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Volumn 76, Issue , 2015, Pages 36-46

Bcpmr1 encodes a P-type Ca2+/Mn2+-ATPase mediating cell-wall integrity and virulence in the phytopathogen Botrytis cinerea

Author keywords

Botrytis cinerea; Cell wall; Glycosylation; PMR1

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); CHITIN; GLUCAN; MANNAN; FUNGAL PROTEIN;

EID: 84923169847     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2015.01.012     Document Type: Article
Times cited : (25)

References (71)
  • 1
    • 55449083640 scopus 로고    scopus 로고
    • Investigation of extracellular elastase, acid proteinase and phospholipase activities as putative virulence factors in clinical isolates of Aspergillus species
    • Alp S., Arikan S. Investigation of extracellular elastase, acid proteinase and phospholipase activities as putative virulence factors in clinical isolates of Aspergillus species. J. Basic Microbiol. 2008, 48:331-337.
    • (2008) J. Basic Microbiol. , vol.48 , pp. 331-337
    • Alp, S.1    Arikan, S.2
  • 2
    • 80052319576 scopus 로고    scopus 로고
    • Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea
    • Amselem J., et al. Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea. PLoS Genet. 2011, 7.
    • (2011) PLoS Genet. , vol.7
    • Amselem, J.1
  • 3
    • 0027097849 scopus 로고
    • The yeast Ca-2+-Atpase Homolog, Pmr1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • Antebi A., Fink G.R. The yeast Ca-2+-Atpase Homolog, Pmr1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 1992, 3:633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 4
    • 80053474775 scopus 로고    scopus 로고
    • Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans
    • Aoki W., et al. Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans. J. Biochem. 2011, 150:431-438.
    • (2011) J. Biochem. , vol.150 , pp. 431-438
    • Aoki, W.1
  • 5
    • 20744455345 scopus 로고    scopus 로고
    • 2+-ATPase, is required for glycosylation and virulence
    • 2+-ATPase, is required for glycosylation and virulence. J. Biol. Chem. 2005, 280:23408-23415.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23408-23415
    • Bates, S.1
  • 6
    • 33644867152 scopus 로고    scopus 로고
    • Outer chain N-glycans are required for cell wall integrity and virulence of Candida albicans
    • Bates S., et al. Outer chain N-glycans are required for cell wall integrity and virulence of Candida albicans. J. Biol. Chem. 2006, 281:90-98.
    • (2006) J. Biol. Chem. , vol.281 , pp. 90-98
    • Bates, S.1
  • 8
    • 0037093384 scopus 로고    scopus 로고
    • Essential role of calcineurin in response to endoplasmic reticulum stress
    • Bonilla M., et al. Essential role of calcineurin in response to endoplasmic reticulum stress. EMBO J. 2002, 21:2343-2353.
    • (2002) EMBO J. , vol.21 , pp. 2343-2353
    • Bonilla, M.1
  • 9
    • 77956106339 scopus 로고    scopus 로고
    • Functional genomic profiling of Aspergillus fumigatus biofilm reveals enhanced production of the mycotoxin gliotoxin
    • Bruns S., et al. Functional genomic profiling of Aspergillus fumigatus biofilm reveals enhanced production of the mycotoxin gliotoxin. Proteomics 2010, 10:3097-3107.
    • (2010) Proteomics , vol.10 , pp. 3097-3107
    • Bruns, S.1
  • 10
    • 0028297135 scopus 로고
    • Variations in ploidy among isolates of Botrytis-Cinerea - implications for genetic and molecular analyses
    • Buttner P., et al. Variations in ploidy among isolates of Botrytis-Cinerea - implications for genetic and molecular analyses. Curr. Genet. 1994, 25:445-450.
    • (1994) Curr. Genet. , vol.25 , pp. 445-450
    • Buttner, P.1
  • 11
    • 38949099113 scopus 로고    scopus 로고
    • The intersection between cell wall disassembly, ripening, and fruit susceptibility to Botrytis cinerea
    • Cantu D., et al. The intersection between cell wall disassembly, ripening, and fruit susceptibility to Botrytis cinerea. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:859-864.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 859-864
    • Cantu, D.1
  • 12
    • 54549084280 scopus 로고    scopus 로고
    • Strangers in the matrix: plant cell walls and pathogen susceptibility
    • Cantu D., et al. Strangers in the matrix: plant cell walls and pathogen susceptibility. Trends Plant Sci. 2008, 13:610-617.
    • (2008) Trends Plant Sci. , vol.13 , pp. 610-617
    • Cantu, D.1
  • 13
    • 70649097280 scopus 로고    scopus 로고
    • Characterization of the cell wall of the ubiquitous plant pathogen Botrytis cinerea
    • Cantu D., et al. Characterization of the cell wall of the ubiquitous plant pathogen Botrytis cinerea. Mycol. Res. 2009, 113:1396-1403.
    • (2009) Mycol. Res. , vol.113 , pp. 1396-1403
    • Cantu, D.1
  • 14
    • 6344235390 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and is required for polarized cell growth and cytokinesis
    • Cortes J.C.G., et al. Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and is required for polarized cell growth and cytokinesis. Eukaryot. Cell 2004, 3:1124-1135.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1124-1135
    • Cortes, J.C.G.1
  • 15
    • 0022377451 scopus 로고
    • Adherence of coagulase-negative staphylococci to plastic tissue culture plates: a quantitative model for the adherence of staphylococci to medical devices
    • Christensen G.D., et al. Adherence of coagulase-negative staphylococci to plastic tissue culture plates: a quantitative model for the adherence of staphylococci to medical devices. J. Clin. Microbiol. 1985, 22:996-1006.
    • (1985) J. Clin. Microbiol. , vol.22 , pp. 996-1006
    • Christensen, G.D.1
  • 16
    • 2442615143 scopus 로고    scopus 로고
    • Characterization of the antifungal activity on Botrytis cinerea of the natural diterpenoids kaurenoic acid and 3 beta-hydroxy-kaurenoic acid
    • Cotoras M., et al. Characterization of the antifungal activity on Botrytis cinerea of the natural diterpenoids kaurenoic acid and 3 beta-hydroxy-kaurenoic acid. J. Agric. Food Chem. 2004, 52:2821-2826.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 2821-2826
    • Cotoras, M.1
  • 17
    • 0037083792 scopus 로고    scopus 로고
    • Calcineurin is essential for survival during membrane stress in Candida albicans
    • Cruz M.C., et al. Calcineurin is essential for survival during membrane stress in Candida albicans. EMBO J. 2002, 21:546-559.
    • (2002) EMBO J. , vol.21 , pp. 546-559
    • Cruz, M.C.1
  • 18
    • 84895397363 scopus 로고    scopus 로고
    • A genomic inventory of cell wall biosynthesis in the ubiquitous plant pathogen botrytis cinerea
    • Nova Biomedical, Hauppauge (NY), H.M. Mora-Montes (Ed.)
    • De Groot P.W., et al. A genomic inventory of cell wall biosynthesis in the ubiquitous plant pathogen botrytis cinerea. The Fungal Cell Wall 2013, Nova Biomedical, Hauppauge (NY). H.M. Mora-Montes (Ed.).
    • (2013) The Fungal Cell Wall
    • De Groot, P.W.1
  • 19
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: current state and perspectives
    • De Pourcq K., et al. Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl. Microbiol. Biotechnol. 2010, 87:1617-1631.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1617-1631
    • De Pourcq, K.1
  • 20
    • 84859372662 scopus 로고    scopus 로고
    • The top 10 fungal pathogens in molecular plant pathology
    • Dean R., et al. The top 10 fungal pathogens in molecular plant pathology. Mol. Plant Pathol. 2012, 13:414-430.
    • (2012) Mol. Plant Pathol. , vol.13 , pp. 414-430
    • Dean, R.1
  • 21
    • 48349093421 scopus 로고    scopus 로고
    • Protein glycosylation pathways in filamentous fungi
    • Deshpande N., et al. Protein glycosylation pathways in filamentous fungi. Glycobiology 2008, 18:626-637.
    • (2008) Glycobiology , vol.18 , pp. 626-637
    • Deshpande, N.1
  • 22
    • 33645049325 scopus 로고    scopus 로고
    • Different signalling pathways involving a G alpha protein, cAMP and a MAP kinase control germination of Botrytis cinerea conidia
    • Doehlemann G., et al. Different signalling pathways involving a G alpha protein, cAMP and a MAP kinase control germination of Botrytis cinerea conidia. Mol. Microbiol. 2006, 59:821-835.
    • (2006) Mol. Microbiol. , vol.59 , pp. 821-835
    • Doehlemann, G.1
  • 23
    • 0031664331 scopus 로고    scopus 로고
    • 2+ required for glycosylation, sorting, and endoplasmic reticulum associated protein degradation
    • 2+ required for glycosylation, sorting, and endoplasmic reticulum associated protein degradation. Mol. Biol. Cell 1998, 9:1149-1162.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1149-1162
    • Durr, G.1
  • 25
    • 72049102104 scopus 로고    scopus 로고
    • The O-Mannosyltransferase PMT4 is essential for normal appressorium formation and penetration in Ustilago maydis
    • Fernandez-Alvarez A., et al. The O-Mannosyltransferase PMT4 is essential for normal appressorium formation and penetration in Ustilago maydis. Plant Cell. 2009, 21:3397-3412.
    • (2009) Plant Cell. , vol.21 , pp. 3397-3412
    • Fernandez-Alvarez, A.1
  • 26
    • 0034623061 scopus 로고    scopus 로고
    • Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall
    • Fontaine T., et al. Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall. J. Biol. Chem. 2000, 275:27594-27607.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27594-27607
    • Fontaine, T.1
  • 27
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch M., Tanner W. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 1996, 15:5752-5759.
    • (1996) EMBO J. , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 28
    • 34347206860 scopus 로고    scopus 로고
    • High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method
    • Gietz R.D., Schiestl R.H. High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method. Nat. Protoc. 2007, 2:31-34.
    • (2007) Nat. Protoc. , vol.2 , pp. 31-34
    • Gietz, R.D.1    Schiestl, R.H.2
  • 29
    • 84866483646 scopus 로고    scopus 로고
    • High abundance of serine/threonine-rich regions predicted to be hyper-O-glycosylated in the secretory proteins coded by eight fungal genomes
    • Gonzalez M., et al. High abundance of serine/threonine-rich regions predicted to be hyper-O-glycosylated in the secretory proteins coded by eight fungal genomes. BMC Microbiol. 2012, 12.
    • (2012) BMC Microbiol. , vol.12
    • Gonzalez, M.1
  • 30
    • 84878782008 scopus 로고    scopus 로고
    • Botrytis cinerea protein O-mannosyltransferases play critical roles in morphogenesis, growth, and virulence
    • Gonzalez M., et al. Botrytis cinerea protein O-mannosyltransferases play critical roles in morphogenesis, growth, and virulence. PLoS ONE 2013, 8.
    • (2013) PLoS ONE , vol.8
    • Gonzalez, M.1
  • 31
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: diverse structures and multiple functions
    • Goto M. Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci. Biotechnol. Biochem. 2007, 71:1415-1427.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1415-1427
    • Goto, M.1
  • 32
    • 0030844713 scopus 로고    scopus 로고
    • Altered extent of cross-linking of beta 1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall beta 1,3-glucan content
    • Kapteyn J.C., et al. Altered extent of cross-linking of beta 1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall beta 1,3-glucan content. J. Bacteriol. 1997, 179:6279-6284.
    • (1997) J. Bacteriol. , vol.179 , pp. 6279-6284
    • Kapteyn, J.C.1
  • 33
    • 33646342452 scopus 로고    scopus 로고
    • Functional analysis of Botrytis cinerea pectin methylesterase genes by PCR-based targeted mutagenesis: Bcpme1 and Bcpme2 are dispensable for virulence of strain B05.10
    • Kars I., et al. Functional analysis of Botrytis cinerea pectin methylesterase genes by PCR-based targeted mutagenesis: Bcpme1 and Bcpme2 are dispensable for virulence of strain B05.10. Mol. Plant Pathol. 2005, 6:641-652.
    • (2005) Mol. Plant Pathol. , vol.6 , pp. 641-652
    • Kars, I.1
  • 34
    • 0026681302 scopus 로고
    • The influence of congo red on the cell-wall and (1-]3)-Beta-D-glucan microfibril biogenesis in Saccharomyces-cerevisiae
    • Kopecka M., Gabriel M. The influence of congo red on the cell-wall and (1-]3)-Beta-D-glucan microfibril biogenesis in Saccharomyces-cerevisiae. Arch. Microbiol. 1992, 158:115-126.
    • (1992) Arch. Microbiol. , vol.158 , pp. 115-126
    • Kopecka, M.1    Gabriel, M.2
  • 35
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., et al. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1
  • 36
    • 0031757398 scopus 로고    scopus 로고
    • Signaling via cAMP in fungi: interconnections with mitogen-activated protein kinase pathways
    • Kronstad J., et al. Signaling via cAMP in fungi: interconnections with mitogen-activated protein kinase pathways. Arch. Microbiol. 1998, 170:395-404.
    • (1998) Arch. Microbiol. , vol.170 , pp. 395-404
    • Kronstad, J.1
  • 37
    • 33645120423 scopus 로고    scopus 로고
    • Cell wall assembly in Saccharomyces cerevisiae
    • Lesage G., Bussey H. Cell wall assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 2006, 70:317-+.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 317-+
    • Lesage, G.1    Bussey, H.2
  • 38
    • 84893584275 scopus 로고    scopus 로고
    • The Fusarium oxysporum gnt2, encoding a putative N-acetylglucosamine transferase, is involved in cell wall architecture and virulence
    • Lopez-Fernandez L., et al. The Fusarium oxysporum gnt2, encoding a putative N-acetylglucosamine transferase, is involved in cell wall architecture and virulence. PLoS ONE 2013, 8.
    • (2013) PLoS ONE , vol.8
    • Lopez-Fernandez, L.1
  • 39
    • 0037031829 scopus 로고    scopus 로고
    • 2+ transient activates calcineurin signaling to mediate ion homeostasis and salt tolerance of Saccharomyces cerevisiae
    • 2+ transient activates calcineurin signaling to mediate ion homeostasis and salt tolerance of Saccharomyces cerevisiae. J. Biol. Chem. 2002, 277:33075-33080.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33075-33080
    • Matsumoto, T.K.1
  • 40
    • 3142736570 scopus 로고    scopus 로고
    • Hydrolysis of Man(9)GlcNAc(2) and Man(8)GlcNAc(2) oligosaccharides by a purified alpha-mannosidase from Candida albicans
    • Mora-Montes H.M., et al. Hydrolysis of Man(9)GlcNAc(2) and Man(8)GlcNAc(2) oligosaccharides by a purified alpha-mannosidase from Candida albicans. Glycobiology 2004, 14:593-598.
    • (2004) Glycobiology , vol.14 , pp. 593-598
    • Mora-Montes, H.M.1
  • 41
    • 37549020379 scopus 로고    scopus 로고
    • Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction
    • Mora-Montes H.M., et al. Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction. Eukaryot. Cell 2007, 6:2184-2193.
    • (2007) Eukaryot. Cell , vol.6 , pp. 2184-2193
    • Mora-Montes, H.M.1
  • 42
    • 77951244325 scopus 로고    scopus 로고
    • A multifunctional mannosyltransferase family in Candida albicans determines cell wall mannan structure and host-fungus interactions
    • Mora-Montes H.M., et al. A multifunctional mannosyltransferase family in Candida albicans determines cell wall mannan structure and host-fungus interactions. J. Biol. Chem. 2010, 285:12087-12095.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12087-12095
    • Mora-Montes, H.M.1
  • 43
    • 34748871970 scopus 로고    scopus 로고
    • Development of a simple model for studying the effects of antifungal agents on multicellular communities of Aspergillus fumigatus
    • Mowat E., et al. Development of a simple model for studying the effects of antifungal agents on multicellular communities of Aspergillus fumigatus. J. Med. Microbiol. 2007, 56:1205-1212.
    • (2007) J. Med. Microbiol. , vol.56 , pp. 1205-1212
    • Mowat, E.1
  • 44
    • 19944431369 scopus 로고    scopus 로고
    • Mnt1p and Mnt2p of Candida albicans are partially redundant alpha-1,2-mannosyltransferases that participate in O-linked mannosylation and are required for adhesion and virulence
    • Munro C.A., et al. Mnt1p and Mnt2p of Candida albicans are partially redundant alpha-1,2-mannosyltransferases that participate in O-linked mannosylation and are required for adhesion and virulence. J. Biol. Chem. 2005, 280:1051-1060.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1051-1060
    • Munro, C.A.1
  • 45
    • 0032538128 scopus 로고    scopus 로고
    • The involvement of mnn4 and mnn6 mutations in mannosylphosphorylation of O-linked oligosaccharide in yeast Saccharomyces cerevisiae
    • Nakayama K., et al. The involvement of mnn4 and mnn6 mutations in mannosylphosphorylation of O-linked oligosaccharide in yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta - Gen. Subjects 1998, 1425:255-262.
    • (1998) Biochim. Biophys. Acta - Gen. Subjects , vol.1425 , pp. 255-262
    • Nakayama, K.1
  • 46
    • 33845968175 scopus 로고    scopus 로고
    • The CRH family coding for cell wall glycosylphosphatidylinositol proteins with a predicted transglycosidase domain affects cell wall organization and virulence of Candida albicans
    • Pardini G., et al. The CRH family coding for cell wall glycosylphosphatidylinositol proteins with a predicted transglycosidase domain affects cell wall organization and virulence of Candida albicans. J. Biol. Chem. 2006, 281:40399-40411.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40399-40411
    • Pardini, G.1
  • 47
    • 6444229572 scopus 로고    scopus 로고
    • PST1 and ECM33 encode two yeast cell surface GPI proteins important for cell wall integrity
    • Pardo M., et al. PST1 and ECM33 encode two yeast cell surface GPI proteins important for cell wall integrity. Microbiol.-Sgm 2004, 150:4157-4170.
    • (2004) Microbiol.-Sgm , vol.150 , pp. 4157-4170
    • Pardo, M.1
  • 48
    • 0035800871 scopus 로고    scopus 로고
    • +-ATPase in plasma membrane
    • +-ATPase in plasma membrane. J. Biol. Chem. 2001, 276:28694-28699.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28694-28699
    • Park, S.Y.1
  • 49
    • 33749512972 scopus 로고    scopus 로고
    • Protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
    • Peltroche-Llacsahuanga H., et al. Protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans. Antimicrob. Agents Chemother. 2006, 50:3488-3491.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3488-3491
    • Peltroche-Llacsahuanga, H.1
  • 50
    • 77649288776 scopus 로고    scopus 로고
    • 2+ ATPase PmrA is involved in cation homeostasis and cell wall integrity but is not essential for pathogenesis
    • 2+ ATPase PmrA is involved in cation homeostasis and cell wall integrity but is not essential for pathogenesis. Eukaryot. Cell 2010, 9:472-476.
    • (2010) Eukaryot. Cell , vol.9 , pp. 472-476
    • Pinchai, N.1
  • 51
    • 53049099570 scopus 로고    scopus 로고
    • Functional analysis of Candida albicans GPI-anchored proteins: roles in cell wall integrity and caspofungin sensitivity
    • Plaine A., et al. Functional analysis of Candida albicans GPI-anchored proteins: roles in cell wall integrity and caspofungin sensitivity. Fungal Genet. Biol. 2008, 45:1404-1414.
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 1404-1414
    • Plaine, A.1
  • 52
    • 0031027101 scopus 로고    scopus 로고
    • Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1 Delta mutant of Saccharomyces cerevisiae
    • Popolo L., et al. Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1 Delta mutant of Saccharomyces cerevisiae. J. Bacteriol. 1997, 179:463-469.
    • (1997) J. Bacteriol. , vol.179 , pp. 463-469
    • Popolo, L.1
  • 53
    • 0032030085 scopus 로고    scopus 로고
    • Detoxification of alpha-tomatine by Botrytis cinerea
    • Quidde T., et al. Detoxification of alpha-tomatine by Botrytis cinerea. Physiol. Mol. Plant Pathol. 1998, 52:151-165.
    • (1998) Physiol. Mol. Plant Pathol. , vol.52 , pp. 151-165
    • Quidde, T.1
  • 54
    • 0021965293 scopus 로고
    • Effect of Calcofluor white and Congo red on fungal cell wall morphogenesis: in vivo activation of chitin polymerization
    • Roncero C., Duran A. Effect of Calcofluor white and Congo red on fungal cell wall morphogenesis: in vivo activation of chitin polymerization. J. Bacteriol. 1985, 163:1180-1185.
    • (1985) J. Bacteriol. , vol.163 , pp. 1180-1185
    • Roncero, C.1    Duran, A.2
  • 55
    • 0024375204 scopus 로고
    • The yeast secretory pathway is perturbed by mutations in Pmr1, a member of a Ca-2+ Atpase family
    • Rudolph H.K., et al. The yeast secretory pathway is perturbed by mutations in Pmr1, a member of a Ca-2+ Atpase family. Cell 1989, 58:133-145.
    • (1989) Cell , vol.58 , pp. 133-145
    • Rudolph, H.K.1
  • 57
    • 33645056930 scopus 로고    scopus 로고
    • Molecular organization of the cell wall of Candida albicans and its relation to pathogenicity
    • Ruiz-Herrera J., et al. Molecular organization of the cell wall of Candida albicans and its relation to pathogenicity. FEMS Yeast Res. 2006, 6:14-29.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 14-29
    • Ruiz-Herrera, J.1
  • 59
    • 23944489892 scopus 로고    scopus 로고
    • A PMR1-like calcium ATPase of Aspergillus fumigatus: cloning, identification and functional expression in S-cerevisiae
    • Soriani F.M., et al. A PMR1-like calcium ATPase of Aspergillus fumigatus: cloning, identification and functional expression in S-cerevisiae. Yeast 2005, 22:813-824.
    • (2005) Yeast , vol.22 , pp. 813-824
    • Soriani, F.M.1
  • 60
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro R.G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12:43R-56R.
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 61
    • 84868113304 scopus 로고    scopus 로고
    • Genome update of Botrytis cinerea strains B05.10 and T4
    • Staats M., van Kan J.A.L. Genome update of Botrytis cinerea strains B05.10 and T4. Eukaryot. Cell 2012, 11:1413-1414.
    • (2012) Eukaryot. Cell , vol.11 , pp. 1413-1414
    • Staats, M.1    van Kan, J.A.L.2
  • 63
    • 0029055848 scopus 로고
    • Identification of three mannoproteins in the cell wall of Saccharomyces cerevisiae
    • van der Vaart J.M., et al. Identification of three mannoproteins in the cell wall of Saccharomyces cerevisiae. J. Bacteriol. 1995, 177:3104-3110.
    • (1995) J. Bacteriol. , vol.177 , pp. 3104-3110
    • van der Vaart, J.M.1
  • 64
    • 54249147051 scopus 로고    scopus 로고
    • The putative alpha-1,2-mannosyltransferase AfMnt1 of the opportunistic fungal pathogen Aspergillus fumigatus is required for cell wall stability and full virulence
    • Wagener J., et al. The putative alpha-1,2-mannosyltransferase AfMnt1 of the opportunistic fungal pathogen Aspergillus fumigatus is required for cell wall stability and full virulence. Eukaryot. Cell 2008, 7:1661-1673.
    • (2008) Eukaryot. Cell , vol.7 , pp. 1661-1673
    • Wagener, J.1
  • 65
    • 0030802291 scopus 로고    scopus 로고
    • MNN6, a member of the KRE2/MNT1 family, is the gene for mannosylphosphate transfer in Saccharomyces cerevisiae
    • Wang X.H., et al. MNN6, a member of the KRE2/MNT1 family, is the gene for mannosylphosphate transfer in Saccharomyces cerevisiae. J. Biol. Chem. 1997, 272:18117-18124.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18117-18124
    • Wang, X.H.1
  • 66
    • 84874694547 scopus 로고    scopus 로고
    • P-type calcium ATPase functions as a core regulator of Beauveria bassiana growth, conidiation and responses to multiple stressful stimuli through cross-talk with signalling networks
    • Wang J., et al. P-type calcium ATPase functions as a core regulator of Beauveria bassiana growth, conidiation and responses to multiple stressful stimuli through cross-talk with signalling networks. Environ. Microbiol. 2013, 15:967-979.
    • (2013) Environ. Microbiol. , vol.15 , pp. 967-979
    • Wang, J.1
  • 67
    • 0141963203 scopus 로고    scopus 로고
    • O-mannosyl glycans: from yeast to novel associations with human disease
    • Willer T., et al. O-mannosyl glycans: from yeast to novel associations with human disease. Curr. Opin. Struct. Biol. 2003, 13:621-630.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 621-630
    • Willer, T.1
  • 68
    • 21244433591 scopus 로고    scopus 로고
    • Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast
    • Willer T., et al. Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast. Mol. Microbiol. 2005, 57:156-170.
    • (2005) Mol. Microbiol. , vol.57 , pp. 156-170
    • Willer, T.1
  • 69
    • 34247228099 scopus 로고    scopus 로고
    • A phenomics approach in yeast links proton and calcium pump function in the Golgi
    • Yadav J., et al. A phenomics approach in yeast links proton and calcium pump function in the Golgi. Mol. Biol. Cell 2007, 18:1480-1489.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1480-1489
    • Yadav, J.1
  • 70
    • 80052271961 scopus 로고    scopus 로고
    • The D-galacturonic acid catabolic pathway in Botrytis cinerea
    • Zhang L.S., et al. The D-galacturonic acid catabolic pathway in Botrytis cinerea. Fungal Genet. Biol. 2011, 48:990-997.
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 990-997
    • Zhang, L.S.1
  • 71
    • 37549070384 scopus 로고    scopus 로고
    • O-mannosyltransferase 1 in Aspergillus fumigatus (AfPmt1p) is crucial for cell wall integrity and conidium morphology, especially at an elevated temperature
    • Zhou H., et al. O-mannosyltransferase 1 in Aspergillus fumigatus (AfPmt1p) is crucial for cell wall integrity and conidium morphology, especially at an elevated temperature. Eukaryot. Cell 2007, 6:2260-2268.
    • (2007) Eukaryot. Cell , vol.6 , pp. 2260-2268
    • Zhou, H.1


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