • 295
    • 0019770751 scopus 로고
    • Localization of chitin in the cell wall of Candida albicans by means of wheat germ agglutinin. Fluorescence and ultrastructural studies
    • Tronchin, G., D. Poulain, J. Herbaut, and J. Biguet. 1981. Localization of chitin in the cell wall of Candida albicans by means of wheat germ agglutinin. Fluorescence and ultrastructural studies. Eur. J. Cell Biol. 26:121-128.
    • (1981) Eur. J. Cell Biol. , vol.26 , pp. 121-128
    • Tronchin, G.1    Poulain, D.2    Herbaut, J.3    Biguet, J.4
  • 296
    • 0021166839 scopus 로고
    • Cytochemical and ultrastructural studies of Candida albicans. III. Evidence for modifications of the cell wall coat during adherence to human buccal epithelial cells
    • Tronchin, G., D. Poulain, and A. Vernes. 1984. Cytochemical and ultrastructural studies of Candida albicans. III. Evidence for modifications of the cell wall coat during adherence to human buccal epithelial cells. Arch. Microbiol. 139:221-224.
    • (1984) Arch. Microbiol. , vol.139 , pp. 221-224
    • Tronchin, G.1    Poulain, D.2    Vernes, A.3
  • 297
    • 0000481284 scopus 로고
    • Multiplicity in the structure of the glucuronoxylomannan of Cryptococcus neoformans
    • J. P. Latgé and D. Boucias (ed.). Springer-Verlag, New York, N.Y.
    • Turner, S. H., and R. Cherniak. 1991. Multiplicity in the structure of the glucuronoxylomannan of Cryptococcus neoformans, p. 123-142. In J. P. Latgé and D. Boucias (ed.), Fungal cell wall and immune response. Springer-Verlag, New York, N.Y.
    • (1991) Fungal Cell Wall and Immune Response , pp. 123-142
    • Turner, S.H.1    Cherniak, R.2
  • 298
    • 0033783189 scopus 로고    scopus 로고
    • Polysaccharide immunomodulators as therapeutic agents: Structural aspects and biologic function
    • Tzianabos, A. O. 2000. Polysaccharide immunomodulators as therapeutic agents: structural aspects and biologic function. Clin. Microbiol. Rev. 13: 523-533.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 523-533
    • Tzianabos, A.O.1
  • 300
    • 0002530622 scopus 로고    scopus 로고
    • Sialic acids
    • A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, and J. Marth (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Varki, A. 1999. Sialic acids, p. 195-209. In A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, and J. Marth (ed.), Essentials of glycobiology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1999) Essentials of Glycobiology , pp. 195-209
    • Varki, A.1
  • 301
    • 0021364466 scopus 로고
    • The release and purification of sialic acids from glycoconjugates: Methods to minimize the loss and migration of O-acetyl groups
    • Varki, A., and S. Diaz. 1984. The release and purification of sialic acids from glycoconjugates: methods to minimize the loss and migration of O-acetyl groups. Anal. Biochem. 137:236-247.
    • (1984) Anal. Biochem. , vol.137 , pp. 236-247
    • Varki, A.1    Diaz, S.2
  • 302
    • 0034176743 scopus 로고    scopus 로고
    • Isolated Pneumocystis carinii cell wall glucan provokes lower respiratory tract inflammatory responses
    • Vassallo, R., J. E. Standing, and A. H. Limper. 2000. Isolated Pneumocystis carinii cell wall glucan provokes lower respiratory tract inflammatory responses. J. Immunol. 164:3755-3763.
    • (2000) J. Immunol. , vol.164 , pp. 3755-3763
    • Vassallo, R.1    Standing, J.E.2    Limper, A.H.3
  • 303
    • 0030035119 scopus 로고    scopus 로고
    • Soluble β-glucan polysaccharide binding to the lectin site of neutrophil or natural killer cell complement receptor type three (CD11b/CD18) generates a primed state of the receptor capable of mediating cytotoxicity of iC3b-opsonized target cells
    • Vetvicka, V., B. P. Thornton, and G. D. Ross. 1996. Soluble β-glucan polysaccharide binding to the lectin site of neutrophil or natural killer cell complement receptor type three (CD11b/CD18) generates a primed state of the receptor capable of mediating cytotoxicity of iC3b-opsonized target cells. J. Clin. Investig. 98:50-61.
    • (1996) J. Clin. Investig. , vol.98 , pp. 50-61
    • Vetvicka, V.1    Thornton, B.P.2    Ross, G.D.3
  • 304
    • 0031570899 scopus 로고    scopus 로고
    • Targeting of natural killer cells to mammary carcinoma via naturally occuring tumor cell-bound iC3b and β-glucan-primed CR3 (CD11b/CD18)
    • Vetvicka, V., B. P. Thornton, T. J. Wieman, and G. D. Ross. 1997. Targeting of natural killer cells to mammary carcinoma via naturally occuring tumor cell-bound iC3b and β-glucan-primed CR3 (CD11b/CD18). J. Immunol. 159:599-605.
    • (1997) J. Immunol. , vol.159 , pp. 599-605
    • Vetvicka, V.1    Thornton, B.P.2    Wieman, T.J.3    Ross, G.D.4
  • 308
    • 0027485530 scopus 로고
    • Analysis of mannoproteins from blastoconidia and hyphae of Candida albicans with a common epitope recognized by anti-complement receptor type 2 antibodies
    • Wadsworth, E., S. C. Prasad, and R. Calderone. 1993. Analysis of mannoproteins from blastoconidia and hyphae of Candida albicans with a common epitope recognized by anti-complement receptor type 2 antibodies. Infect. Immun. 61:4675-4681.
    • (1993) Infect. Immun. , vol.61 , pp. 4675-4681
    • Wadsworth, E.1    Prasad, S.C.2    Calderone, R.3
  • 309
    • 0035907146 scopus 로고    scopus 로고
    • Determination of carbohydrates as their p-sulfophenylhydrazones by capillary zone electrophoresis
    • Wang, X., and Y. Chen. 2001. Determination of carbohydrates as their p-sulfophenylhydrazones by capillary zone electrophoresis. Carbohydr. Res. 332:191-196.
    • (2001) Carbohydr. Res. , vol.332 , pp. 191-196
    • Wang, X.1    Chen, Y.2
  • 310
    • 0032036503 scopus 로고    scopus 로고
    • Cytokine involvement in immunomodulatory activity affected by Candida albicans mannan
    • Wang, Y., S. P. Li, S. A. Moser, K. L. Bost, and J. E. Domer. 1998. Cytokine involvement in immunomodulatory activity affected by Candida albicans mannan. Infect. Immun. 66:1384-1391.
    • (1998) Infect. Immun. , vol.66 , pp. 1384-1391
    • Wang, Y.1    Li, S.P.2    Moser, S.A.3    Bost, K.L.4    Domer, J.E.5
  • 312
    • 0018571998 scopus 로고
    • Immunodiagnosis of systemic candidiasis: Mannan antigenemia detected by radioimmunoassay in experimental and human infections
    • Weiner, M. H., and M. Coats-Stephen. 1979. Immunodiagnosis of systemic candidiasis: mannan antigenemia detected by radioimmunoassay in experimental and human infections. J. Infect. Dis. 140:989-993.
    • (1979) J. Infect. Dis. , vol.140 , pp. 989-993
    • Weiner, M.H.1    Coats-Stephen, M.2
  • 313
    • 0017101690 scopus 로고
    • Mannan antigenemia in the diagnosis of invasive Candida infections
    • Weiner, M. H., and W. J. Yount. 1976. Mannan antigenemia in the diagnosis of invasive Candida infections. J. Clin. Investig. 58:1045-1053.
    • (1976) J. Clin. Investig. , vol.58 , pp. 1045-1053
    • Weiner, M.H.1    Yount, W.J.2
  • 314
    • 0029052354 scopus 로고
    • Nosocomial candidemia: Risk factors and attributable mortality
    • Wenzel, R. P. 1995. Nosocomial candidemia: Risk factors and attributable mortality. Clin. Infect. Dis. 20:1531-1534.
    • (1995) Clin. Infect. Dis. , vol.20 , pp. 1531-1534
    • Wenzel, R.P.1
  • 315
    • 0345552244 scopus 로고    scopus 로고
    • The β-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells
    • Xia, Y., V. Vetvicka, J. Yan, M. Hanikýrová, T. Mayadas, and G. D. Ross. 1999. The β-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells. J. Immunol. 162:2281-2290.
    • (1999) J. Immunol. , vol.162 , pp. 2281-2290
    • Xia, Y.1    Vetvicka, V.2    Yan, J.3    Hanikýrová, M.4    Mayadas, T.5    Ross, G.D.6
  • 316
    • 0038824605 scopus 로고    scopus 로고
    • First syntheses of D-mannose penta- and decasaccharides, the repeating unit and its dimer of the cell-wall mannan of Candida kefyr IFO 0586
    • Xing, Y., and J. Ning. 2003. First syntheses of D-mannose penta- and decasaccharides, the repeating unit and its dimer of the cell-wall mannan of Candida kefyr IFO 0586. Tetrahedron Asymm. 14:1275-1283.
    • (2003) Tetrahedron Asymm. , vol.14 , pp. 1275-1283
    • Xing, Y.1    Ning, J.2
  • 317
    • 0033570214 scopus 로고    scopus 로고
    • A pyridylamination method aimed at automatic oligosaccharide analysis of N-linked sugar chains
    • Yanagida, K., S. Natsuka, and S. Hase. 1999. A pyridylamination method aimed at automatic oligosaccharide analysis of N-linked sugar chains. Anal. Biochem. 274:229-234.
    • (1999) Anal. Biochem. , vol.274 , pp. 229-234
    • Yanagida, K.1    Natsuka, S.2    Hase, S.3
  • 318
    • 0035709533 scopus 로고    scopus 로고
    • Contribution of serological tests and blood culture to the early diagnosis of systemic candidiasis
    • Yera, H., B. Sendid, N. Francois, D. Camus, and D. Poulain. 2001. Contribution of serological tests and blood culture to the early diagnosis of systemic candidiasis. Eur. J. Clin. Microbiol. Infect. Dis. 20:864-870.
    • (2001) Eur. J. Clin. Microbiol. Infect. Dis. , vol.20 , pp. 864-870
    • Yera, H.1    Sendid, B.2    Francois, N.3    Camus, D.4    Poulain, D.5
  • 320
    • 0028836187 scopus 로고
    • Isotype switching from IgG3 to IgG1 converts nonprotective murine antibody to Cryptococcus neoformans into a protective antibody
    • Yuan, R., A. Casadevall, G. Spira, and M. D. Scharff. 1995. Isotype switching from IgG3 to IgG1 converts nonprotective murine antibody to Cryptococcus neoformans into a protective antibody. J. Immunol. 154:1810-1816.
    • (1995) J. Immunol. , vol.154 , pp. 1810-1816
    • Yuan, R.1    Casadevall, A.2    Spira, G.3    Scharff, M.D.4
  • 321
    • 1842601412 scopus 로고    scopus 로고
    • Isotype switching increases efficacy of antibody protection against Cryptococcus neoformans infection in mice
    • Yuan, R. R., G. Spira, J. Oh, M. Paizi, A. Casadevall, and M. D. Scharff. 1998. Isotype switching increases efficacy of antibody protection against Cryptococcus neoformans infection in mice. Infect. Immun. 66:1057-1062.
    • (1998) Infect. Immun. , vol.66 , pp. 1057-1062
    • Yuan, R.R.1    Spira, G.2    Oh, J.3    Paizi, M.4    Casadevall, A.5    Scharff, M.D.6
  • 322
    • 0034898516 scopus 로고    scopus 로고
    • Glycoscreening by on-line sheathless capillary electrophoresis/electrospray ionization-quadrupole time of flight-tandem mass spectrometry
    • Zamfir, A., and J. Peter-Katalinic. 2001. Glycoscreening by on-line sheathless capillary electrophoresis/electrospray ionization-quadrupole time of flight-tandem mass spectrometry. Electrophoresis 22:2448-2457.
    • (2001) Electrophoresis , vol.22 , pp. 2448-2457
    • Zamfir, A.1    Peter-Katalinic, J.2
  • 323
    • 0031931055 scopus 로고    scopus 로고
    • Differential binding of lectins IL-2 and CSL to Candida albicans and cancer cells
    • Zanetta, J.-P., R. Bonaly, S. Maschke, G. Strecker, and J.-C. Michalski. 1998. Differential binding of lectins IL-2 and CSL to Candida albicans and cancer cells. Glycobiology 8:221-225.
    • (1998) Glycobiology , vol.8 , pp. 221-225
    • Zanetta, J.-P.1    Bonaly, R.2    Maschke, S.3    Strecker, G.4    Michalski, J.-C.5
  • 324
    • 0031796442 scopus 로고    scopus 로고
    • Contrasting roles of mannan-specific monoclonal immunoglobulin M antibodies in the activation of classical and alternative pathways by Candida albicans
    • Zhang, M. X., J. E. Cutler, Y. Han, and T. R. Kozel. 1998. Contrasting roles of mannan-specific monoclonal immunoglobulin M antibodies in the activation of classical and alternative pathways by Candida albicans. Infect. Immun. 66:6027-6029.
    • (1998) Infect. Immun. , vol.66 , pp. 6027-6029
    • Zhang, M.X.1    Cutler, J.E.2    Han, Y.3    Kozel, T.R.4
  • 325
    • 0021122967 scopus 로고
    • Saccharomyces cerevisiae mannoproteins form an external cell wall layer that determines wall porosity
    • Zlotnik, H., M. P. Fernandez, B. Bowers, and E. Cabib. 1984. Saccharomyces cerevisiae mannoproteins form an external cell wall layer that determines wall porosity. J. Bacteriol. 159:1018-1026.
    • (1984) J. Bacteriol. , vol.159 , pp. 1018-1026
    • Zlotnik, H.1    Fernandez, M.P.2    Bowers, B.3    Cabib, E.4


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