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Volumn 5, Issue 5, 2014, Pages

Identification of Aph1, a phosphate-regulated, secreted, and vacuolar acid phosphatase in Cryptococcus neoformans

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; ANTERIOR PHARYNX DEFECTIVE 1 PROTEIN; FUNGAL PROTEIN; GLUCOSE 1 PHOSPHATE; GLYCEROL 2 PHOSPHATE; MANNOSE 6 PHOSPHATE; PHOSPHOTYROSINE; PROTEIN PLB1; UNCLASSIFIED DRUG; ACID PHOSPHATASE; BETA-GLYCEROPHOSPHORIC ACID; GLUCOSE PHOSPHATE; GLYCEROPHOSPHATE; GREEN FLUORESCENT PROTEIN; MANNOSE PHOSPHATE; MANNOSE-6-PHOSPHATE;

EID: 84908439763     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01649-14     Document Type: Article
Times cited : (28)

References (64)
  • 2
    • 23644450411 scopus 로고    scopus 로고
    • Secretion of cryptococcal phospholipase B1 (PLB1) is regulated by a glycosylphosphatidylinositol (GPI) anchor
    • Djordjevic JT, Del Poeta M, Sorrell TC, Turner KM, Wright LC. 2005. Secretion of cryptococcal phospholipase B1 (PLB1) is regulated by a glycosylphosphatidylinositol (GPI) anchor. Biochem. J. 389:803-812. http:// dx.doi.org/10.1042/BJ20050063.
    • (2005) Biochem. J , vol.389 , pp. 803-812
    • Djordjevic, J.T.1    Del Poeta, M.2    Sorrell, T.C.3    Turner, K.M.4    Wright, L.C.5
  • 3
    • 38049129579 scopus 로고    scopus 로고
    • Cell wall-linked cryptococcal phospholipase B1 is a source of secreted enzyme and a determinant of cell wall integrity
    • Siafakas AR, Sorrell TC, Wright LC, Wilson C, Larsen M, Boadle R, Williamson PR, Djordjevic JT. 2007. Cell wall-linked cryptococcal phospholipase B1 is a source of secreted enzyme and a determinant of cell wall integrity. J. Biol. Chem. 282:37508 -37514. http://dx.doi.org/10.1074/ jbc.M707913200.
    • (2007) J. Biol. Chem , vol.282 , pp. 37508-37514
    • Siafakas, A.R.1    Sorrell, T.C.2    Wright, L.C.3    Wilson, C.4    Larsen, M.5    Boadle, R.6    Williamson, P.R.7    Djordjevic, J.T.8
  • 4
    • 33645050376 scopus 로고    scopus 로고
    • Lipid rafts in Cryptococcus neoformans concentrate the virulence determinants phospholipase B1 and Cu/Zn superoxide dismutase
    • Siafakas AR, Wright LC, Sorrell TC, Djordjevic JT. 2006. Lipid rafts in Cryptococcus neoformans concentrate the virulence determinants phospholipase B1 and Cu/Zn superoxide dismutase. Eukaryot. Cell 5:488-498. http://dx.doi.org/10.1128/EC.5.3.488-498.2006.
    • (2006) Eukaryot. Cell , vol.5 , pp. 488-498
    • Siafakas, A.R.1    Wright, L.C.2    Sorrell, T.C.3    Djordjevic, J.T.4
  • 5
    • 33846849091 scopus 로고    scopus 로고
    • Cell wall targeting of laccase of Cryptococcus neoformans during infection of mice
    • Waterman SR, Hacham M, Panepinto J, Hu G, Shin S, Williamson PR. 2007. Cell wall targeting of laccase of Cryptococcus neoformans during infection of mice. Infect. Immun. 75:714-722. http://dx.doi.org/10.1128/ IAI.01351-06.
    • (2007) Infect. Immun , vol.75 , pp. 714-722
    • Waterman, S.R.1    Hacham, M.2    Panepinto, J.3    Hu, G.4    Shin, S.5    Williamson, P.R.6
  • 6
    • 0034867481 scopus 로고    scopus 로고
    • Laccase of Cryptococcus neoformans is a cell wall-associated virulence factor
    • Zhu X, Gibbons J, Garcia-Rivera J, Casadevall A, Williamson PR. 2001. Laccase of Cryptococcus neoformans is a cell wall-associated virulence factor. Infect. Immun. 69:5589 -5596. http://dx.doi.org/10.1128/ IAI.69.9.5589-5596.2001.
    • (2001) Infect. Immun , vol.69 , pp. 5589-5596
    • Zhu, X.1    Gibbons, J.2    Garcia-Rivera, J.3    Casadevall, A.4    Williamson, P.R.5
  • 7
    • 33750940775 scopus 로고    scopus 로고
    • Extracellular enzymatic activities in Cryptococcus neoformans strains isolated from AIDS patients in different countries
    • Vidotto V, Ito-Kuwa S, Nakamura K, Aoki S, Melhem M, Fukushima K, Bollo E. 2006. Extracellular enzymatic activities in Cryptococcus neoformans strains isolated from AIDS patients in different countries. Rev. Iberoam. Micol. 23:216 -220. http://dx.doi.org/10.1016/S1130 -1406(06)70047-X.
    • (2006) Rev. Iberoam. Micol , vol.23 , pp. 216-220
    • Vidotto, V.1    Ito-Kuwa, S.2    Nakamura, K.3    Aoki, S.4    Melhem, M.5    Fukushima, K.6    Bollo, E.7
  • 12
    • 84880831979 scopus 로고    scopus 로고
    • Secreted acid phosphatase (SapM) of Mycobacterium tuberculosis is indispensable for arresting phagosomal maturation and growth of the pathogen in guinea pig tissues
    • Puri RV, Reddy PV, Tyagi AK. 2013. Secreted acid phosphatase (SapM) of Mycobacterium tuberculosis is indispensable for arresting phagosomal maturation and growth of the pathogen in guinea pig tissues. PLoS One 8:e70514. http://dx.doi.org/10.1371/journal.pone.0070514.
    • (2013) PLoS One , vol.8
    • Puri, R.V.1    Reddy, P.V.2    Tyagi, A.K.3
  • 13
    • 0024288466 scopus 로고
    • Legionella micdadei phosphatase catalyzes the hydrolysis of phosphatidylinositol 4,5- bisphosphate in human neutrophils
    • Saha AK, Dowling JN, Pasculle AW, Glew RH. 1988. Legionella micdadei phosphatase catalyzes the hydrolysis of phosphatidylinositol 4,5- bisphosphate in human neutrophils. Arch. Biochem. Biophys. 265: 94-104. http://dx.doi.org/10.1016/0003-9861(88)90375-X.
    • (1988) Arch. Biochem. Biophys , vol.265 , pp. 94-104
    • Saha, A.K.1    Dowling, J.N.2    Pasculle, A.W.3    Glew, R.H.4
  • 14
    • 0037124122 scopus 로고    scopus 로고
    • Molecular dissection of the functional domains of a unique, tartrate-resistant, surface membrane acid phosphatase in the primitive human pathogen Leishmania donovani
    • Shakarian AM, Joshi MB, Ghedin E, Dwyer DM. 2002. Molecular dissection of the functional domains of a unique, tartrate-resistant, surface membrane acid phosphatase in the primitive human pathogen Leishmania donovani. J. Biol. Chem. 277:17994 -18001. http://dx.doi.org/ 10.1074/jbc.M200114200.
    • (2002) J. Biol. Chem , vol.277 , pp. 17994-18001
    • Shakarian, A.M.1    Joshi, M.B.2    Ghedin, E.3    Dwyer, D.M.4
  • 16
    • 78951479850 scopus 로고    scopus 로고
    • Novel acid phosphatase in Candida glabrata suggests selective pressure and niche specialization in the phosphate signal transduction pathway
    • Orkwis BR, Davies DL, Kerwin CL, Sanglard D, Wykoff DD. 2010. Novel acid phosphatase in Candida glabrata suggests selective pressure and niche specialization in the phosphate signal transduction pathway. Genetics 186:885-895. http://dx.doi.org/10.1534/genetics.110.120824.
    • (2010) Genetics , vol.186 , pp. 885-895
    • Orkwis, B.R.1    Davies, D.L.2    Kerwin, C.L.3    Sanglard, D.4    Wykoff, D.D.5
  • 18
    • 6444240424 scopus 로고    scopus 로고
    • Ectophosphatase activity in conidial forms of Fonsecaea pedrosoi is modulated by exogenous phosphate and influences fungal adhesion to mammalian cells
    • Kneipp LF, Rodrigues ML, Holandino C, Esteves FF, Souto-Padrón T, Alviano CS, Travassos LR, Meyer-Fernandes JR. 2004. Ectophosphatase activity in conidial forms of Fonsecaea pedrosoi is modulated by exogenous phosphate and influences fungal adhesion to mammalian cells. Microbiology 150:3355-3362. http://dx.doi.org/10.1099/mic.0.27405-0.
    • (2004) Microbiology , vol.150 , pp. 3355-3362
    • Kneipp, L.F.1    Rodrigues, M.L.2    Holandino, C.3    Esteves, F.F.4    Souto-Padrón, T.5    Alviano, C.S.6    Travassos, L.R.7    Meyer-Fernandes, J.R.8
  • 19
    • 84863893091 scopus 로고    scopus 로고
    • Inorganic phosphate as an important regulator of phosphatases
    • Dick CF, Dos-Santos AL, Meyer-Fernandes JR. 2011. Inorganic phosphate as an important regulator of phosphatases. Enzyme Res. 2011: 103980.
    • (2011) Enzyme Res , vol.2011
    • Dick, C.F.1    Dos-Santos, A.L.2    Meyer-Fernandes, J.R.3
  • 20
    • 0031427079 scopus 로고    scopus 로고
    • The phosphatase system in Saccharomyces cerevisiae
    • Oshima Y. 1997. The phosphatase system in Saccharomyces cerevisiae. Genes Genet. Syst. 72:323-334. http://dx.doi.org/10.1266/ggs.72.323.
    • (1997) Genes Genet. Syst , vol.72 , pp. 323-334
    • Oshima, Y.1
  • 21
    • 0025607931 scopus 로고
    • The yeast phosphatase system
    • Vogel K, Hinnen A. 1990. The yeast phosphatase system. Mol. Microbiol. 4:2013-2017. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00560.x.
    • (1990) Mol. Microbiol , vol.4 , pp. 2013-2017
    • Vogel, K.1    Hinnen, A.2
  • 22
    • 84860559037 scopus 로고    scopus 로고
    • Unravelling secretion in Cryptococcus neoformans: More than one way to skin a cat
    • Rodrigues ML, Djordjevic JT. 2012. Unravelling secretion in Cryptococcus neoformans: more than one way to skin a cat. Mycopathologia 173: 407-418. http://dx.doi.org/10.1007/s11046-011-9468-9.
    • (2012) Mycopathologia , vol.173 , pp. 407-418
    • Rodrigues, M.L.1    Djordjevic, J.T.2
  • 24
    • 77956858246 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the secretome of Candida albicans
    • Sorgo AG, Heilmann CJ, Dekker HL, Brul S, de Koster CG, Klis FM. 2010. Mass spectrometric analysis of the secretome of Candida albicans. Yeast 27:661-672. http://dx.doi.org/10.1002/yea.1775.
    • (2010) Yeast , vol.27 , pp. 661-672
    • Sorgo, A.G.1    Heilmann, C.J.2    Dekker, H.L.3    Brul, S.4    de Koster, C.G.5    Klis, F.M.6
  • 27
    • 65449128888 scopus 로고    scopus 로고
    • Phospholipid transfer protein Sec14 is required for trafficking from endosomes and regulates distinct trans-Golgi export pathways
    • Curwin AJ, Fairn GD, McMaster CR. 2009. Phospholipid transfer protein Sec14 is required for trafficking from endosomes and regulates distinct trans-Golgi export pathways. J. Biol. Chem. 284:7364-7375. http:// dx.doi.org/10.1074/jbc.M808732200.
    • (2009) J. Biol. Chem , vol.284 , pp. 7364-7375
    • Curwin, A.J.1    Fairn, G.D.2    McMaster, C.R.3
  • 29
    • 34249034938 scopus 로고    scopus 로고
    • Extracellular glycosylphosphatidylinositol-anchored mannoproteins and proteases of Cryptococcus neoformans
    • Eigenheer RA, Jin Lee Y, Blumwald E, Phinney BS, Gelli A. 2007. Extracellular glycosylphosphatidylinositol-anchored mannoproteins and proteases of Cryptococcus neoformans. FEMS Yeast Res. 7:499-510. http:// dx.doi.org/10.1111/j.1567-1364.2006.00198.x.
    • (2007) FEMS Yeast Res , vol.7 , pp. 499-510
    • Eigenheer, R.A.1    Jin Lee, Y.2    Blumwald, E.3    Phinney, B.S.4    Gelli, A.5
  • 30
  • 31
    • 38749083839 scopus 로고    scopus 로고
    • The histidine phosphatase superfamily: Structure and function
    • Rigden DJ. 2008. The histidine phosphatase superfamily: structure and function. Biochem. J. 409:333-348. http://dx.doi.org/10.1042/ BJ20071097.
    • (2008) Biochem. J , vol.409 , pp. 333-348
    • Rigden, D.J.1
  • 32
    • 0036138545 scopus 로고    scopus 로고
    • Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed)
    • Bevis BJ, Glick BS. 2002. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat. Biotechnol. 20:83- 87. http:// dx.doi.org/10.1038/nbt0102-83.
    • (2002) Nat. Biotechnol , vol.20 , pp. 83-87
    • Bevis, B.J.1    Glick, B.S.2
  • 33
    • 0024401822 scopus 로고
    • Functional analysis of the signal-sequence processing site of yeast acid phosphatase
    • Monod M, Haguenauer-Tsapis R, Rauseo-Koenig I, Hinnen A. 1989. Functional analysis of the signal-sequence processing site of yeast acid phosphatase. Eur. J. Biochem. 182:213-221.
    • (1989) Eur. J. Biochem , vol.182 , pp. 213-221
    • Monod, M.1    Haguenauer-Tsapis, R.2    Rauseo-Koenig, I.3    Hinnen, A.4
  • 34
    • 0037148531 scopus 로고    scopus 로고
    • A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway
    • Harsay E, Schekman R. 2002. A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J. Cell Biol. 156:271-285. http://dx.doi.org/10.1083/jcb.200109077.
    • (2002) J. Cell Biol , vol.156 , pp. 271-285
    • Harsay, E.1    Schekman, R.2
  • 35
    • 84884790029 scopus 로고    scopus 로고
    • An acidic microenvironment increases NK cell killing of Cryptococcus neoformans and Cryptococcus gattii by enhancing perforin degranulation
    • Islam A, Li SS, Oykhman P, Timm-McCann M, Huston SM, Stack D, Xiang RF, Kelly MM, Mody CH. 2013. An acidic microenvironment increases NK cell killing of Cryptococcus neoformans and Cryptococcus gattii by enhancing perforin degranulation. PLoS Pathog. 9:e1003439. http:// dx.doi.org/10.1371/journal.ppat.1003439.
    • (2013) PLoS Pathog , vol.9
    • Islam, A.1    Li, S.S.2    Oykhman, P.3    Timm-McCann, M.4    Huston, S.M.5    Stack, D.6    Xiang, R.F.7    Kelly, M.M.8    Mody, C.H.9
  • 36
    • 14944341462 scopus 로고    scopus 로고
    • Innate host defense of the lung: Effects of lung-lining fluid pH
    • Ng AW, Bidani A, Heming TA. 2004. Innate host defense of the lung: effects of lung-lining fluid pH. Lung 182:297-317. http://dx.doi.org/ 10.1007/s00408-004-2511-6.
    • (2004) Lung , vol.182 , pp. 297-317
    • Ng, A.W.1    Bidani, A.2    Heming, T.A.3
  • 37
    • 12444317532 scopus 로고    scopus 로고
    • Identification of metabolites of importance in the pathogenesis of pulmonary cryptococcoma using nuclear magnetic resonance spectroscopy
    • Himmelreich U, Allen C, Dowd S, Malik R, Shehan BP, Mountford C, Sorrell TC. 2003. Identification of metabolites of importance in the pathogenesis of pulmonary cryptococcoma using nuclear magnetic resonance spectroscopy. Microbes Infect. 5:285-290. http://dx.doi.org/ 10.1016/S1286-4579(03)00028-5.
    • (2003) Microbes Infect , vol.5 , pp. 285-290
    • Himmelreich, U.1    Allen, C.2    Dowd, S.3    Malik, R.4    Shehan, B.P.5    Mountford, C.6    Sorrell, T.C.7
  • 38
    • 34249736906 scopus 로고    scopus 로고
    • Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans
    • Baker LG, Specht CA, Donlin MJ, Lodge JK. 2007. Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans. Eukaryot. Cell 6:855- 867. http://dx.doi.org/10.1128/ EC.00399-06.
    • (2007) Eukaryot. Cell , vol.6 , pp. 855-867
    • Baker, L.G.1    Specht, C.A.2    Donlin, M.J.3    Lodge, J.K.4
  • 40
    • 0025698194 scopus 로고
    • Cell-wall glucans of Cryptococcus neoformans Cap 67
    • James PG, Cherniak R, Jones RG, Stortz CA, Reiss E. 1990. Cell-wall glucans of Cryptococcus neoformans Cap 67. Carbohydr. Res. 198:23-38. http://dx.doi.org/10.1016/0008-6215(90)84273-W.
    • (1990) Carbohydr. Res , vol.198 , pp. 23-38
    • James, P.G.1    Cherniak, R.2    Jones, R.G.3    Stortz, C.A.4    Reiss, E.5
  • 41
    • 77951185078 scopus 로고    scopus 로고
    • KRE genes are required for beta-1,6- glucan synthesis, maintenance of capsule architecture and cell wall protein anchoring in Cryptococcus neoformans
    • Gilbert NM, Donlin MJ, Gerik KJ, Specht CA, Djordjevic JT, Wilson CF, Sorrell TC, Lodge JK. 2010. KRE genes are required for beta-1,6- glucan synthesis, maintenance of capsule architecture and cell wall protein anchoring in Cryptococcus neoformans. Mol. Microbiol. 76:517-534. http://dx.doi.org/10.1111/j.1365-2958.2010.07119.x.
    • (2010) Mol. Microbiol , vol.76 , pp. 517-534
    • Gilbert, N.M.1    Donlin, M.J.2    Gerik, K.J.3    Specht, C.A.4    Djordjevic, J.T.5    Wilson, C.F.6    Sorrell, T.C.7    Lodge, J.K.8
  • 42
    • 0034685921 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositolanchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall
    • Mouyna I, Fontaine T, Vai M, Monod M, Fonzi WA, Diaquin M, Popolo L, Hartland RP, Latgé JP. 2000. Glycosylphosphatidylinositolanchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall. J. Biol. Chem. 275:14882-14889. http://dx.doi.org/ 10.1074/jbc.275.20.14882.
    • (2000) J. Biol. Chem , vol.275 , pp. 14882-14889
    • Mouyna, I.1    Fontaine, T.2    Vai, M.3    Monod, M.4    Fonzi, W.A.5    Diaquin, M.6    Popolo, L.7    Hartland, R.P.8    Latgé, J.P.9
  • 43
    • 0027537342 scopus 로고
    • Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation
    • Popolo L, Vai M, Gatti E, Porello S, Bonfante P, Balestrini R, Alberghina L. 1993. Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation. J. Bacteriol. 175:1879-1885.
    • (1993) J. Bacteriol , vol.175 , pp. 1879-1885
    • Popolo, L.1    Vai, M.2    Gatti, E.3    Porello, S.4    Bonfante, P.5    Balestrini, R.6    Alberghina, L.7
  • 44
    • 0031938052 scopus 로고    scopus 로고
    • Loss of the plasma membranebound protein Gas1p in Saccharomyces cerevisiae results in the release of _1,3-glucan into the medium and induces a compensation mechanism to ensure cell wall integrity
    • Ram AF, Kapteyn JC, Montijn RC, Caro LH, Douwes JE, Baginsky W, Mazur P, van den Ende H, Klis FM. 1998. Loss of the plasma membranebound protein Gas1p in Saccharomyces cerevisiae results in the release of _1,3-glucan into the medium and induces a compensation mechanism to ensure cell wall integrity. J. Bacteriol. 180:1418-1424.
    • (1998) J. Bacteriol , vol.180 , pp. 1418-1424
    • Ram, A.F.1    Kapteyn, J.C.2    Montijn, R.C.3    Caro, L.H.4    Douwes, J.E.5    Baginsky, W.6    Mazur, P.7    van den Ende, H.8    Klis, F.M.9
  • 47
    • 84875581774 scopus 로고    scopus 로고
    • The mannoprotein Cig1 Supports iron acquisition from heme and virulence in the pathogenic fungus Cryptococcus neoformans
    • Cadieux B, Lian T, Hu G, Wang J, Biondo C, Teti G, Liu V, Murphy ME, Creagh AL, Kronstad JW. 2013. The mannoprotein Cig1 Supports iron acquisition from heme and virulence in the pathogenic fungus Cryptococcus neoformans. J. Infect. Dis. 207:1339 -1347. http://dx.doi.org/ 10.1093/infdis/jit029.
    • (2013) J. Infect. Dis , vol.207 , pp. 1339-1347
    • Cadieux, B.1    Lian, T.2    Hu, G.3    Wang, J.4    Biondo, C.5    Teti, G.6    Liu, V.7    Murphy, M.E.8    Creagh, A.L.9    Kronstad, J.W.10
  • 48
    • 33748929270 scopus 로고    scopus 로고
    • Exosomes: A common pathway for a specialized function
    • van Niel G, Porto-Carreiro I, Simoes S, Raposo G. 2006. Exosomes: a common pathway for a specialized function. J. Biochem. 140:13-21. http://dx.doi.org/10.1093/jb/mvj128.
    • (2006) J. Biochem , vol.140 , pp. 13-21
    • van Niel, G.1    Porto-Carreiro, I.2    Simoes, S.3    Raposo, G.4
  • 50
    • 33749353869 scopus 로고    scopus 로고
    • Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response
    • Bauman SJ, Kuehn MJ. 2006. Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response. Microbes Infect. 8:2400 -2408. http://dx.doi.org/10.1016/ j.micinf.2006.05.001.
    • (2006) Microbes Infect , vol.8 , pp. 2400-2408
    • Bauman, S.J.1    Kuehn, M.J.2
  • 51
    • 0345599951 scopus 로고    scopus 로고
    • Lipid raft-associated protein sorting in exosomes
    • de Gassart A, Geminard C, Fevrier B, Raposo G, Vidal M. 2003. Lipid raft-associated protein sorting in exosomes. Blood 102:4336-4344. http:// dx.doi.org/10.1182/blood-2003-03-0871.
    • (2003) Blood , vol.102 , pp. 4336-4344
    • de Gassart, A.1    Geminard, C.2    Fevrier, B.3    Raposo, G.4    Vidal, M.5
  • 53
    • 0017521638 scopus 로고
    • Localization of acid phospha- tase in Saccharomyces cerevisiae: A clue to cell wall formation
    • Linnemans WA, Boer P, Elbers PF. 1977. Localization of acid phospha- tase in Saccharomyces cerevisiae: a clue to cell wall formation. J. Bacteriol. 131:638-644.
    • (1977) J. Bacteriol , vol.131 , pp. 638-644
    • Linnemans, W.A.1    Boer, P.2    Elbers, P.F.3
  • 54
    • 0032465240 scopus 로고    scopus 로고
    • Lipid mobilization and acid phosphatase activity in lytic compartments during conidium dormancy and appressorium formation of Colletotrichum graminicola
    • Schadeck RJ, Leite B, de Freitas Buchi D. 1998. Lipid mobilization and acid phosphatase activity in lytic compartments during conidium dormancy and appressorium formation of Colletotrichum graminicola. Cell Struct. Funct. 23:333-340. http://dx.doi.org/10.1247/csf.23.333.
    • (1998) Cell Struct. Funct , vol.23 , pp. 333-340
    • Schadeck, R.J.1    Leite, B.2    de Freitas Buchi, D.3
  • 55
    • 77954290084 scopus 로고    scopus 로고
    • Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition
    • Tran HT, Hurley BA, Plaxton WC. 2010. Feeding hungry plants: the role of purple acid phosphatases in phosphate nutrition. Plant Sci. 179:14-27. http://dx.doi.org/10.1016/j.plantsci.2010.04.005.
    • (2010) Plant Sci , vol.179 , pp. 14-27
    • Tran, H.T.1    Hurley, B.A.2    Plaxton, W.C.3
  • 56
    • 77954292773 scopus 로고    scopus 로고
    • The dual-targeted purple acid phosphatase isozyme AtPAP26 is essential for efficient acclimation of Arabidopsis to nutritional phosphate deprivation
    • Hurley BA, Tran HT, Marty NJ, Park J, Snedden WA, Mullen RT, Plaxton WC. 2010. The dual-targeted purple acid phosphatase isozyme AtPAP26 is essential for efficient acclimation of Arabidopsis to nutritional phosphate deprivation. Plant Physiol. 153:1112-1122. http://dx.doi.org/ 10.1104/pp.110.153270.
    • (2010) Plant Physiol , vol.153 , pp. 1112-1122
    • Hurley, B.A.1    Tran, H.T.2    Marty, N.J.3    Park, J.4    Snedden, W.A.5    Mullen, R.T.6    Plaxton, W.C.7
  • 57
    • 77955405132 scopus 로고    scopus 로고
    • Trehalose 6-phosphate phosphatase is required for cell wall integrity and fungal virulence but not trehalose biosynthesis in the human fungal pathogen Aspergillus fumigatus
    • 9 June
    • Puttikamonkul S, Willger SD, Grahl N, Perfect JR, Movahed N, Bothner B, Park S, Paderu P, Perlin DS, Cramer RA, Jr. 9 June 2010. Trehalose 6-phosphate phosphatase is required for cell wall integrity and fungal virulence but not trehalose biosynthesis in the human fungal pathogen Aspergillus fumigatus. Mol. Microbiol. http://dx.doi.org/ 10.1111/j.1365-2958.2010.07254.x.
    • (2010) Mol. Microbiol
    • Puttikamonkul, S.1    Willger, S.D.2    Grahl, N.3    Perfect, J.R.4    Movahed, N.5    Bothner, B.6    Park, S.7    Paderu, P.8    Perlin, D.S.9    Cramer, R.A.10
  • 59
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida TA, Emr SD. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792. http:// dx.doi.org/10.1083/jcb.128.5.779.
    • (1995) J. Cell Biol , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 60
    • 0025019627 scopus 로고
    • Lysosomal acid phosphatase is transported via endosomes to lysosomes
    • Tanaka Y, Yano S, Okada K, Ishikawa T, Himeno M, Kato K. 1990. Lysosomal acid phosphatase is transported via endosomes to lysosomes. Biochem. Biophys. Res. Commun. 166:1176 -1182. http://dx.doi.org/ 10.1016/0006-291X(90)90990-5.
    • (1990) Biochem. Biophys. Res. Commun , vol.166 , pp. 1176-1182
    • Tanaka, Y.1    Yano, S.2    Okada, K.3    Ishikawa, T.4    Himeno, M.5    Kato, K.6
  • 61
    • 0032711653 scopus 로고    scopus 로고
    • The relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cells
    • Fernanado PH, Panagoda GJ, Samaranayake LP. 1999. The relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cells. APMIS 107:1034 -1042. http://dx.doi.org/10.1111/j.1699 -0463.1999.tb01507.x.
    • (1999) APMIS , vol.107 , pp. 1034-1042
    • Fernanado, P.H.1    Panagoda, G.J.2    Samaranayake, L.P.3
  • 63
    • 18744415029 scopus 로고    scopus 로고
    • Metabolites released by Cryptococcus neoformans var. neoformans and var. gattii differentially affect human neutrophil function. Microbes Infect
    • Wright L, Bubb W, Davidson J, Santangelo R, Krockenberger M, Himmelreich U, Sorrell T. 2002. Metabolites released by Cryptococcus neoformans var. neoformans and var. gattii differentially affect human neutrophil function. Microbes Infect. Aprel:1427-1438. http://dx.doi.org/ 10.1016/S1286-4579(02)00024-2.
    • (2002) Aprel , pp. 1427-1438
    • Wright, L.1    Bubb, W.2    Davidson, J.3    Santangelo, R.4    Krockenberger, M.5    Himmelreich, U.6    Sorrell, T.7


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