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Volumn 18, Issue 4, 2009, Pages 694-706

Aegerolysins: Structure, function, and putative biological role

Author keywords

Aegerolysin; Aspergillus; Hemolytic protein; Lipid raft; Mushroom; Pleurotus; Protein family

Indexed keywords

AEGEROLYSIN; ASPERGILLUS FUMIGATUS HEMOLYSIN; BIOLOGICAL MARKER; CYTOLYSIN; ERYNGEOLYSIN; FUNGAL PROTEIN; HEMOLYSIN; MYCOTOXIN; OSTREOLYSIN; PLEUROTOLYSIN A; UNCLASSIFIED DRUG;

EID: 63449118079     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.85     Document Type: Review
Times cited : (72)

References (109)
  • 1
    • 0016566893 scopus 로고
    • Purification and characteristics of hemolytic toxin from Aspergillus fumigatus
    • Sakaguchi O, Shimada H Yokota K (1975) 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
  • 2
    • 0027936215 scopus 로고
    • Cloning and nucleotide sequence of cDNA encoding Asp-he-molysin from Aspergillus fumigatus
    • Ebina K, Sakagami H, Yokota K Kondo H (1994) Cloning and nucleotide sequence of cDNA encoding Asp-he-molysin 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
  • 4
    • 2642601131 scopus 로고    scopus 로고
    • Cloning and sequencing of the Aa-Pri1 gene specifically expressed during fruiting initiation in the edible mushroom Agro-cybe aegerita, and analysis of the predicted amino-acid sequence
    • Fernandez-Espinar MT, Labarère J (1997) Cloning and sequencing of the Aa-Pri1 gene specifically expressed during fruiting initiation in the edible mushroom Agro-cybe 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.T.1    Labarère, J.2
  • 5
    • 0032510775 scopus 로고    scopus 로고
    • Cloning and sequencing of three new putative toxin genes from Clostridium bifermentans CH18
    • 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
  • 7
    • 0037089465 scopus 로고    scopus 로고
    • Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting
    • 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
  • 8
    • 0037464589 scopus 로고    scopus 로고
    • Galagan JE, Calvo SE, Borkovich KA, Selker EU, Read ND, Jaffe D, FitzHugh W, Ma LJ, Smirnov S, Purcell S, Rehman B, Elkins T, Engels R, Wang S, Nielsen CB, Butler J, Endrizzi M, Qui D, Ianakiev P, Bell-Pedersen D, Nelson MA, Werner-Washburne M. Selitrennikoff CP, Kinsey JA, Braun EL, Zelter A, Schulte U, Kothe GO, Jedd G, Mewes W, Staben C, Marcotte E, Green-berg D, Roy A, Foley K, Naylor J, Stange-Thomann N, Barrett R, Gnerre S, Kamal M. Kamvysselis M, Mauceli E, Bielke C, Rudd S, Frishman D, Krystofova S, Ras-mussen C, Metzenberg RL, Perkins DD, Kroken S, Cogoni C, Macino G, Catcheside D, Li W, Pratt RJ, Osmani SA, DeSouza CP, Glass L, Orbach MJ, Berglund JA, Voelker R, Yarden O, Plamann M, Seiler S, Dunlap J, Radford A, Aramayo R, Natvig DO, Alex LA, Man-nhaupt G, Ebbole DJ, Freitag M, Paulsen I, Sachs MS, Lander ES, Nusbaum C, Birren B (2003) The genome sequence of the filamentous fungus. Neurospora crassa Nature 422:859-868
    • Galagan JE, Calvo SE, Borkovich KA, Selker EU, Read ND, Jaffe D, FitzHugh W, Ma LJ, Smirnov S, Purcell S, Rehman B, Elkins T, Engels R, Wang S, Nielsen CB, Butler J, Endrizzi M, Qui D, Ianakiev P, Bell-Pedersen D, Nelson MA, Werner-Washburne M. Selitrennikoff CP, Kinsey JA, Braun EL, Zelter A, Schulte U, Kothe GO, Jedd G, Mewes W, Staben C, Marcotte E, Green-berg D, Roy A, Foley K, Naylor J, Stange-Thomann N, Barrett R, Gnerre S, Kamal M. Kamvysselis M, Mauceli E, Bielke C, Rudd S, Frishman D, Krystofova S, Ras-mussen C, Metzenberg RL, Perkins DD, Kroken S, Cogoni C, Macino G, Catcheside D, Li W, Pratt RJ, Osmani SA, DeSouza CP, Glass L, Orbach MJ, Berglund JA, Voelker R, Yarden O, Plamann M, Seiler S, Dunlap J, Radford A, Aramayo R, Natvig DO, Alex LA, Man-nhaupt G, Ebbole DJ, Freitag M, Paulsen I, Sachs MS, Lander ES, Nusbaum C, Birren B (2003) The genome sequence of the filamentous fungus. Neurospora crassa Nature 422:859-868.
  • 9
    • 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
    • Tomita T, Noguchi K, Mimuro H, Ukaji F, Ito K, Suga-wara-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.
    • (2004) J Biol Chem , vol.279 , pp. 26975-26982
    • Tomita, T.1    Noguchi, K.2    Mimuro, H.3    Ukaji, F.4    Ito, K.5    Suga-wara-Tomita, N.6    Hashimoto, Y.7
  • 10
    • 33749855455 scopus 로고    scopus 로고
    • A hemolysin from the mushroom Pleurotus eryngii
    • Ngai PHK, Ng TB (2006) A hemolysin from the mushroom Pleurotus eryngii. Appl Microbiol Biotechnol 72:1185-1191.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1185-1191
    • Ngai, P.H.K.1    Ng, T.B.2
  • 12
    • 63449113520 scopus 로고
    • Note sur une toxine producte par l'Aspergillus fumigatus.
    • Bodin E, Gautier L (1906) Note sur une toxine producte par l'Aspergillus fumigatus. Ann Inst Pasteur 20:209-24.
    • (1906) Ann Inst Pasteur , vol.20 , pp. 209-224
    • Bodin, E.1    Gautier, L.2
  • 13
    • 0001572761 scopus 로고
    • An endotoxin from Aspergillus fumigatus
    • Henrici AT (1938) An endotoxin from Aspergillus fumigatus. J. Immunol 36:319-338.
    • (1938) J. Immunol , vol.36 , pp. 319-338
    • Henrici, A.T.1
  • 16
    • 3042863641 scopus 로고
    • Partial purification and characterization of the endotoxin from Aspergillus fumigatus
    • Rau EM, Tilden EB, Koenig VL (1961) Partial purification and characterization of the endotoxin from Aspergillus fumigatus. Mycopathologia 14:347-358.
    • (1961) Mycopathologia , vol.14 , pp. 347-358
    • Rau, E.M.1    Tilden, E.B.2    Koenig, V.L.3
  • 17
    • 0018781339 scopus 로고
    • Cytolytic protein from the edible mushroom, Pleurotus ostreatus. Bio-chim
    • Bernheimer AW, Avigad LS (1979) Cytolytic protein from the edible mushroom, Pleurotus ostreatus. Bio-chim Biophys Acta 585:451-461.
    • (1979) Biophys Acta , vol.585 , pp. 451-461
    • Bernheimer, A.W.1    Avigad, L.S.2
  • 18
    • 18244367696 scopus 로고    scopus 로고
    • Temporal and spatial expression of ostreolysin during development of the oyster mushroom (Pleurotus ostreatus)
    • 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.
    • (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
  • 19
    • 0036364159 scopus 로고    scopus 로고
    • Expression of a synthetic gene encoding the Asp-hemolysin from Aspergillus fumigatus in Escherichia coll
    • Kumagai T, Kudo Y, Fukuchi Y, Ebina K, Yokota K(2002) Expression of a synthetic gene encoding the Asp-hemolysin from Aspergillus fumigatus in Escherichia coll Biol Pharm Bull 25:115-117.
    • (2002) Biol Pharm Bull , vol.25 , pp. 115-117
    • Kumagai, T.1    Kudo, Y.2    Fukuchi, Y.3    Ebina, K.4    Yokota, K.5
  • 20
    • 0034865728 scopus 로고    scopus 로고
    • The Cry toxins and the putative hemolysins of Clostridium bifermentans ser. malaysia are not involved in mosqnitocidal activity
    • Juárez-Pérez V, Delécluse A (2001) The Cry toxins and the putative hemolysins of Clostridium bifermentans ser. malaysia are not involved in mosqnitocidal activity. J Invertebr Pathol 78:57-58.
    • (2001) J Invertebr Pathol , vol.78 , pp. 57-58
    • Juárez-Pérez, V.1    Delécluse, A.2
  • 21
    • 3042771822 scopus 로고    scopus 로고
    • Cloning, expression, and pore-forming properties of mature and precursor forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus
    • Sakurai N, Kaneko J, Kamio Y, Tomita T (2004) Cloning, expression, and pore-forming properties of mature and precursor forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus. Biochim Biophys Acta 1679:65-73.
    • (2004) Biochim Biophys Acta , vol.1679 , pp. 65-73
    • Sakurai, N.1    Kaneko, J.2    Kamio, Y.3    Tomita, T.4
  • 26
    • 34547571027 scopus 로고    scopus 로고
    • The M-Coffee webserver: A meta-method for computing multiple sequence alignments by combining alternative alignment methods
    • Web Server issue, W645-W648
    • Moretti S, Armougom F, Wallace IM, Higgins DG, Jongeneel CV, Notredame C (2007) The M-Coffee webserver: a meta-method for computing multiple sequence alignments by combining alternative alignment methods. Nucleic Acids Res 35 (Web Server issue): W645-W648.
    • (2007) Nucleic Acids Res , vol.35
    • Moretti, S.1    Armougom, F.2    Wallace, I.M.3    Higgins, D.G.4    Jongeneel, C.V.5    Notredame, C.6
  • 27
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: Analysis and visualization of genetic variation
    • Available at
    • Nicholas KB, Nicholas HB, Jr, Deerfield DW, II (1997) GeneDoc: analysis and visualization of genetic variation, EMBNEW.NEWS 4:14. Available at: http://www.psc.edu/biomed/genedoc..
    • (1997) EMBNEW.NEWS , vol.4 , pp. 14
    • Nicholas, K.B.1    Nicholas Jr, H.B.2    Deerfield II, D.W.3
  • 29
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Web Server issue:W197-W201
    • Cole C, Barber JD, Barton GJ (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36 (Web Server issue):W197-W201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 30
    • 25144432549 scopus 로고    scopus 로고
    • HYPROSP II-A knowledge-based hybrid method for protein secondary structure prediction based on local prediction confidence
    • Lin H-N, Chang J-M, Wu K-P, Sung T-Y, Hsu W-L (2005) HYPROSP II-A knowledge-based hybrid method for protein secondary structure prediction based on local prediction confidence. Bioinformatics 21:3227-3233.
    • (2005) Bioinformatics , vol.21 , pp. 3227-3233
    • Lin, H.-N.1    Chang, J.-M.2    Wu, K.-P.3    Sung, T.-Y.4    Hsu, W.-L.5
  • 31
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • Web Server issue, W321-W326
    • Rost B, Yachdav G, Liu J (2004) The PredictProtein server. Nucleic Acids Res 32 (Web Server issue): W321-W326.
    • (2004) Nucleic Acids Res , vol.32
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 32
    • 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
    • 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,
    • (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
  • 33
    • 3042596916 scopus 로고    scopus 로고
    • Interaction of ostreolysin, a cytolytic protein from the edible mushroom Pleurotus ostreatus, with lipid membranes and modulation by lysophospho-lipids
    • Sepčić K, Berne S, Potrich C, Turk T, Maček P, Menesstrina G (2003) Interaction of ostreolysin, a cytolytic protein from the edible mushroom Pleurotus ostreatus, with lipid membranes and modulation by lysophospho-lipids. Eur J Biochem 270:1199-1210.
    • (2003) Eur J Biochem , vol.270 , pp. 1199-1210
    • Sepčić, K.1    Berne, S.2    Potrich, C.3    Turk, T.4    Maček, P.5    Menesstrina, G.6
  • 34
    • 0029915003 scopus 로고    scopus 로고
    • ukuchi Y. Kumagai T, Ebina K, Yokota K (1996b) Apo-lipoprotein B inhibits the hemolytic activity of asp-hemolysin from Aspergillus fumigatus. Biol Pharm BulBull 19:547-550.
    • ukuchi Y. Kumagai T, Ebina K, Yokota K (1996b) Apo-lipoprotein B inhibits the hemolytic activity of asp-hemolysin from Aspergillus fumigatus. Biol Pharm BulBull 19:547-550.
  • 35
    • 0034201441 scopus 로고    scopus 로고
    • Longden I Bleasby A. EMBOSS: The eu-ropean molecular biology open software suite
    • Rice P (2000) Longden I Bleasby A. EMBOSS: The eu-ropean molecular biology open software suite. Trends Genet 16:276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1
  • 36
    • 0029955803 scopus 로고    scopus 로고
    • Binding assay of low density lipoprotein to Asp-hemolysin from Aspergillus fumigatus
    • Fukuchi Y, Kudo Y, Kumagai T, Ebina K, Yokota K (1996a) Binding assay of low density lipoprotein to Asp-hemolysin from Aspergillus fumigatus. Biol Pharm Bull 19:1380-1381.
    • (1996) Biol Pharm Bull , vol.19 , pp. 1380-1381
    • Fukuchi, Y.1    Kudo, Y.2    Kumagai, T.3    Ebina, K.4    Yokota, K.5
  • 37
    • 0031755837 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein inhibits the hemolytic activity of Asp-hemolysin from Aspergillus fumigatus
    • Fukuchi Y, Kudo Y, Kumagai T, Ebina K, Yokota K (1998) Oxidized low density lipoprotein inhibits the hemolytic activity of Asp-hemolysin from Aspergillus fumigatus. FEMS Microbiol Lett 167:275-280.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 275-280
    • Fukuchi, Y.1    Kudo, Y.2    Kumagai, T.3    Ebina, K.4    Yokota, K.5
  • 38
    • 0036594103 scopus 로고    scopus 로고
    • A novel oxidized low-density lipoprotein binding protein, Asp-hemolysin, recognizes lysophosphatidyl-choline
    • Kudo Y, Ootani T, Kumagai T, Fukuchi Y, Ebina K (2002) A novel oxidized low-density lipoprotein binding protein, Asp-hemolysin, recognizes lysophosphatidyl-choline. Biol Pharm Bull 25:787-790.
    • (2002) Biol Pharm Bull , vol.25 , pp. 787-790
    • Kudo, Y.1    Ootani, T.2    Kumagai, T.3    Fukuchi, Y.4    Ebina, K.5
  • 39
    • 0018452713 scopus 로고
    • Investigation of the hemolytic site of Asp-hemolysin
    • Kamaguchi A, Yokota K, Sakaguchi O (1979) Investigation of the hemolytic site of Asp-hemolysin. Jpn J Med Sci Biol 32:118-121.
    • (1979) Jpn J Med Sci Biol , vol.32 , pp. 118-121
    • Kamaguchi, A.1    Yokota, K.2    Sakaguchi, O.3
  • 41
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R, Heuck AP, Tweten RK, Johnson AE (2002) Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat Struct Biol 9:823-827.
    • (2002) Nat Struct Biol , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 42
    • 4444317733 scopus 로고    scopus 로고
    • Cholesterol and the activity of bacterial toxins
    • Palmer M (2004) Cholesterol and the activity of bacterial toxins. FEMS Microbiol Lett 238:281-289.
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 281-289
    • Palmer, M.1
  • 43
    • 0036846746 scopus 로고    scopus 로고
    • The origin and evolution of model organisms
    • Hedges SB (2002) The origin and evolution of model organisms. Nature Rev Gen 3:838-849.
    • (2002) Nature Rev Gen , vol.3 , pp. 838-849
    • Hedges, S.B.1
  • 44
    • 33847737366 scopus 로고    scopus 로고
    • Comparative genomics and the evolution of prokaryotes
    • Abby S, Daubin V (2007) Comparative genomics and the evolution of prokaryotes. Trends Microbiol 15:135-141.
    • (2007) Trends Microbiol , vol.15 , pp. 135-141
    • Abby, S.1    Daubin, V.2
  • 47
    • 0037469341 scopus 로고    scopus 로고
    • Growth promotion of the edible fungus Pleurotus ostreatus by fluorescent pseudomonads
    • 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
  • 48
    • 33845904639 scopus 로고    scopus 로고
    • Horizontal gene transfer in plants
    • Richardson AO, Palmer JD (2007) Horizontal gene transfer in plants. J Exp Bot 58:1-9.
    • (2007) J Exp Bot , vol.58 , pp. 1-9
    • Richardson, A.O.1    Palmer, J.D.2
  • 49
    • 33748455342 scopus 로고    scopus 로고
    • Evolution of filamentous plant pathogens: Gene exchange across eukaryotic kingdoms
    • Richards TA, Dacks JB, Jenkinson JM, Thornton CR, Talbot NJ (2006) Evolution of filamentous plant pathogens: gene exchange across eukaryotic kingdoms. Curr Biol 16:1857-1864.
    • (2006) Curr Biol , vol.16 , pp. 1857-1864
    • Richards, T.A.1    Dacks, J.B.2    Jenkinson, J.M.3    Thornton, C.R.4    Talbot, N.J.5
  • 51
    • 0037654703 scopus 로고    scopus 로고
    • Expressed sequences from the basidiomycetous tree pathogen Het-erobasidion annosum during early infection of Scots pine
    • Karlsson M. Olson A, Stenlid J (2003) Expressed sequences from the basidiomycetous tree pathogen Het-erobasidion annosum during early infection of Scots pine. Fungal Genet Biol 39:51-59.
    • (2003) Fungal Genet Biol , vol.39 , pp. 51-59
    • Karlsson, M.1    Olson, A.2    Stenlid, J.3
  • 52
    • 4544239246 scopus 로고    scopus 로고
    • Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains
    • Sepčić K, Berne S, Rebolj K, Batista U, Plemenitaš A, Šentjure 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.
    • (2004) FEBS Lett , vol.575 , pp. 81-85
    • Sepčić, K.1    Berne, S.2    Rebolj, K.3    Batista, U.4    Plemenitaš, A.5    Šentjure, M.6    Maček, P.7
  • 53
    • 28644434509 scopus 로고    scopus 로고
    • Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, Berriman M, Abe K, Archer DB, Bermejo C, Bennett J, Bowyer P. Chen D, Collins M, Coulsen R. Davies R. Dyer PS, Farman M. Fedorova N, Fedorova N, Feldblyum TV, Fischer R, Fosker N, Fraser A, Garcia JL, Garcia MJ, Goble A, Goldman GH, Gomi K, Griffith-Jones S, Gwilliam R, Haas B, Haas H, Harris D, Horiuchi H, Huang J, Humphrey S, Jimenez J, Keller N, Khouri H. Kitamoto K. Kobayashi T, Konzack S, Kulkarni R, Kumagai T, Lafton A, Latgé JP, Li W, Lord A, Lu C, Majoros WH, May GS, Miller BL, Mohamoud Y, Molina M, Monod M, Mouyna I, Mulligan S, Murphy L, O'Neil S, Paulsen I, Penalva MA, Pertea M, Price C, Pritchard BL, Quail MA, Rab- binowitsch E, Rawlins N, Rajandream MA, Reichard U, Renauld H, Robson GD, Rodriguez de Cordoba S, Rodriguez-Pena JM, Ronning CM, Rutter S, Salzberg SL, Sanchez M. Sanchez-Ferrero JC, Saunders D, Seeger K, Squares R, Squares S, Takeuchi M, Tekaia F, Turner G, Vazquez de Aldana CR, Weidman J, Whi
    • Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, Berriman M, Abe K, Archer DB, Bermejo C, Bennett J, Bowyer P. Chen D, Collins M, Coulsen R. Davies R. Dyer PS, Farman M. Fedorova N, Fedorova N, Feldblyum TV, Fischer R, Fosker N, Fraser A, Garcia JL, Garcia MJ, Goble A, Goldman GH, Gomi K, Griffith-Jones S, Gwilliam R, Haas B, Haas H, Harris D, Horiuchi H, Huang J, Humphrey S, Jimenez J, Keller N, Khouri H. Kitamoto K. Kobayashi T, Konzack S, Kulkarni R, Kumagai T, Lafton A, Latgé JP, Li W, Lord A, Lu C, Majoros WH, May GS, Miller BL, Mohamoud Y, Molina M, Monod M, Mouyna I, Mulligan S, Murphy L, O'Neil S, Paulsen I, Penalva MA, Pertea M, Price C, Pritchard BL, Quail MA, Rab- binowitsch E, Rawlins N, Rajandream MA, Reichard U, Renauld H, Robson GD, Rodriguez de Cordoba S, Rodriguez-Pena JM, Ronning CM, Rutter S, Salzberg SL, Sanchez M. Sanchez-Ferrero JC, Saunders D, Seeger K, Squares R, Squares S, Takeuchi M, Tekaia F, Turner G, Vazquez de Aldana CR, Weidman J, White O, Woodward J, Yu JH, Fraser C, Galagan JE, Asai K, Machida M, Hall N, Barrell B, Denning DW (2005) Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus. Nature 438:1151-1156.
  • 54
    • 33846861493 scopus 로고    scopus 로고
    • Pel HJ, de Winde JH, Archer DB, Dyer PS, Hofmann G, Schaap PJ, Turner G, de Vries RP, Albang R. Alber- mann K. Andersen MR, Bendtsen JD, Benen JA, van den Berg M. Breestraat S, Caddick MX, Contreras R, Cornell M, Coutinho PM, Danchin EG, Debets AJ, Dek-ker P, van Dijck PW, van Dijk A, Dijkhuizen L, Driessen AJ, d'Enfert C, Geysens S, Goosen Groot GS, de Groot PW, Guillemette T, Henrissat B, Herweijer M, van den Hombergh JP, van den Hondel CA, van der Heijden RT, van der Kaaij KM. Klis FM, Kools HJ, Kubicek CP, van Kuyk PA, Lauber J, Lu X. van der Maarel MJ, Meulen-berg R, Menke H, Mortimer MA, Nielsen J, Oliver SG, Olsthoorn M, Pal K, van Peij NN, Ram AF, Rinas U, Roubos JA, Sagt CM, Schmoll M, Sun J, Ussery D, Varga J, Vervecken W, van de Vondervoort PJ, Wedler H, Wosten HA. Zeng AP. van Ooyen AJ, Visser J Stam H (2007) Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nat Bio-technol 25:221-231
    • Pel HJ, de Winde JH, Archer DB, Dyer PS, Hofmann G, Schaap PJ, Turner G, de Vries RP, Albang R. Alber- mann K. Andersen MR, Bendtsen JD, Benen JA, van den Berg M. Breestraat S, Caddick MX, Contreras R, Cornell M, Coutinho PM, Danchin EG, Debets AJ, Dek-ker P, van Dijck PW, van Dijk A, Dijkhuizen L, Driessen AJ, d'Enfert C, Geysens S, Goosen Groot GS, de Groot PW, Guillemette T, Henrissat B, Herweijer M, van den Hombergh JP, van den Hondel CA, van der Heijden RT, van der Kaaij KM. Klis FM, Kools HJ, Kubicek CP, van Kuyk PA, Lauber J, Lu X. van der Maarel MJ, Meulen-berg R, Menke H, Mortimer MA, Nielsen J, Oliver SG, Olsthoorn M, Pal K, van Peij NN, Ram AF, Rinas U, Roubos JA, Sagt CM, Schmoll M, Sun J, Ussery D, Varga J, Vervecken W, van de Vondervoort PJ, Wedler H, Wosten HA. Zeng AP. van Ooyen AJ, Visser J Stam H (2007) Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nat Bio-technol 25:221-231.
  • 55
    • 29244442741 scopus 로고    scopus 로고
    • Machida M, Asai K, Sano M. Tanaka T, Kumagai T, Terai G, Kusumoto K, Arima T, Akita O, Kashiwagi Y, Abe K. Gomi K. Horiuchi H, Kitamoto K, Kobayashi T, Takeuchi M, Denning DW, Galagan JE, Nierman WC, Yu J, Archer DB, Bennett JW, Bhatnagar D, Cleveland TE, Fedorova ND, Gotoh O, Horikawa H, Hosoyama A, Ichinomiya M, Igarashi R, Iwashita K, Juvvadi PR, Kato M, Kato Y, Kin T, Kokubun A, Maeda H, Maeyama N, Maruyama J, Nagasaki H, Nakajima T, Oda K. Okada K, Paulsen I, Sakamoto K, Sawano T, Takahashi M. Takase K, Terabayashi Y, Wortman JR, Yamada O, Yamagata Y, Anazawa H, Hata Y, Koide Y, Komori T, Koyama Y, Minetoki T, Suharnan S, Tanaka A, Isono K, Kuhara S, Ogasawara N, Kikuchi H (2005) Genome sequencing and analysis of Aspergillus oryzae. Nature 438: 1157-1161.
    • Machida M, Asai K, Sano M. Tanaka T, Kumagai T, Terai G, Kusumoto K, Arima T, Akita O, Kashiwagi Y, Abe K. Gomi K. Horiuchi H, Kitamoto K, Kobayashi T, Takeuchi M, Denning DW, Galagan JE, Nierman WC, Yu J, Archer DB, Bennett JW, Bhatnagar D, Cleveland TE, Fedorova ND, Gotoh O, Horikawa H, Hosoyama A, Ichinomiya M, Igarashi R, Iwashita K, Juvvadi PR, Kato M, Kato Y, Kin T, Kokubun A, Maeda H, Maeyama N, Maruyama J, Nagasaki H, Nakajima T, Oda K. Okada K, Paulsen I, Sakamoto K, Sawano T, Takahashi M. Takase K, Terabayashi Y, Wortman JR, Yamada O, Yamagata Y, Anazawa H, Hata Y, Koide Y, Komori T, Koyama Y, Minetoki T, Suharnan S, Tanaka A, Isono K, Kuhara S, Ogasawara N, Kikuchi H (2005) Genome sequencing and analysis of Aspergillus oryzae. Nature 438: 1157-1161.
  • 56
    • 33746659356 scopus 로고    scopus 로고
    • Generation and analysis of expressed sequence tags from Botrytis cinerea
    • Silva EM, Valdes J, Holmes D, Shmaryahu A, Valen-zuela PD (2006) Generation and analysis of expressed sequence tags from Botrytis cinerea. Biol Res 39: 367-379
    • (2006) Biol Res , vol.39 , pp. 367-379
    • Silva, E.M.1    Valdes, J.2    Holmes, D.3    Shmaryahu, A.4    Valen-zuela, P.D.5
  • 57
    • 21644441527 scopus 로고    scopus 로고
    • Felipe MS, Andrade RV, Arraes FB, Nicola AM, Maran-hao AQ, Torres FA, Silva-Pereira I, Pocas-Fonseca MJ, Campos EG, Moraes LM, Andrade PA, Tavares AH, Silva SS, Kyaw CM, Souza DP, Network P, Pereira M, Jesuino RS, Andrade EV, Parente JA, Oliveira GS, Bar-bosa MS, Martins NF, Fachin AL, Cardoso RS, Passes GA, Almeida NF, Walter ME, Soares CM, Carvalho MJ Brigido MM (2005) Transcriptional Profiles of the Human Pathogenic Fungus Paracoccidioides brasilien- sis in Mycelium and Yeast Cells. J Biol Chem 280:24706-24714.
    • Felipe MS, Andrade RV, Arraes FB, Nicola AM, Maran-hao AQ, Torres FA, Silva-Pereira I, Pocas-Fonseca MJ, Campos EG, Moraes LM, Andrade PA, Tavares AH, Silva SS, Kyaw CM, Souza DP, Network P, Pereira M, Jesuino RS, Andrade EV, Parente JA, Oliveira GS, Bar-bosa MS, Martins NF, Fachin AL, Cardoso RS, Passes GA, Almeida NF, Walter ME, Soares CM, Carvalho MJ Brigido MM (2005) Transcriptional Profiles of the Human Pathogenic Fungus Paracoccidioides brasilien- sis in Mycelium and Yeast Cells. J Biol Chem 280:24706-24714.
  • 61
    • 33748973402 scopus 로고    scopus 로고
    • Sequence and organization of the Trichoplusia ni aseovirus 2c (Ascoviridae) genome
    • Wang L, Xue J, Seaborn CP, Arif BM, Cheng XW (2006) Sequence and organization of the Trichoplusia ni aseovirus 2c (Ascoviridae) genome. Virology 354:167-177.
    • (2006) Virology , vol.354 , pp. 167-177
    • Wang, L.1    Xue, J.2    Seaborn, C.P.3    Arif, B.M.4    Cheng, X.W.5
  • 62
    • 0021956024 scopus 로고
    • Studies on toxin of Aspergillus fumigatus. XXII Fashion of binding of Asp-hemolysin to human erythrocytes and Asp-he-molysin-binding proteins of erythrocyte membranes
    • Ebina K, Ichinowatari S, Yokota K (1985) Studies on toxin of Aspergillus fumigatus. XXII Fashion of binding of Asp-hemolysin to human erythrocytes and Asp-he-molysin-binding proteins of erythrocyte membranes Microbiol Immunol 29:91-101.
    • (1985) Microbiol Immunol , vol.29 , pp. 91-101
    • Ebina, K.1    Ichinowatari, S.2    Yokota, K.3
  • 63
    • 0021257870 scopus 로고    scopus 로고
    • Yokota K, Kamaguchi A, Sakaguchi O (1984a)Studies on the toxin of Aspergillus fumigatus XVII. Photooxida-tion of asp-hemolysin in the presence of various dyes and its relation to the site of hemolytic activity .Micro biol Immunol 28:385-391.
    • Yokota K, Kamaguchi A, Sakaguchi O (1984a)Studies on the toxin of Aspergillus fumigatus XVII. Photooxida-tion of asp-hemolysin in the presence of various dyes and its relation to the site of hemolytic activity .Micro biol Immunol 28:385-391.
  • 64
    • 0021703928 scopus 로고
    • Studies on the toxin of Aspergillus fumigatus XX. Chemical modification of Asp-hemolysin
    • Yokota K, Ichinowatari S, Ebina K (1984b) Studies on the toxin of Aspergillus fumigatus XX. Chemical modification of Asp-hemolysin. Jpn J Med Mycol 25:332-339.
    • (1984) Jpn J Med Mycol , vol.25 , pp. 332-339
    • Yokota, K.1    Ichinowatari, S.2    Ebina, K.3
  • 65
    • 0022259012 scopus 로고
    • Studies on the toxin of Aspergillus fumigatus XXI. Site of binding of Asp-hemolysin to erythrocytes and mechanism of inhibition of hemolysis
    • Yokota K, Ichinowatari S, Ebina K, Wakabayashi N (1985) Studies on the toxin of Aspergillus fumigatus XXI. Site of binding of Asp-hemolysin to erythrocytes and mechanism of inhibition of hemolysis. Jpn J Med Mycol 26:332-339.
    • (1985) Jpn J Med Mycol , vol.26 , pp. 332-339
    • Yokota, K.1    Ichinowatari, S.2    Ebina, K.3    Wakabayashi, N.4
  • 66
    • 0017571588 scopus 로고
    • Studies on the toxin of Aspergillus fumigatus VIII. Biological properties of Asp-hemolysin
    • Sakaguchi O, Yokota K, Kamaguchi A (1977) Studies on the toxin of Aspergillus fumigatus VIII. Biological properties of Asp-hemolysin. Nippon Saikingaku Zasshi 32:821-828.
    • (1977) Nippon Saikingaku Zasshi , vol.32 , pp. 821-828
    • Sakaguchi, O.1    Yokota, K.2    Kamaguchi, A.3
  • 67
    • 53649102075 scopus 로고    scopus 로고
    • Ostreolysin, a cytolytic protein from culinary-medicinal oyster mushroom Pleurotus ostreatus (Jack.: Fr.) P. Kumm. (Agaricomycetidae), and its potential use in medicine and biotechnology
    • Rebolj K, Sepčić K (2008) Ostreolysin, a cytolytic protein from culinary-medicinal oyster mushroom Pleurotus ostreatus (Jack.: Fr.) P. Kumm. (Agaricomycetidae), and its potential use in medicine and biotechnology. Int J Med Mushr 10:293-302.
    • (2008) Int J Med Mushr , vol.10 , pp. 293-302
    • Rebolj, K.1    Sepčić, K.2
  • 68
    • 33746954571 scopus 로고    scopus 로고
    • Toxic and lethal effects of ostreolysin, a cytolytic protein from edible oyster mushroom (Pleurotus ostreatus), in rodents
    • Žužek MC, Maček P, Sepčić K, Cestnik V, Frangež R (2006) Toxic and lethal effects of ostreolysin, a cytolytic protein from edible oyster mushroom (Pleurotus ostreatus), in rodents. Toxicon 48:264-271.
    • (2006) Toxicon , vol.48 , pp. 264-271
    • Žužek, M.C.1    Maček, P.2    Sepčić, K.3    Cestnik, V.4    Frangež, R.5
  • 69
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E.Functional rafts in cell membranes. Nature 387:569-572.
    • Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 70
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin M (2003) The state of lipid rafts: from model membranes to cells. Annu Rev Biophys Biomol Struct 32:257-283.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 71
    • 0036667737 scopus 로고    scopus 로고
    • Insights into lipid raft structure and formation from experiments in model membranes
    • London E (2002) Insights into lipid raft structure and formation from experiments in model membranes. Curr Opin Struct Biol 12:480-486.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 480-486
    • London, E.1
  • 72
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D, Goni FM, Heerklotz H (2005) Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem Sci 30:430-436.
    • (2005) Trends Biochem Sci , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 73
    • 0141642121 scopus 로고    scopus 로고
    • Sphingo-myelin/ phosphatidylcholine/cholesterol phase diagram:boundaries and composition of lipid rafts
    • de Almeida REM, Fedorov A, Prieto M (2003) Sphingo-myelin/ phosphatidylcholine/cholesterol phase diagram:boundaries and composition of lipid rafts. Biophys J 85:2406-2416.
    • (2003) Biophys J , vol.85 , pp. 2406-2416
    • de Almeida, R.E.M.1    Fedorov, A.2    Prieto, M.3
  • 74
    • 33749060200 scopus 로고    scopus 로고
    • Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers
    • Rebolj K, Poklar Ulrih N, 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.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1662-1670
    • Rebolj, K.1    Poklar Ulrih, N.2    Maček, P.3    Sepčić, K.4
  • 75
    • 44949199084 scopus 로고    scopus 로고
    • Lysophospholipids prevent binding of a cytolytic protein ostreolysin to cholesterol-enriched membrane domains
    • 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.
    • (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
  • 76
    • 18144417503 scopus 로고    scopus 로고
    • Crosslinking a lipid raft component triggers liquid ordered-liquid disordered phase separation in model plasma membranes
    • Hammond AT, Heberle FA, Baumgart T, Holowka D, Baird B, Feigenson GW (2005) Crosslinking a lipid raft component triggers liquid ordered-liquid disordered phase separation in model plasma membranes. Proc Natl Acad Sci USA 102:6320-3625.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6320-3625
    • Hammond, A.T.1    Heberle, F.A.2    Baumgart, T.3    Holowka, D.4    Baird, B.5    Feigenson, G.W.6
  • 77
    • 0030037295 scopus 로고    scopus 로고
    • Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess
    • Nagamune H, Ohnishi C, Katsuura A, Fushitani K, Whiley RA, Tsuji A, Matsuda Y (1996) Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess. Infect Immun 64:3093-3100.
    • (1996) Infect Immun , vol.64 , pp. 3093-3100
    • Nagamune, H.1    Ohnishi, C.2    Katsuura, A.3    Fushitani, K.4    Whiley, R.A.5    Tsuji, A.6    Matsuda, Y.7
  • 78
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol- dependent cytolysins
    • Giddings KS, Johnson AE, Tweten R (2003) Redefining cholesterol's role in the mechanism of the cholesterol- dependent cytolysins, Proc Natl Acad Sci USA 100:11315-11320.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.3
  • 79
    • 14144251524 scopus 로고    scopus 로고
    • Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin
    • Polekhina G, Giddings KS, Tweten RK, Parker MW (2005) Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. Proc Natl Acad Sci USA 102:600-605.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 600-605
    • Polekhina, G.1    Giddings, K.S.2    Tweten, R.K.3    Parker, M.W.4
  • 80
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten R (2005) Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect Immun 73:6199-6209.
    • (2005) Infect Immun , vol.73 , pp. 6199-6209
    • Tweten, R.1
  • 81
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • Olson R, Gouaux E (2005) Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J Mol Biol 350:997-1016.
    • (2005) J Mol Biol , vol.350 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 82
    • 0033556418 scopus 로고    scopus 로고
    • Oligome-rization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane
    • Zitzer A, Zitzer O, Bhakdi S, Palmer M (1999) Oligome-rization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J Biol Chem 274:1375-1380.
    • (1999) J Biol Chem , vol.274 , pp. 1375-1380
    • Zitzer, A.1    Zitzer, O.2    Bhakdi, S.3    Palmer, M.4
  • 83
    • 0035915501 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein-binding specificity of Asp-hemolysin from Aspergillus fumigatus
    • 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.
    • (2001) Biochim Biophys Acta , vol.1568 , pp. 183-188
    • Kudo, Y.1    Fukuchi, Y.2    Kumagai, T.3    Ebina, K.4    Yokota, K.5
  • 84
    • 0033257454 scopus 로고    scopus 로고
    • Cytotoxic activity and cytokine gene induction of Asp-hemolysin to murine macrophages
    • Kumagai T, Nagata Y, 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, Y.2    Kudo, Y.3    Fukuchi, Y.4    Ebina, K.5    Yokota, K.6
  • 85
    • 0034989471 scopus 로고    scopus 로고
    • Interactions between Asp-hemolysin from Aspergillus fumigatus and blood plasma components
    • Fukuchi Y (2001) Interactions between Asp-hemolysin from Aspergillus fumigatus and blood plasma components. Yakugaku Zasshi 121:423-432.
    • (2001) Yakugaku Zasshi , vol.121 , pp. 423-432
    • Fukuchi, Y.1
  • 86
    • 0033050623 scopus 로고    scopus 로고
    • Binding of Asp-hemolysin from Aspergillus fumigatus to oxidized low density lipoprotein
    • Kudo Y, Kumagai T, Fukuchi Y, Ebina K, Yokota K (1999) Binding of Asp-hemolysin from Aspergillus fumigatus to oxidized low density lipoprotein. Biol Pharm Bull 22:549-550.
    • (1999) Biol Pharm Bull , vol.22 , pp. 549-550
    • Kudo, Y.1    Kumagai, T.2    Fukuchi, Y.3    Ebina, K.4    Yokota, K.5
  • 87
    • 25644460996 scopus 로고    scopus 로고
    • A synthetic peptide (P-21) derived from Asp-he molysin inhibits the induction of macrophage proliferation by oxidized low-density lipoprotein
    • Kumagai T, Ogawa N, Tsutsumi H, Ebina K Yokota K (2005) A synthetic peptide (P-21) derived from Asp-he molysin inhibits the induction of macrophage proliferation by oxidized low-density lipoprotein. Biol Pharm Bull 28:1381-1384.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1381-1384
    • Kumagai, T.1    Ogawa, N.2    Tsutsumi, H.3    Ebina, K.4    Yokota, K.5
  • 88
    • 33750608662 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein-binding specificity of the Asp-hemolysin-related synthetic peptides from Aspergillus fumigatus
    • Kumagai T, Tsutsumi H, Ogawa N, Naito S, Ebina, K. Yokota K Nagata K (2006) Oxidized low-density lipoprotein-binding specificity of the Asp-hemolysin-related synthetic peptides from Aspergillus fumigatus. Biol Pharm Bull 29:2181-2186.
    • (2006) Biol Pharm Bull , vol.29 , pp. 2181-2186
    • Kumagai, T.1    Tsutsumi, H.2    Ogawa, N.3    Naito, S.4    Ebina, K.5    Yokota, K.6    Nagata, K.7
  • 89
    • 0028079980 scopus 로고
    • Lysophos-phatidylcholine plays an essential role in the mitogenic effect of oxidized low density lipoprotein on murine macrophages
    • Sakai M, Miyazaki A, Hakamata H, Sasaki T, Yui S, Yamazaki M, Shichiri M, Horiuchi S (1994) Lysophos-phatidylcholine 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
  • 90
    • 0021071505 scopus 로고
    • Studies on toxin of Aspergilus fumigatus XVI, Biological properties of Asp-hemolysin as a parasite factor
    • Ebina K, Yokota K, Sakaguchi O (1983) Studies on toxin of Aspergilus fumigatus XVI, Biological properties of Asp-hemolysin as a parasite factor. Jpn J Med Mycol 24:245-252.
    • (1983) Jpn J Med Mycol , vol.24 , pp. 245-252
    • Ebina, K.1    Yokota, K.2    Sakaguchi, O.3
  • 91
    • 0035071156 scopus 로고    scopus 로고
    • Cytotoxic activity and cytokine induction of Asp-hemolysin to vascular endothelial cells
    • Kumagai T, Nagata T, Kudo Y. Fukuchi Y, Ebina K Yokota K (2001) Cytotoxic activity and cytokine induction of Asp-hemolysin to vascular endothelial cells. Yakugaku Zasshi 121:271-275.
    • (2001) Yakugaku Zasshi , vol.121 , pp. 271-275
    • Kumagai, T.1    Nagata, T.2    Kudo, Y.3    Fukuchi, Y.4    Ebina, K.5    Yokota, K.6
  • 92
    • 33847745303 scopus 로고    scopus 로고
    • Effect of ostreolysin, an Asp-hemolysin isoform, on human chondrocytes and osteoblasts, and possible role of Asp-hemolysin in pathogenesis
    • Maličev E, Chowdhury H, Maček P, Sepčić K (2007) Effect of ostreolysin, an Asp-hemolysin isoform, on human chondrocytes and osteoblasts, and possible role of Asp-hemolysin in pathogenesis. Med Mycol 45: 123-30.
    • (2007) Med Mycol , vol.45 , pp. 123-130
    • Maličev, E.1    Chowdhury, H.2    Maček, P.3    Sepčić, K.4
  • 93
    • 34249005344 scopus 로고    scopus 로고
    • Ostreolysin affects rat aorta ring tension and endothelial cells viability in vitro
    • Rebolj K, Batista U, Sepčić K. Cestnik V, Maček P, Fran-gež R (2007) Ostreolysin affects rat aorta ring tension and endothelial cells viability in vitro. Toxicon 49:1211-1213.
    • (2007) Toxicon , vol.49 , pp. 1211-1213
    • Rebolj, K.1    Batista, U.2    Sepčić, K.3    Cestnik, V.4    Maček, P.5    Fran-gež, R.6
  • 94
    • 0001572761 scopus 로고
    • An endotoxin from Aspergillus fumigatus
    • Henrici AT (1938) An endotoxin from Aspergillus fumigatus. J Immunol 36:319-338.
    • (1938) J Immunol , vol.36 , pp. 319-338
    • Henrici, A.T.1
  • 96
    • 0015392978 scopus 로고
    • Studies on the toxin of Aspergillus fumigatus III. Fraction causing dermonec-rosis and hemorrhage-like changes
    • Sakaguchi O, Yokota K (1972) Studies on the toxin of Aspergillus fumigatus III. Fraction causing dermonec-rosis and hemorrhage-like changes. Nippon Saikingaku Zasshi 27:649-655.
    • (1972) Nippon Saikingaku Zasshi , vol.27 , pp. 649-655
    • Sakaguchi, O.1    Yokota, K.2
  • 98
    • 0017175042 scopus 로고
    • Depletion of complemeni in vivo and in vitro by extracts of Aspergillus fumigatus
    • Budzko DB, Negroni R (1976) Depletion of complemeni in vivo and in vitro by extracts of Aspergillus fumigatus. Int Arch Allergy Appl Immun 51:518-524.
    • (1976) Int Arch Allergy Appl Immun , vol.51 , pp. 518-524
    • Budzko, D.B.1    Negroni, R.2
  • 99
    • 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
  • 100
    • 0021736229 scopus 로고
    • Studies on toxin of Aspergilus fumigatus XIX. Biochemical alteration of sera after Asp-hemolysin inoculation or Aspergillus infection in mice
    • Ebina K, Ichinowatari S, Yokota K, Sakaguchi O (1984) Studies on toxin of Aspergilus fumigatus XIX. Biochemical alteration of sera after Asp-hemolysin inoculation or Aspergillus infection in mice. Jpn J Med Mycol 25:236-243.
    • (1984) Jpn J Med Mycol , vol.25 , pp. 236-243
    • Ebina, K.1    Ichinowatari, S.2    Yokota, K.3    Sakaguchi, O.4
  • 101
    • 0023514882 scopus 로고
    • Toxicologic and histopathologic studies of Pleurotus ostreatus mushroom in mice
    • Al-Deen IHS, Twaij HAA, Al-Badr AA, Istarabad TAW (1987) Toxicologic and histopathologic studies of Pleurotus ostreatus mushroom in mice. J Ethnopharm 21:297-305.
    • (1987) J Ethnopharm , vol.21 , pp. 297-305
    • Al-Deen, I.H.S.1    Twaij, H.A.A.2    Al-Badr, A.A.3    Istarabad, T.A.W.4
  • 102
    • 19844375221 scopus 로고    scopus 로고
    • Schachter EN, Zuskin E, Goswami S, Castranova V, Aru- mugam U, Whitmer M, Siegel P, Chiarelli A Fainberg J (2005) Pharmacological study of oyster mushroom (Pleurotus ostreatus) extract on isolated guinea pig trachea smooth muscle. Lung 183:63-71.
    • Schachter EN, Zuskin E, Goswami S, Castranova V, Aru- mugam U, Whitmer M, Siegel P, Chiarelli A Fainberg J (2005) Pharmacological study of oyster mushroom (Pleurotus ostreatus) extract on isolated guinea pig trachea smooth muscle. Lung 183:63-71.
  • 104
    • 0032916340 scopus 로고    scopus 로고
    • Aspergillus fumigatus and aspergillosis
    • Latgé JP (1999) Aspergillus fumigatus and aspergillosis. Clin Microbiol Rev 12:310-350.
    • (1999) Clin Microbiol Rev , vol.12 , pp. 310-350
    • Latgé, J.P.1
  • 105
    • 35648963643 scopus 로고    scopus 로고
    • Monitoring the distribution and dynamics of signaling mierodomains in living cells with lipid-specific probes
    • Hullin-Matsuda F, Kobayasbi T (2007) Monitoring the distribution and dynamics of signaling mierodomains in living cells with lipid-specific probes. Cell Mol Life Sci 64:2492-2504.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2492-2504
    • Hullin-Matsuda, F.1    Kobayasbi, T.2
  • 106
    • 33845614097 scopus 로고    scopus 로고
    • Rafting with cholera toxin: Endocytosis and trafficking from plasma membrane to ER
    • Chinnapen DJ, Chinnapen H, Saslowsky D Lencer Wl (2007) Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER. FEMS Microbiol Lett 266:129-137.
    • (2007) FEMS Microbiol Lett , vol.266 , pp. 129-137
    • Chinnapen, D.J.1    Chinnapen, H.2    Saslowsky, D.3    Lencer, W.4
  • 107
    • 41949085510 scopus 로고    scopus 로고
    • How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH
    • Nelson LD, Johnson AE, London E (2008) How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH. J Biol Chem 283:4632-4642.
    • (2008) J Biol Chem , vol.283 , pp. 4632-4642
    • Nelson, L.D.1    Johnson, A.E.2    London, E.3
  • 108
    • 28844461287 scopus 로고    scopus 로고
    • Galagan JE, Calvo SE, Cuomo C, Ma LJ, Wortman JR, Batzoglou S, Lee SI, Basturkmen M, Spevak CC, Clutter buck J, Kapitonov V, Jurka J, Scazzocchio C, Farman M. Butler J, Purcell S, Harris S, Braus GH, Draht O, Busch S, D'Enfert C, Bouchier C, Goldman GH, Bell-Pe-dersen D, Griffiths-Jones S, Doonan JH, Yu J, Vienken K, Pain A, Freitag M, Selker EU, Archer DB, Penalva MA, Oakley BR, Momany M, Tanaka T, Kumagai T, Asai K, Machida M, Merman WC, Denning DW, Caddick M, Hynes M, Paoletti M. Fischer R, Miller B, Dyer P, Sachs MS, Osmani SA, Birren BW (2005) Sequencing of Aspergillus nidulans and comparative analysis with A.fumigatus and A, oryzae. Nature 438:1105-1115 .
    • Galagan JE, Calvo SE, Cuomo C, Ma LJ, Wortman JR, Batzoglou S, Lee SI, Basturkmen M, Spevak CC, Clutter buck J, Kapitonov V, Jurka J, Scazzocchio C, Farman M. Butler J, Purcell S, Harris S, Braus GH, Draht O, Busch S, D'Enfert C, Bouchier C, Goldman GH, Bell-Pe-dersen D, Griffiths-Jones S, Doonan JH, Yu J, Vienken K, Pain A, Freitag M, Selker EU, Archer DB, Penalva MA, Oakley BR, Momany M, Tanaka T, Kumagai T, Asai K, Machida M, Merman WC, Denning DW, Caddick M, Hynes M, Paoletti M. Fischer R, Miller B, Dyer P, Sachs MS, Osmani SA, Birren BW (2005) Sequencing of Aspergillus nidulans and comparative analysis with A.fumigatus and A, oryzae. Nature 438:1105-1115 .


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