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Volumn 99, Issue 2, 2015, Pages 601-610

Fungal aegerolysin-like proteins: distribution, activities, and applications

Author keywords

Aegerolysin; Fungal biomarkers; Fungi; Hemolysin; Heterologous expression; Lipid markers

Indexed keywords

BIOMARKERS; BLOOD; DIAGNOSIS; GENE EXPRESSION; LIPIDS; MAMMALS; PROTEINS;

EID: 84925482304     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6239-9     Document Type: Review
Times cited : (26)

References (68)
  • 4
    • 82355182085 scopus 로고    scopus 로고
    • Isolation of a novel promoter for efficient protein expression by Aspergillus oryzae in solid-state culture
    • COI: 1:CAS:528:DC%2BC3MXht1yhur3M, PID: 21732241
    • Bando H, Hisada H, Ishida H, Hata Y, Katakura Y, Kondo A (2011) Isolation of a novel promoter for efficient protein expression by Aspergillus oryzae in solid-state culture. Appl Microbiol Biotechnol 92:561–569. doi:10.1007/s00253-011-3446-5
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 561-569
    • Bando, H.1    Hisada, H.2    Ishida, H.3    Hata, Y.4    Katakura, Y.5    Kondo, A.6
  • 5
    • 0032510775 scopus 로고    scopus 로고
    • Cloning and sequencing of three new putative toxin genes from Clostridium bifermentans CH18
    • COI: 1:CAS:528:DyaK1cXjtl2nu7k%3D, PID: 9602158
    • Barloy F, Lecadet MM, Delécluse A (1998) Cloning and sequencing of three new putative toxin genes from Clostridium bifermentans CH18. Gene 211:293–299
    • (1998) Gene , vol.211 , pp. 293-299
    • Barloy, F.1    Lecadet, M.M.2    Delécluse, A.3
  • 6
    • 0037089465 scopus 로고    scopus 로고
    • Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting
    • COI: 1:CAS:528:DC%2BD38XjvVeitr0%3D, PID: 12020804
    • Berne S, Križaj I, Pohleven F, Turk T, Maček P, Sepčić K (2002) Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting. Biochim Biophys Acta 1570:153–159
    • (2002) Biochim Biophys Acta , vol.1570 , pp. 153-159
    • Berne, S.1    Križaj, I.2    Pohleven, F.3    Turk, T.4    Maček, P.5    Sepčić, K.6
  • 7
    • 63449118079 scopus 로고    scopus 로고
    • Aegerolysins: structure, function, and putative biological role
    • COI: 1:CAS:528:DC%2BD1MXms1ags7s%3D, PID: 19309687
    • Berne S, Lah L, Sepčić K (2009) Aegerolysins: structure, function, and putative biological role. Protein Sci 18:694–706. doi:10.1002/pro.85
    • (2009) Protein Sci , vol.18 , pp. 694-706
    • Berne, S.1    Lah, L.2    Sepčić, K.3
  • 8
    • 50349091327 scopus 로고    scopus 로고
    • Induction of fruiting in oyster mushroom (Pleurotus ostreatus) by polymeric 3-alkylpyridinium salts
    • COI: 1:CAS:528:DC%2BD1cXhtlWitbzJ, PID: 18692375
    • Berne S, Pohleven F, Turk T, Sepčić K (2008) Induction of fruiting in oyster mushroom (Pleurotus ostreatus) by polymeric 3-alkylpyridinium salts. Mycol Res 112:1085–1087. doi:10.1016/j.mycres.2008.03.009
    • (2008) Mycol Res , vol.112 , pp. 1085-1087
    • Berne, S.1    Pohleven, F.2    Turk, T.3    Sepčić, K.4
  • 9
    • 36549088655 scopus 로고    scopus 로고
    • Ostreolysin enhances fruiting initiation in the oyster mushroom (Pleurotus ostreatus)
    • COI: 1:CAS:528:DC%2BD1cXhsVOmt7c%3D, PID: 18037282
    • Berne S, Pohleven J, Vidic I, Rebolj K, Pohleven F, Turk T, Maček P, Sonnenberg A, Sepčić K (2007) Ostreolysin enhances fruiting initiation in the oyster mushroom (Pleurotus ostreatus). Mycol Res 111:1431–1436. doi:10.1016/j.mycres.2007.09.005
    • (2007) Mycol Res , vol.111 , pp. 1431-1436
    • Berne, S.1    Pohleven, J.2    Vidic, I.3    Rebolj, K.4    Pohleven, F.5    Turk, T.6    Maček, P.7    Sonnenberg, A.8    Sepčić, K.9
  • 10
    • 23944453855 scopus 로고    scopus 로고
    • Effect of pH on the pore forming activity and conformational stability of ostreolysin, a lipid raft-binding protein from the edible mushroom Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2MXmvVWgtb4%3D, PID: 16101298
    • Berne S, Sepčić K, Anderluh G, Turk T, Maček P, Poklar Ulrih N (2005) Effect of pH on the pore forming activity and conformational stability of ostreolysin, a lipid raft-binding protein from the edible mushroom Pleurotus ostreatus. Biochemistry 44:11137–11147. doi:10.1021/bi051013y
    • (2005) Biochemistry , vol.44 , pp. 11137-11147
    • Berne, S.1    Sepčić, K.2    Anderluh, G.3    Turk, T.4    Maček, P.5    Poklar Ulrih, N.6
  • 12
    • 77957907451 scopus 로고    scopus 로고
    • An inventory of the Aspergillus niger secretome by combining in-silico predictions with shotgun proteomics data
    • PID: 20959013
    • Braaksma M, Martens-Uzunova ES, Punt PJ, Schaap PJ (2010) An inventory of the Aspergillus niger secretome by combining in-silico predictions with shotgun proteomics data. BMC Genomics 11:584. doi:10.1186/1471-2164-11-584
    • (2010) BMC Genomics , vol.11 , pp. 584
    • Braaksma, M.1    Martens-Uzunova, E.S.2    Punt, P.J.3    Schaap, P.J.4
  • 13
    • 0037469341 scopus 로고    scopus 로고
    • Growth promotion of the edible fungus Pleurotus ostreatus by fluorescent pseudomonads
    • COI: 1:CAS:528:DC%2BD3sXhtVGjtL0%3D, PID: 12586403
    • Cho YS, Kim JS, Crowley DE, Cho BG (2003) Growth promotion of the edible fungus Pleurotus ostreatus by fluorescent pseudomonads. FEMS Microbiol Lett 218:271–276
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 271-276
    • Cho, Y.S.1    Kim, J.S.2    Crowley, D.E.3    Cho, B.G.4
  • 14
    • 44949199084 scopus 로고    scopus 로고
    • Lysophospholipids prevent binding of a cytolytic protein ostreolysin to cholesterol-enriched membrane domains
    • COI: 1:CAS:528:DC%2BD1cXmvVGjtb4%3D, PID: 18455213
    • Chowdhury HH, Rebolj K, Kreft M, Zorec R, Maček P, Sepčić K (2008) Lysophospholipids prevent binding of a cytolytic protein ostreolysin to cholesterol-enriched membrane domains. Toxicon 51:1345–1356. doi:10.1016/j.toxicon.2008.03.010
    • (2008) Toxicon , vol.51 , pp. 1345-1356
    • Chowdhury, H.H.1    Rebolj, K.2    Kreft, M.3    Zorec, R.4    Maček, P.5    Sepčić, K.6
  • 15
    • 0742307287 scopus 로고    scopus 로고
    • β-Adenosine, a bioactive compound in grass chaff stimulating mushroom production
    • COI: 1:CAS:528:DC%2BD2cXjsVyjsQ%3D%3D, PID: 14732277
    • Domondon DL, He W, De Kimpe N, Höfte M, Poppe J (2004) β-Adenosine, a bioactive compound in grass chaff stimulating mushroom production. Phytochemistry 65:181–187. doi:10.1016/j.phytochem.2003.11.004
    • (2004) Phytochemistry , vol.65 , pp. 181-187
    • Domondon, D.L.1    He, W.2    De Kimpe, N.3    Höfte, M.4    Poppe, J.5
  • 16
    • 31044456712 scopus 로고    scopus 로고
    • Characterization of nigerlysin, hemolysin produced by Aspergillus niger, and effect on mouse neuronal cells in vitro
    • COI: 1:CAS:528:DC%2BD28Xls1elsw%3D%3D, PID: 16338047
    • Donohue M, Wei W, Wu J, Zawia NH, Hud N, De Jesus V, Schmechel D, Hettick JM, Beezhold DH, Vesper S (2006) Characterization of nigerlysin, hemolysin produced by Aspergillus niger, and effect on mouse neuronal cells in vitro. Toxicology 219:150–155. doi:10.1016/j.tox.2005.11.013
    • (2006) Toxicology , vol.219 , pp. 150-155
    • Donohue, M.1    Wei, W.2    Wu, J.3    Zawia, N.H.4    Hud, N.5    De Jesus, V.6    Schmechel, D.7    Hettick, J.M.8    Beezhold, D.H.9    Vesper, S.10
  • 17
    • 0020285699 scopus 로고
    • Studies on toxin of Aspergillus fumigatus. XIV. Relationship between Asp-hemolysin and experimental infection for mice
    • Ebina K, Yokota K, Sakaguchi O (1982) Studies on toxin of Aspergillus fumigatus. XIV. Relationship between Asp-hemolysin and experimental infection for mice. Jpn J Med Mycol 23:246–252
    • (1982) Jpn J Med Mycol , vol.23 , pp. 246-252
    • Ebina, K.1    Yokota, K.2    Sakaguchi, O.3
  • 18
    • 0027936215 scopus 로고
    • Cloning and nucleotide sequence of cDNA encoding Asp-hemolysin from Aspergillus fumigatus
    • COI: 1:CAS:528:DyaK2cXmslent7k%3D, PID: 8086452
    • Ebina K, Sakagami H, Yokota K, Kondo H (1994) Cloning and nucleotide sequence of cDNA encoding Asp-hemolysin from Aspergillus fumigatus. Biochim Biophys Acta 1219:148–150
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 148-150
    • Ebina, K.1    Sakagami, H.2    Yokota, K.3    Kondo, H.4
  • 19
    • 84860008663 scopus 로고    scopus 로고
    • Proteins of higher fungi—from forest to application
    • COI: 1:CAS:528:DC%2BC38XjtVyiuro%3D, PID: 22341093
    • Erjavec J, Kos J, Ravnikar M, Dreo T, Sabotič J (2012) Proteins of higher fungi—from forest to application. Trends Biotechnol 30:259–273. doi:10.1016/j.tibtech.2012.01.004
    • (2012) Trends Biotechnol , vol.30 , pp. 259-273
    • Erjavec, J.1    Kos, J.2    Ravnikar, M.3    Dreo, T.4    Sabotič, J.5
  • 20
    • 2642601131 scopus 로고    scopus 로고
    • Cloning and sequencing of the Aa-Pri1 gene specifically expressed during fruiting initiation in the edible mushroom Agrocybe aegerita, and analysis of the predicted amino-acid sequence
    • COI: 1:CAS:528:DyaK2sXns1ChtLg%3D, PID: 9388298
    • Fernandez Espinar M, Labarere J (1997) Cloning and sequencing of the Aa-Pri1 gene specifically expressed during fruiting initiation in the edible mushroom Agrocybe aegerita, and analysis of the predicted amino-acid sequence. Curr Genet 32:420–424
    • (1997) Curr Genet , vol.32 , pp. 420-424
    • Fernandez Espinar, M.1    Labarere, J.2
  • 23
  • 26
    • 84925501418 scopus 로고    scopus 로고
    • Herstellung und Charakterisierung monoklonaler Antikörper gegen sezernierte Moleküle des human pathogenen Schimmelpilzes Aspergillus fumigatus
    • Heesemann L (2010) Herstellung und Charakterisierung monoklonaler Antikörper gegen sezernierte Moleküle des human pathogenen Schimmelpilzes Aspergillus fumigatus. Ludwig-Maximillians-Universitat zu Munchen
    • (2010) Ludwig-Maximillians-Universitat zu Munchen
    • Heesemann, L.1
  • 27
    • 84873992167 scopus 로고    scopus 로고
    • High production of llama variable heavy-chain antibody fragment (VHH) fused to various reader proteins by Aspergillus oryzae
    • COI: 1:CAS:528:DC%2BC3sXosFSrsg%3D%3D, PID: 22752366
    • Hisada H, Tsutsumi H, Ishida H, Hata Y (2013) High production of llama variable heavy-chain antibody fragment (VHH) fused to various reader proteins by Aspergillus oryzae. Appl Microbiol Biotechnol 97:761–766. doi:10.1007/s00253-012-4211-0
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 761-766
    • Hisada, H.1    Tsutsumi, H.2    Ishida, H.3    Hata, Y.4
  • 28
    • 4444336073 scopus 로고
    • Endotoxin-like substance from Aspergillus fumigatus
    • Iwata K, Matsuda A, Wakabayashi K, Fununaga N (1962) Endotoxin-like substance from Aspergillus fumigatus. Jpn J Med Mycol 3:66–73. doi:10.3314/jjmm1960.3.66
    • (1962) Jpn J Med Mycol , vol.3 , pp. 66-73
    • Iwata, K.1    Matsuda, A.2    Wakabayashi, K.3    Fununaga, N.4
  • 29
  • 30
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: a case study using the Phyre server
    • COI: 1:CAS:528:DC%2BD1MXivF2itbs%3D, PID: 19247286
    • Kelley LA, Sternberg MJE (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat Protoc 4:363–371
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 31
    • 0035915501 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein-binding specificity of Asp-hemolysin from Aspergillus fumigatus
    • COI: 1:CAS:528:DC%2BD38XitFaguw%3D%3D, PID: 11786224
    • Kudo Y, Fukuchi Y, Kumagai T, Ebina K, Yokota K (2001) Oxidized low-density lipoprotein-binding specificity of Asp-hemolysin from Aspergillus fumigatus. Biochim Biophys Acta 1568:183–188. doi:10.1016/S0304-4165(01)00217-3
    • (2001) Biochim Biophys Acta , vol.1568 , pp. 183-188
    • Kudo, Y.1    Fukuchi, Y.2    Kumagai, T.3    Ebina, K.4    Yokota, K.5
  • 32
    • 0035071156 scopus 로고    scopus 로고
    • Cytotoxic activity and cytokine gene induction of Asp-hemolysin to vascular endothelial cells
    • COI: 1:CAS:528:DC%2BD3MXisVShtbs%3D
    • Kumagai T, Nagata T, Kudo Y, Fukuchi Y, Ebina K, Yokota K (2001) Cytotoxic activity and cytokine gene induction of Asp-hemolysin to vascular endothelial cells. J Pharm Soc Jpn 121:271–275
    • (2001) J Pharm Soc Jpn , vol.121 , pp. 271-275
    • Kumagai, T.1    Nagata, T.2    Kudo, Y.3    Fukuchi, Y.4    Ebina, K.5    Yokota, K.6
  • 33
    • 0033257454 scopus 로고    scopus 로고
    • Cytotoxic activity and cytokine gene induction of Asp-hemolysin to murine macrophages
    • COI: 1:CAS:528:DC%2BD3cXhvVKksA%3D%3D
    • Kumagai T, Nagata T, Kudo Y, Fukuchi Y, Ebina K, Yokota K (1999) Cytotoxic activity and cytokine gene induction of Asp-hemolysin to murine macrophages. Jpn J Med Mycol 40:217–222
    • (1999) Jpn J Med Mycol , vol.40 , pp. 217-222
    • Kumagai, T.1    Nagata, T.2    Kudo, Y.3    Fukuchi, Y.4    Ebina, K.5    Yokota, K.6
  • 34
    • 84925498213 scopus 로고    scopus 로고
    • Homologous genes, Pe.pleurotolysin A and Pe.ostreolysin, are both specifically and highly expressed in primordia and young fruiting bodies of Pleurotus eryngii
    • COI: 1:CAS:528:DC%2BC2cXivVGhsQ%3D%3D
    • Kurahashi A, Sato M, Kobayashi T, Nishibori K, Fujimori F (2014) Homologous genes, Pe.pleurotolysin A and Pe.ostreolysin, are both specifically and highly expressed in primordia and young fruiting bodies of Pleurotus eryngii. Mycoscience 55:113–117. doi:10.1016/j.myc.2013.06.005
    • (2014) Mycoscience , vol.55 , pp. 113-117
    • Kurahashi, A.1    Sato, M.2    Kobayashi, T.3    Nishibori, K.4    Fujimori, F.5
  • 37
    • 0000930636 scopus 로고    scopus 로고
    • Saponin stimulates fruiting of the edible basidiomycete Pleurotus ostreatus
    • COI: 1:CAS:528:DyaK1MXnt1GjtLo%3D
    • Magae Y (1999) Saponin stimulates fruiting of the edible basidiomycete Pleurotus ostreatus. Biosci Biotechnol Biochem 63:1840–1842
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1840-1842
    • Magae, Y.1
  • 38
    • 68449088768 scopus 로고    scopus 로고
    • An active compound for fruiting body induction
    • COI: 1:CAS:528:DC%2BD1MXmvVWru7c%3D
    • Magae Y, Nishimura T, Ohara S (2009) An active compound for fruiting body induction. Curr Chem Biol 3:231–237
    • (2009) Curr Chem Biol , vol.3 , pp. 231-237
    • Magae, Y.1    Nishimura, T.2    Ohara, S.3
  • 39
    • 18244404613 scopus 로고    scopus 로고
    • 3-O-Alkyl-D-glucose derivatives induce fruit bodies of Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2MXisFKhtLk%3D, PID: 15912955
    • Magae Y, Nishimura T, Ohara S (2005) 3-O-Alkyl-D-glucose derivatives induce fruit bodies of Pleurotus ostreatus. Mycol Res 109:374–376. doi:10.1017/S0953756204002096
    • (2005) Mycol Res , vol.109 , pp. 374-376
    • Magae, Y.1    Nishimura, T.2    Ohara, S.3
  • 40
    • 84870914281 scopus 로고    scopus 로고
    • Fungal hemolysins
    • COI: 1:CAS:528:DC%2BC38XhvVeltLzO, PID: 22769586
    • Nayak AP, Green BJ, Beezhold DH (2013) Fungal hemolysins. Med Mycol 51:1–16. doi:10.3109/13693786.2012.698025
    • (2013) Med Mycol , vol.51 , pp. 1-16
    • Nayak, A.P.1    Green, B.J.2    Beezhold, D.H.3
  • 41
    • 84858133939 scopus 로고    scopus 로고
    • Development of monoclonal antibodies to recombinant terrelysin and characterization of expression in Aspergillus terreus
    • COI: 1:CAS:528:DC%2BC38XotFKgu70%3D, PID: 22160315
    • Nayak AP, Green BJ, Friend S, Beezhold DH (2012) Development of monoclonal antibodies to recombinant terrelysin and characterization of expression in Aspergillus terreus. J Med Microbiol 61:489–499. doi:10.1099/jmm. 0.039511-0
    • (2012) J Med Microbiol , vol.61 , pp. 489-499
    • Nayak, A.P.1    Green, B.J.2    Friend, S.3    Beezhold, D.H.4
  • 42
    • 78650515518 scopus 로고    scopus 로고
    • Characterization of recombinant terrelysin, a hemolysin of Aspergillus terreus
    • COI: 1:CAS:528:DC%2BC3cXhsF2htb3E, PID: 20632211
    • Nayak AP, Blachere FM, Hettick JM, Lukomski S, Schmechel D, Beezhold DH (2011a) Characterization of recombinant terrelysin, a hemolysin of Aspergillus terreus. Mycopathologia 171:23–34. doi:10.1007/s11046-010-9343-0
    • (2011) Mycopathologia , vol.171 , pp. 23-34
    • Nayak, A.P.1    Blachere, F.M.2    Hettick, J.M.3    Lukomski, S.4    Schmechel, D.5    Beezhold, D.H.6
  • 43
    • 80052470869 scopus 로고    scopus 로고
    • Monoclonal antibodies to hyphal exoantigens derived from the opportunistic pathogen Aspergillus terreus
    • COI: 1:CAS:528:DC%2BC3MXhtF2hsbrN, PID: 21734068
    • Nayak AP, Green BJ, Janotka E, Hettick JM, Friend S, Vesper SJ, Schmechel D, Beezhold DH (2011b) Monoclonal antibodies to hyphal exoantigens derived from the opportunistic pathogen Aspergillus terreus. Clin Vaccine Immunol 18:1568–1576. doi:10.1128/CVI. 05163-11
    • (2011) Clin Vaccine Immunol , vol.18 , pp. 1568-1576
    • Nayak, A.P.1    Green, B.J.2    Janotka, E.3    Hettick, J.M.4    Friend, S.5    Vesper, S.J.6    Schmechel, D.7    Beezhold, D.H.8
  • 44
    • 84904799374 scopus 로고    scopus 로고
    • Targeted lipid analysis of haemolytic mycelial extracts of Aspergillus niger
    • COI: 1:CAS:528:DC%2BC2cXht1CmsL%2FP, PID: 24983857
    • Novak M, Sepčić K, Kraševec N, Križaj I, Maček P, Anderluh G, Guella G, Mancini I (2014) Targeted lipid analysis of haemolytic mycelial extracts of Aspergillus niger. Molecules 19:9051–9069. doi:10.3390/molecules19079051
    • (2014) Molecules , vol.19 , pp. 9051-9069
    • Novak, M.1    Sepčić, K.2    Kraševec, N.3    Križaj, I.4    Maček, P.5    Anderluh, G.6    Guella, G.7    Mancini, I.8
  • 45
    • 84904790227 scopus 로고    scopus 로고
    • Fungal MACPF-like proteins and aegerolysins: bi-component pore-forming proteins?
    • PID: 24798017
    • Ota K, Butala M, Viero G, Dalla Serra M, Sepčić K, Maček P (2014) Fungal MACPF-like proteins and aegerolysins: bi-component pore-forming proteins? Subcell Biochem 80:271–291
    • (2014) Subcell Biochem , vol.80 , pp. 271-291
    • Ota, K.1    Butala, M.2    Viero, G.3    Dalla Serra, M.4    Sepčić, K.5    Maček, P.6
  • 46
    • 84883238674 scopus 로고    scopus 로고
    • Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B
    • COI: 1:CAS:528:DC%2BC3sXhtVOrsL7K, PID: 23806422
    • Ota K, Leonardi A, Mikelj M, Skočaj M, Wohlschlager T, Künzler M, Aebi M, Narat M, Križaj I, Anderluh G, Sepčić K, Maček P (2013) Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B. Biochimie 95:1855–1864. doi:10.1016/j.biochi.2013.06.012
    • (2013) Biochimie , vol.95 , pp. 1855-1864
    • Ota, K.1    Leonardi, A.2    Mikelj, M.3    Skočaj, M.4    Wohlschlager, T.5    Künzler, M.6    Aebi, M.7    Narat, M.8    Križaj, I.9    Anderluh, G.10    Sepčić, K.11    Maček, P.12
  • 48
    • 33749060200 scopus 로고    scopus 로고
    • Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers
    • COI: 1:CAS:528:DC%2BD28XhtVGis7zO, PID: 16857161
    • Rebolj K, Ulrih NP, Maček P, Sepčić K (2006) Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers. Biochim Biophys Acta 1758:1662–1670. doi:10.1016/j.bbamem.2006.06.003
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1662-1670
    • Rebolj, K.1    Ulrih, N.P.2    Maček, P.3    Sepčić, K.4
  • 49
    • 78651404102 scopus 로고    scopus 로고
    • Desmosome assembly and cell-cell adhesion are membrane raft-dependent processes
    • COI: 1:CAS:528:DC%2BC3MXjtFegtw%3D%3D, PID: 21071449
    • Resnik N, Sepčić K, Plemenitaš A, Windoffer R, Leube R, Veranič P (2011) Desmosome assembly and cell-cell adhesion are membrane raft-dependent processes. J Biol Chem 286:1499–1507. doi:10.1074/jbc.M110.189464
    • (2011) J Biol Chem , vol.286 , pp. 1499-1507
    • Resnik, N.1    Sepčić, K.2    Plemenitaš, A.3    Windoffer, R.4    Leube, R.5    Veranič, P.6
  • 50
    • 84859431773 scopus 로고    scopus 로고
    • Differential gene expression in Alternaria gaisen exposed to dark and light
    • Roberts RG, Bischoff JF, Reymond ST (2011) Differential gene expression in Alternaria gaisen exposed to dark and light. Mycol Prog 11:373–382. doi:10.1007/s11557-011-0752-3
    • (2011) Mycol Prog , vol.11 , pp. 373-382
    • Roberts, R.G.1    Bischoff, J.F.2    Reymond, S.T.3
  • 52
    • 0016566893 scopus 로고
    • Proceedings: Purification and characteristics of hemolytic toxin from Aspergillus fumigatus
    • COI: 1:CAS:528:DyaE28XksFOktbk%3D, PID: 778450
    • Sakaguchi O, Shimada H, Yokota K (1975) Proceedings: Purification and characteristics of hemolytic toxin from Aspergillus fumigatus. Jpn J Med Sci Biol 28:328–331
    • (1975) Jpn J Med Sci Biol , vol.28 , pp. 328-331
    • Sakaguchi, O.1    Shimada, H.2    Yokota, K.3
  • 53
    • 0028079980 scopus 로고
    • Lysophosphatidylcholine plays an essential role in the mitogenic effect of oxidized low density lipoprotein on murine macrophages
    • COI: 1:CAS:528:DyaK2cXmvFyhsbw%3D, PID: 7989310
    • Sakai M, Miyazaki A, Hakamata H, Sasaki T, Yui S, Yamazaki M, Shichiri M, Horiuchi S (1994) Lysophosphatidylcholine plays an essential role in the mitogenic effect of oxidized low density lipoprotein on murine macrophages. J Biol Chem 269:31430–31435
    • (1994) J Biol Chem , vol.269 , pp. 31430-31435
    • Sakai, M.1    Miyazaki, A.2    Hakamata, H.3    Sasaki, T.4    Yui, S.5    Yamazaki, M.6    Shichiri, M.7    Horiuchi, S.8
  • 54
    • 85057636114 scopus 로고    scopus 로고
    • Modified Cry34 proteins
    • Schnepf HE (2013) Modified Cry34 proteins. US 8,372,803 B2
    • (2013) US 8,372 , vol.803 , pp. B2
    • Schnepf, H.E.1
  • 55
    • 17444380109 scopus 로고    scopus 로고
    • Characterization of Cry34/Cry35 binary insecticidal proteins from diverse Bacillus thuringiensis strain collections
    • COI: 1:CAS:528:DC%2BD2MXjsVOqt7o%3D, PID: 15811999
    • Schnepf HE, Lee S, Dojillo J, Burmeister P, Fencil K, Morera L, Nygaard L, Narva KE, Wolt JD (2005) Characterization of Cry34/Cry35 binary insecticidal proteins from diverse Bacillus thuringiensis strain collections. Appl Environ Microbiol 71:1765–1774. doi:10.1128/AEM. 71.4.1765-1774.2005
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1765-1774
    • Schnepf, H.E.1    Lee, S.2    Dojillo, J.3    Burmeister, P.4    Fencil, K.5    Morera, L.6    Nygaard, L.7    Narva, K.E.8    Wolt, J.D.9
  • 57
    • 84859972408 scopus 로고    scopus 로고
    • Nuclear ribosomal internal transcribed spacer (ITS) region as a universal DNA barcode marker for Fungi
    • COI: 1:CAS:528:DC%2BC38Xmt12mu7o%3D, PID: 22454494
    • Schoch CL, Seifert KA, Huhndorf S, Robert V, Spouge JL, Levesque CA, Chen W (2012) Nuclear ribosomal internal transcribed spacer (ITS) region as a universal DNA barcode marker for Fungi. Proc Natl Acad Sci U S A 109:6241–6246. doi:10.1073/pnas.1117018109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6241-6246
    • Schoch, C.L.1    Seifert, K.A.2    Huhndorf, S.3    Robert, V.4    Spouge, J.L.5    Levesque, C.A.6    Chen, W.7
  • 58
    • 4544239246 scopus 로고    scopus 로고
    • Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains
    • PID: 15388337
    • Sepčić K, Berne S, Rebolj K, Batista U, Plemenitaš A, Šentjurc M, Maček P (2004) Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains. FEBS Lett 575:81–85. doi:10.1016/j.febslet.2004.07.093
    • (2004) FEBS Lett , vol.575 , pp. 81-85
    • Sepčić, K.1    Berne, S.2    Rebolj, K.3    Batista, U.4    Plemenitaš, A.5    Šentjurc, M.6    Maček, P.7
  • 59
    • 77958479289 scopus 로고    scopus 로고
    • Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii
    • COI: 1:CAS:528:DC%2BC3cXhtlGntbzI, PID: 20816689
    • Shibata T, Kudou M, Hoshi Y, Kudo A, Nanashima N, Miyairi K (2010) Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii. Toxicon 56:1436–1442. doi:10.1016/j.toxicon.2010.08.010
    • (2010) Toxicon , vol.56 , pp. 1436-1442
    • Shibata, T.1    Kudou, M.2    Hoshi, Y.3    Kudo, A.4    Nanashima, N.5    Miyairi, K.6
  • 62
    • 0035862439 scopus 로고    scopus 로고
    • Veratryl alcohol stimulates fruiting body formation in the oyster mushroom, Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD3MXksVahtg%3D%3D, PID: 11164314
    • Suguimoto HH, Barbosa AM, Dekker RF, Castro-Gomez RJ (2001) Veratryl alcohol stimulates fruiting body formation in the oyster mushroom, Pleurotus ostreatus. FEMS Microbiol Lett 194:235–238. doi:10.1111/j.1574-6968.2001.tb09475.x
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 235-238
    • Suguimoto, H.H.1    Barbosa, A.M.2    Dekker, R.F.3    Castro-Gomez, R.J.4
  • 63
    • 3042555480 scopus 로고    scopus 로고
    • Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex
    • COI: 1:CAS:528:DC%2BD2cXkvFGnsrg%3D, PID: 15084605
    • Tomita T, Noguchi K, Mimuro H, Ukaji F, Ito K, Sugawara-Tomita N, Hashimoto Y (2004) Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex. J Biol Chem 279:26975–26982. doi:10.1074/jbc.M402676200
    • (2004) J Biol Chem , vol.279 , pp. 26975-26982
    • Tomita, T.1    Noguchi, K.2    Mimuro, H.3    Ukaji, F.4    Ito, K.5    Sugawara-Tomita, N.6    Hashimoto, Y.7
  • 64
    • 0027350612 scopus 로고
    • Effect of phenol on the mycelial growth and fructification in some of basidiomycetous fungi
    • COI: 1:CAS:528:DyaK2cXitFahtbk%3D, PID: 8229674
    • Upadhyay RC, Hofrichter M (1993) Effect of phenol on the mycelial growth and fructification in some of basidiomycetous fungi. J Basic Microbiol 33:343–347
    • (1993) J Basic Microbiol , vol.33 , pp. 343-347
    • Upadhyay, R.C.1    Hofrichter, M.2
  • 65
    • 4444247498 scopus 로고    scopus 로고
    • Possible role of fungal hemolysins in sick building syndrome
    • COI: 1:CAS:528:DC%2BD2cXhtVentL3E, PID: 15350795
    • Vesper S, Vesper M (2004) Possible role of fungal hemolysins in sick building syndrome. Adv Appl Microbiol 55:191–208
    • (2004) Adv Appl Microbiol , vol.55 , pp. 191-208
    • Vesper, S.1    Vesper, M.2
  • 66
    • 18244367696 scopus 로고    scopus 로고
    • Temporal and spatial expression of ostreolysin during development of the oyster mushroom (Pleurotus ostreatus)
    • COI: 1:CAS:528:DC%2BD2MXisFKhtLY%3D, PID: 15912956
    • Vidic I, Berne S, Drobne D, Maček P, Frangež R, Turk T, Štrus J, Sepčić K (2005) Temporal and spatial expression of ostreolysin during development of the oyster mushroom (Pleurotus ostreatus). Mycol Res 109:377–382. doi:10.1017/S0953756204002187
    • (2005) Mycol Res , vol.109 , pp. 377-382
    • Vidic, I.1    Berne, S.2    Drobne, D.3    Maček, P.4    Frangež, R.5    Turk, T.6    Štrus, J.7    Sepčić, K.8
  • 67
    • 80052761783 scopus 로고    scopus 로고
    • Secretome analysis of Aspergillus fumigatus reveals Asp-hemolysin as a major secreted protein
    • COI: 1:CAS:528:DC%2BC3MXhtFKjtLbF, PID: 21658997
    • Wartenberg D, Lapp K, Jacobsen ID, Dahse H-M, Kniemeyer O, Heinekamp T, Brakhage AA (2011) Secretome analysis of Aspergillus fumigatus reveals Asp-hemolysin as a major secreted protein. Int J Med Microbiol 301:602–611. doi:10.1016/j.ijmm.2011.04.016
    • (2011) Int J Med Microbiol , vol.301 , pp. 602-611
    • Wartenberg, D.1    Lapp, K.2    Jacobsen, I.D.3    Dahse, H.-M.4    Kniemeyer, O.5    Heinekamp, T.6    Brakhage, A.A.7


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