메뉴 건너뛰기




Volumn 171, Issue 5, 2011, Pages 299-323

Fungal Proteases and Their Pathophysiological Effects

Author keywords

Allergens; Fungi; Inflammation; Proteases; Th2 responses

Indexed keywords

FUNGAL PROTEIN; PEPTIDE HYDROLASE;

EID: 79953294138     PISSN: 0301486X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11046-010-9386-2     Document Type: Review
Times cited : (173)

References (205)
  • 1
    • 0022766061 scopus 로고
    • Nomenclature: protease, proteinase and peptidase
    • Barrett AJ, McDonald JK. Nomenclature: protease, proteinase and peptidase. Biochem J. 1986; 237: 935.
    • (1986) Biochem J , vol.237 , pp. 935
    • Barrett, A.J.1    McDonald, J.K.2
  • 2
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings ND, Barrett AJ. Evolutionary families of peptidases. Biochem J. 1993; 290: 205-18.
    • (1993) Biochem J , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 4
    • 42249109450 scopus 로고    scopus 로고
    • Serine peptidases: classification, structure and function
    • Page MJ, Di Cera E. Serine peptidases: classification, structure and function. Cell Mol Life Sci. 2008; 65: 1220-36.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1220-1236
    • Page, M.J.1    Di Cera, E.2
  • 7
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings ND, Barrett AJ. Families of cysteine peptidases. Meth Enzymol. 1994; 244: 461-86.
    • (1994) Meth Enzymol , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 8
    • 0028136279 scopus 로고
    • Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization
    • Xu HE, Johnston SA. Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem. 1994; 269: 21177-83.
    • (1994) J Biol Chem , vol.269 , pp. 21177-21183
    • Xu, H.E.1    Johnston, S.A.2
  • 9
    • 0035951635 scopus 로고    scopus 로고
    • Molecular cloning of PalBH, a mammalian homologue of the Aspergillus atypical calpain PalB
    • Futai E, Kubo T, Sorimachi H, Suzuki K, Maeda T. Molecular cloning of PalBH, a mammalian homologue of the Aspergillus atypical calpain PalB. Biochim Biophys Acta. 2001; 1517: 316-9.
    • (2001) Biochim Biophys Acta , vol.1517 , pp. 316-319
    • Futai, E.1    Kubo, T.2    Sorimachi, H.3    Suzuki, K.4    Maeda, T.5
  • 10
    • 0029004315 scopus 로고
    • Families of aspartic peptidases and those of unknown catalytic mechanism
    • Rawlings ND, Barrett AJ. Families of aspartic peptidases and those of unknown catalytic mechanism. Meth Enzymol. 1995; 248: 105-20.
    • (1995) Meth Enzymol , vol.248 , pp. 105-120
    • Rawlings, N.D.1    Barrett, A.J.2
  • 11
    • 57649219258 scopus 로고    scopus 로고
    • Penicillopepsin
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), London: Elsevier
    • Hofmann T. Penicillopepsin. In: Barrett AJ, Rawlings ND, Woessner JF, editors. Handbook of proteolytic enzymes. London: Elsevier; 2004. p. 99-104.
    • (2004) Handbook of Proteolytic Enzymes , pp. 99-104
    • Hofmann, T.1
  • 12
    • 79953322482 scopus 로고    scopus 로고
    • Rhizopuspepsin
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), London: Elsevier
    • Dunn BM. Rhizopuspepsin. In: Barrett AJ, Rawlings ND, Woessner JF, editors. Handbook of proteolytic enzymes. London: Elsevier; 2004. p. 108-11.
    • (2004) Handbook of Proteolytic Enzymes , pp. 108-111
    • Dunn, B.M.1
  • 13
    • 84944043841 scopus 로고    scopus 로고
    • Aspergillopepsin I
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), London: Elsevier
    • Ichishima E. Aspergillopepsin I. In: Barrett AJ, Rawlings ND, Woessner JF, editors. Handbook of proteolytic enzymes. London: Elsevier; 2004. p. 92-9.
    • (2004) Handbook of Proteolytic Enzymes , pp. 92-99
    • Ichishima, E.1
  • 14
    • 70450225229 scopus 로고    scopus 로고
    • The yeast Candidaalbicans evades human complement attack by secretion of aspartic proteases
    • Gropp K, Schild L, Schindler S, Hube B, Zipfel PF, Skerka C. The yeast Candidaalbicans evades human complement attack by secretion of aspartic proteases. Mol Immunol. 2009; 47: 465-75.
    • (2009) Mol Immunol , vol.47 , pp. 465-475
    • Gropp, K.1    Schild, L.2    Schindler, S.3    Hube, B.4    Zipfel, P.F.5    Skerka, C.6
  • 15
    • 23844501292 scopus 로고    scopus 로고
    • Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae
    • Krysan DJ, Ting EL, Abeijon C, Kroos L, Fuller RS. Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae. Eukaryot Cell. 2005; 4: 1364-74.
    • (2005) Eukaryot Cell , vol.4 , pp. 1364-1374
    • Krysan, D.J.1    Ting, E.L.2    Abeijon, C.3    Kroos, L.4    Fuller, R.S.5
  • 16
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings ND, Barrett AJ. Evolutionary families of metallopeptidases. Methods Enzymol. 1995; 248: 183-228.
    • (1995) Methods Enzymol , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 17
    • 0028340071 scopus 로고
    • Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung
    • Markaryan A, Morozova I, Yu H, Kolattukudy PE. Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung. Infect Immun. 1994; 62: 2149-57.
    • (1994) Infect Immun , vol.62 , pp. 2149-2157
    • Markaryan, A.1    Morozova, I.2    Yu, H.3    Kolattukudy, P.E.4
  • 18
    • 69049098541 scopus 로고    scopus 로고
    • Aspergillus fumigatus secreted proteases
    • J.-P. Latge and W. J. Steinbach (Eds.), Washington, DC: ASM Press
    • Monod M, Jousson O, Reichard U. Aspergillus fumigatus secreted proteases. In: Latge J-P, Steinbach WJ, editors. Aspergillus fumigatus and aspergillosis. Washington, DC: ASM Press; 2009. p. 87-106.
    • (2009) Aspergillus Fumigatus and Aspergillosis , pp. 87-106
    • Monod, M.1    Jousson, O.2    Reichard, U.3
  • 22
    • 0027119999 scopus 로고
    • Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus
    • Jaton-Ogay K, Suter M, Crameri R, Falchetto R, Fatih A, Monod M. Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus. FEMS Microbiol Lett. 1992; 71: 163-8.
    • (1992) FEMS Microbiol Lett , vol.71 , pp. 163-168
    • Jaton-Ogay, K.1    Suter, M.2    Crameri, R.3    Falchetto, R.4    Fatih, A.5    Monod, M.6
  • 23
    • 0034163776 scopus 로고    scopus 로고
    • Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies
    • Chow LP, Liu SL, Yu CJ, Liao HK, Tsai JJ, Tang TK. Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies. Biochem J. 2000; 346: 423-31.
    • (2000) Biochem J , vol.346 , pp. 423-431
    • Chow, L.P.1    Liu, S.L.2    Yu, C.J.3    Liao, H.K.4    Tsai, J.J.5    Tang, T.K.6
  • 25
    • 0028057705 scopus 로고
    • Recombinant expression and antigenic properties of a 32-kilodalton extracellular alkaline protease, representing a possible virulence factor from Aspergillus fumigatus
    • Moser M, Menz G, Blaser K, Crameri R. Recombinant expression and antigenic properties of a 32-kilodalton extracellular alkaline protease, representing a possible virulence factor from Aspergillus fumigatus. Infect Immun. 1994; 62: 936-42.
    • (1994) Infect Immun , vol.62 , pp. 936-942
    • Moser, M.1    Menz, G.2    Blaser, K.3    Crameri, R.4
  • 26
    • 0034471552 scopus 로고    scopus 로고
    • Review: peptidases and peptidase inhibitors in the pathogenesis of diseases. Disturbances in the ubiquitin-mediated proteolytic system. Protease-antiprotease imbalance in inflammatory reactions. Role of cathepsins in tumor progression
    • Bank U, Krüger S, Langner J, Roessner A. Review: peptidases and peptidase inhibitors in the pathogenesis of diseases. Disturbances in the ubiquitin-mediated proteolytic system. Protease-antiprotease imbalance in inflammatory reactions. Role of cathepsins in tumor progression. Adv Exp Med Biol. 2000; 477: 349-78.
    • (2000) Adv Exp Med Biol , vol.477 , pp. 349-378
    • Bank, U.1    Krüger, S.2    Langner, J.3    Roessner, A.4
  • 27
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • Schaller A. A cut above the rest: the regulatory function of plant proteases. Planta. 2004; 220: 183-97.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 29
    • 0033773109 scopus 로고    scopus 로고
    • Molecular characterization and influence on fungal development of ALP2, a novel serine proteinase from Aspergillus fumigatus
    • Reichard U, Cole GT, Hill TW, Rüchel R, Monod M. Molecular characterization and influence on fungal development of ALP2, a novel serine proteinase from Aspergillus fumigatus. Int J Med Microbiol. 2000; 290: 549-58.
    • (2000) Int J Med Microbiol , vol.290 , pp. 549-558
    • Reichard, U.1    Cole, G.T.2    Hill, T.W.3    Rüchel, R.4    Monod, M.5
  • 30
    • 0036090485 scopus 로고    scopus 로고
    • Protease secretion in glucoamylase producer Aspergillus niger cultures: fungal morphology and inoculum effects
    • Papagianni M, Moo-Young M. Protease secretion in glucoamylase producer Aspergillus niger cultures: fungal morphology and inoculum effects. Proc Biochem. 2002; 37: 1271-88.
    • (2002) Proc Biochem , vol.37 , pp. 1271-1288
    • Papagianni, M.1    Moo-Young, M.2
  • 31
    • 0026593801 scopus 로고
    • Evidence for controlled autoproteolysis of alkaline protease. A mechanism for physiological regulation of conidial discharge in Conidiobolus coronatus
    • Phadatare SU, Srinivasan MC, Deshpande VV. Evidence for controlled autoproteolysis of alkaline protease. A mechanism for physiological regulation of conidial discharge in Conidiobolus coronatus. Eur J Biochem. 1992; 205: 679-86.
    • (1992) Eur J Biochem , vol.205 , pp. 679-686
    • Phadatare, S.U.1    Srinivasan, M.C.2    Deshpande, V.V.3
  • 32
    • 0036180681 scopus 로고    scopus 로고
    • Breaking the singleton of germination protease
    • Pei J, Grishin NV. Breaking the singleton of germination protease. Protein Sci. 2002; 11: 691-7.
    • (2002) Protein Sci , vol.11 , pp. 691-697
    • Pei, J.1    Grishin, N.V.2
  • 33
    • 73649119219 scopus 로고    scopus 로고
    • Identification and purification of metalloprotease from dry grass pea (Lathyrus sativus L.) seeds
    • Ramakrishna V, Rajasekhar S, Reddy LS. Identification and purification of metalloprotease from dry grass pea (Lathyrus sativus L.) seeds. Appl Biochem Biotechnol. 2010; 160: 63-71.
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 63-71
    • Ramakrishna, V.1    Rajasekhar, S.2    Reddy, L.S.3
  • 35
    • 0037323859 scopus 로고    scopus 로고
    • Allergen detection from 11 fungal species before and after germination
    • Green BJ, Mitakakis TZ, Tovey ER. Allergen detection from 11 fungal species before and after germination. J Allergy Clin Immunol. 2003; 111: 285-9.
    • (2003) J Allergy Clin Immunol , vol.111 , pp. 285-289
    • Green, B.J.1    Mitakakis, T.Z.2    Tovey, E.R.3
  • 38
    • 0033693198 scopus 로고    scopus 로고
    • Intra- and intermolecular events direct maturation of Candida albicans secreted aspartic proteinase Sap1p
    • Beggah S, Lechénne B, Reichard U, Foundling S, Monod M. Intra- and intermolecular events direct maturation of Candida albicans secreted aspartic proteinase Sap1p. Microbiology. 2000; 146: 2765-73.
    • (2000) Microbiology , vol.146 , pp. 2765-2773
    • Beggah, S.1    Lechénne, B.2    Reichard, U.3    Foundling, S.4    Monod, M.5
  • 39
    • 0029930574 scopus 로고    scopus 로고
    • Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides
    • Markaryan A, Lee JD, Sirakova TD, Kolattukudy PE. Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides. J Bacteriol. 1996; 178: 2211-5.
    • (1996) J Bacteriol , vol.178 , pp. 2211-2215
    • Markaryan, A.1    Lee, J.D.2    Sirakova, T.D.3    Kolattukudy, P.E.4
  • 42
    • 70349245249 scopus 로고    scopus 로고
    • Characterization and gene cloning of a novel serine protease with nematicidal activity from Trichoderma pseudokoningii SMF2
    • Chen LL, Liu LJ, Shi M, Song XY, Zheng CY, Chen XL, Zhang YZ. Characterization and gene cloning of a novel serine protease with nematicidal activity from Trichoderma pseudokoningii SMF2. FEMS Microbiol Lett. 2009; 299: 135-42.
    • (2009) FEMS Microbiol Lett , vol.299 , pp. 135-142
    • Chen, L.L.1    Liu, L.J.2    Shi, M.3    Song, X.Y.4    Zheng, C.Y.5    Chen, X.L.6    Zhang, Y.Z.7
  • 43
    • 0023426052 scopus 로고
    • Distribution of chymoelastases and trypsin-like enzymes in five species of entomopathogenic deuteromycetes
    • St. Leger RJ, Cooper RM, Charnley AK. Distribution of chymoelastases and trypsin-like enzymes in five species of entomopathogenic deuteromycetes. Arch Biochem Biophys. 1987; 258: 123-31.
    • (1987) Arch Biochem Biophys , vol.258 , pp. 123-131
    • St. Leger, R.J.1    Cooper, R.M.2    Charnley, A.K.3
  • 44
    • 0027478095 scopus 로고
    • Analysis of aminopeptidase and dipeptidylpeptidase IV from the entomopathogenic fungus Metarhizium anisopliae
    • St. Leger RJ, Cooper RM, Charnley AK. Analysis of aminopeptidase and dipeptidylpeptidase IV from the entomopathogenic fungus Metarhizium anisopliae. J Gen Microbiol. 1993; 139: 237-43.
    • (1993) J Gen Microbiol , vol.139 , pp. 237-243
    • St. Leger, R.J.1    Cooper, R.M.2    Charnley, A.K.3
  • 45
    • 77953432815 scopus 로고    scopus 로고
    • Conidial surface proteins of Metarhizium anisopliae: source of activities related with toxic effects, host penetration and pathogenesis
    • Santi L, Beys da Silva WO, Berger M, Guimarãesv JA, Schrank A, Vainstein MH. Conidial surface proteins of Metarhizium anisopliae: source of activities related with toxic effects, host penetration and pathogenesis. Toxicon. 2010; 55: 874-80.
    • (2010) Toxicon , vol.55 , pp. 874-880
    • Santi, L.1    da Beys silva, W.O.2    Berger, M.3    Guimarãesv, J.A.4    Schrank, A.5    Vainstein, M.H.6
  • 46
    • 70249106320 scopus 로고    scopus 로고
    • Expressing a fusion protein with protease and chitinase activities increases the virulence of the insect pathogen Beauveria bassiana
    • Fang W, Feng J, Fan Y, Zhang Y, Bidochka MJ, Leger RJ, Pei Y. Expressing a fusion protein with protease and chitinase activities increases the virulence of the insect pathogen Beauveria bassiana. J Invertebr Pathol. 2009; 102: 155-9.
    • (2009) J Invertebr Pathol , vol.102 , pp. 155-159
    • Fang, W.1    Feng, J.2    Fan, Y.3    Zhang, Y.4    Bidochka, M.J.5    Leger, R.J.6    Pei, Y.7
  • 47
    • 43449084620 scopus 로고    scopus 로고
    • Addition of exogenous carbon and nitrogen sources to aphid exuviae modulates synthesis of proteases and chitinase by germinating conidia of Beauveria bassiana
    • Qazi SS, Khachatourians GG. Addition of exogenous carbon and nitrogen sources to aphid exuviae modulates synthesis of proteases and chitinase by germinating conidia of Beauveria bassiana. Arch Microbiol. 2008; 189: 589-96.
    • (2008) Arch Microbiol , vol.189 , pp. 589-596
    • Qazi, S.S.1    Khachatourians, G.G.2
  • 48
    • 0029940951 scopus 로고    scopus 로고
    • Mutations affecting extracellular protease production in the filamentous fungus Aspergillus nidulans
    • Katz ME, Flynn PK, vanKuyk PA, Cheetham BF. Mutations affecting extracellular protease production in the filamentous fungus Aspergillus nidulans. Mol Gen Genet. 1996; 250: 715-24.
    • (1996) Mol Gen Genet , vol.250 , pp. 715-724
    • Katz, M.E.1    Flynn, P.K.2    Vankuyk, P.A.3    Cheetham, B.F.4
  • 49
    • 0028093358 scopus 로고
    • Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger
    • Jarai G, Buxton F. Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger. Curr Genet. 1994; 26: 238-44.
    • (1994) Curr Genet , vol.26 , pp. 238-244
    • Jarai, G.1    Buxton, F.2
  • 50
    • 67650287293 scopus 로고    scopus 로고
    • Mutations in genes encoding sorting nexins alter production of intracellular and extracellular proteases in Aspergillus nidulans
    • Katz ME, Evans CJ, Heagney EE, vanKuyk PA, Kelly JM, Cheetham BF. Mutations in genes encoding sorting nexins alter production of intracellular and extracellular proteases in Aspergillus nidulans. Genetics. 2009; 181: 1239-47.
    • (2009) Genetics , vol.181 , pp. 1239-1247
    • Katz, M.E.1    Evans, C.J.2    Heagney, E.E.3    Vankuyk, P.A.4    Kelly, J.M.5    Cheetham, B.F.6
  • 51
    • 0032844240 scopus 로고    scopus 로고
    • The entomopathogenic fungus Metarhizium anisopliae alters ambient pH, allowing extracellular protease production and activity
    • St Leger RJ, Nelson JO, Screen SE. The entomopathogenic fungus Metarhizium anisopliae alters ambient pH, allowing extracellular protease production and activity. Microbiology. 1999; 145: 2691-9.
    • (1999) Microbiology , vol.145 , pp. 2691-2699
    • St Leger, R.J.1    Nelson, J.O.2    Screen, S.E.3
  • 52
    • 70749143546 scopus 로고    scopus 로고
    • Spontaneous and protein-induced secretion of proteinases from Saccharomyces cerevisiae
    • Kurucová A, Farkasová E, Varecka L, Simkovic M. Spontaneous and protein-induced secretion of proteinases from Saccharomyces cerevisiae. J Basic Microbiol. 2009; 49: 545-52.
    • (2009) J Basic Microbiol , vol.49 , pp. 545-552
    • Kurucová, A.1    Farkasová, E.2    Varecka, L.3    Simkovic, M.4
  • 53
    • 0028208859 scopus 로고
    • Immunologic significance of a collagen-derived culture filtrate containing proteolytic activity in Aspergillus-related diseases
    • Tomee JF, Kauffman HF, Klimp AH, de Monchy JG, Köeter GH, Dubois AE. Immunologic significance of a collagen-derived culture filtrate containing proteolytic activity in Aspergillus-related diseases. Allergy Clin Immunol. 1994; 93: 768-78.
    • (1994) Allergy Clin Immunol , vol.93 , pp. 768-778
    • Tomee, J.F.1    Kauffman, H.F.2    Klimp, A.H.3    de Monchy, J.G.4    Köeter, G.H.5    Dubois, A.E.6
  • 54
    • 34548398775 scopus 로고    scopus 로고
    • The role of fungal proteinases in pathophysiology of Stachybotrys chartarum
    • Yike I, Rand T, Dearborn DG. The role of fungal proteinases in pathophysiology of Stachybotrys chartarum. Mycopathologia. 2007; 164: 171-81.
    • (2007) Mycopathologia , vol.164 , pp. 171-181
    • Yike, I.1    Rand, T.2    Dearborn, D.G.3
  • 55
    • 71049123227 scopus 로고    scopus 로고
    • The effect of environmental conditions on extracellular protease activity in controlled fermentations of Aspergillus niger
    • Braaksma M, Smilde AK, van der Werf MJ, Punt PJ. The effect of environmental conditions on extracellular protease activity in controlled fermentations of Aspergillus niger. Microbiology. 2009; 155: 3430-9.
    • (2009) Microbiology , vol.155 , pp. 3430-3439
    • Braaksma, M.1    Smilde, A.K.2    van der Werf, M.J.3    Punt, P.J.4
  • 56
    • 55149091122 scopus 로고    scopus 로고
    • Secreted proteases from dermatophytes
    • Monod M. Secreted proteases from dermatophytes. Mycopathologia. 2008; 166: 285-94.
    • (2008) Mycopathologia , vol.166 , pp. 285-294
    • Monod, M.1
  • 57
    • 67349117281 scopus 로고    scopus 로고
    • Making the cut: central roles of intra membrane proteolysis in pathogenic microorganisms
    • Urban S. Making the cut: central roles of intra membrane proteolysis in pathogenic microorganisms. Nat Rev Microbiol. 2009; 7: 411-23.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 411-423
    • Urban, S.1
  • 59
    • 23744452791 scopus 로고    scopus 로고
    • Characterization of the Aspergillus niger dapB gene, which encodes a novel fungal type IV dipeptidyl aminopeptidase
    • Jalving R, Godefrooij J, Veen WJ, van Ooyen AJJ, Schaap PJ. Characterization of the Aspergillus niger dapB gene, which encodes a novel fungal type IV dipeptidyl aminopeptidase. Mol Genet Genomics. 2005; 273: 319-25.
    • (2005) Mol Genet Genomics , vol.273 , pp. 319-325
    • Jalving, R.1    Godefrooij, J.2    Veen, W.J.3    van Ooyen, A.J.J.4    Schaap, P.J.5
  • 62
    • 63949088399 scopus 로고    scopus 로고
    • Signal peptide peptidases: a family of intra membrane-cleaving proteases that cleave type 2 transmembrane proteins
    • Golde TE, Wolfe MS, Greenbaum DC. Signal peptide peptidases: a family of intra membrane-cleaving proteases that cleave type 2 transmembrane proteins. Semin Cell Dev Biol. 2009; 20: 225-30.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 225-230
    • Golde, T.E.1    Wolfe, M.S.2    Greenbaum, D.C.3
  • 63
    • 20444466821 scopus 로고    scopus 로고
    • ADAMs are present in fungi: Identification of two novel ADAM genes in Aspergillus fumigatus
    • Lavens SE, Rovira-Graells N, Birch M, Tuckwell D. ADAMs are present in fungi: Identification of two novel ADAM genes in Aspergillus fumigatus. FEMS Microbiol Lett. 2005; 248: 23-30.
    • (2005) FEMS Microbiol Lett , vol.248 , pp. 23-30
    • Lavens, S.E.1    Rovira-Graells, N.2    Birch, M.3    Tuckwell, D.4
  • 64
    • 1242300153 scopus 로고    scopus 로고
    • ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe
    • Nakamura TH, Abe H, Hirata A, Shimoda C. ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe. Eukaryot Cell. 2004; 3: 27-39.
    • (2004) Eukaryot Cell , vol.3 , pp. 27-39
    • Nakamura, T.H.1    Abe, H.2    Hirata, A.3    Shimoda, C.4
  • 65
    • 67651211898 scopus 로고    scopus 로고
    • Characterization of a novel ADAM protease expressed by Pneumocystis carinii
    • Kennedy CC, Kottom TJ, Limper AH. Characterization of a novel ADAM protease expressed by Pneumocystis carinii. Infect Immun. 2009; 77: 3328-36.
    • (2009) Infect Immun , vol.77 , pp. 3328-3336
    • Kennedy, C.C.1    Kottom, T.J.2    Limper, A.H.3
  • 66
    • 47749133814 scopus 로고    scopus 로고
    • Activation mechanism, functional role and shedding of glycosyl phosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface
    • Gagnon-Arsenault I, Parisé L, Tremblay J, Bourbonnais Y. Activation mechanism, functional role and shedding of glycosyl phosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface. Mol Microbiol. 2008; 69: 982-93.
    • (2008) Mol Microbiol , vol.69 , pp. 982-993
    • Gagnon-Arsenault, I.1    Parisé, L.2    Tremblay, J.3    Bourbonnais, Y.4
  • 67
    • 70350020265 scopus 로고    scopus 로고
    • Covalently linked cell wall proteins of Candida albicans and their role in fitness and virulence
    • Klis FM, Sosinska GJ, de Groot PW, Brul S. Covalently linked cell wall proteins of Candida albicans and their role in fitness and virulence. FEMS Yeast Res. 2009; 9: 1013-28.
    • (2009) FEMS Yeast Res , vol.9 , pp. 1013-1028
    • Klis, F.M.1    Sosinska, G.J.2    de Groot, P.W.3    Brul, S.4
  • 68
    • 0036571641 scopus 로고    scopus 로고
    • A polymerase chain reaction-based method for cloning novel members of a gene family using a combination of degenerate and inhibitory primers
    • Kunihiro S, Kananishi Y, Sano M, Naito K, Matsuura Y, Taleno Y, Gojohori T, Yamagata Y, Abe K, Machida M. A polymerase chain reaction-based method for cloning novel members of a gene family using a combination of degenerate and inhibitory primers. Gene. 2002; 289: 177-84.
    • (2002) Gene , vol.289 , pp. 177-184
    • Kunihiro, S.1    Kananishi, Y.2    Sano, M.3    Naito, K.4    Matsuura, Y.5    Taleno, Y.6    Gojohori, T.7    Yamagata, Y.8    Abe, K.9    Machida, M.10
  • 71
    • 0023463750 scopus 로고
    • Protease B of the lysosome-like vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases
    • Moehle CM, Tizard R, Lemmon SK, Smart J, Jones EW. Protease B of the lysosome-like vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases. Mol Cell Biol. 1987; 7: 4390-9.
    • (1987) Mol Cell Biol , vol.7 , pp. 4390-4399
    • Moehle, C.M.1    Tizard, R.2    Lemmon, S.K.3    Smart, J.4    Jones, E.W.5
  • 72
    • 0035086673 scopus 로고    scopus 로고
    • Identification of vacuolar serine protease, major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis
    • Shen HD, Lin WL, Tam MF, Chou H, Wang CW, Tsai JJ, Wang SR, Han SH. Identification of vacuolar serine protease, major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis. Clin Exp Allergy. 2001; 31: 295-302.
    • (2001) Clin Exp Allergy , vol.31 , pp. 295-302
    • Shen, H.D.1    Lin, W.L.2    Tam, M.F.3    Chou, H.4    Wang, C.W.5    Tsai, J.J.6    Wang, S.R.7    Han, S.H.8
  • 76
    • 63249101831 scopus 로고    scopus 로고
    • Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III
    • Rodríguez-Galán O, Galindo A, Hervás-Aguilar A, Arst HN Jr, Peñalva MA. Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III. J Biol Chem. 2009; 284: 4404-12.
    • (2009) J Biol Chem , vol.284 , pp. 4404-4412
    • Rodríguez-Galán, O.1    Galindo, A.2    Hervás-Aguilar, A.3    Arst Jr., H.N.4    Peñalva, M.A.5
  • 81
    • 0142058021 scopus 로고    scopus 로고
    • Exposure, sensitization, and mechanisms of fungus-induced asthma
    • Kauffman HF, van der Heide S. Exposure, sensitization, and mechanisms of fungus-induced asthma. Curr Allergy Asthma Rep. 2003; 3: 430-7.
    • (2003) Curr Allergy Asthma Rep , vol.3 , pp. 430-437
    • Kauffman, H.F.1    van der Heide, S.2
  • 83
    • 69549091576 scopus 로고    scopus 로고
    • Reddish, scaly, and itchy: how proteases and their inhibitors contribute to inflammatory skin diseases
    • Meyer-Hoffert U. Reddish, scaly, and itchy: how proteases and their inhibitors contribute to inflammatory skin diseases. Arch Immunol Ther Exp. 2009; 57: 345-54.
    • (2009) Arch Immunol Ther Exp , vol.57 , pp. 345-354
    • Meyer-Hoffert, U.1
  • 84
    • 34548175783 scopus 로고    scopus 로고
    • Comprehensive analysis of proteins secreted by Trichophytonrubrum and Trichophytonviolaceum under in vitro conditions
    • Giddey K, Monod M, Barblan J, Potts A, Waridel P, Zaugg C, Quadroni M. Comprehensive analysis of proteins secreted by Trichophytonrubrum and Trichophytonviolaceum under in vitro conditions. J Proteome Res. 2007; 6: 3081-92.
    • (2007) J Proteome Res , vol.6 , pp. 3081-3092
    • Giddey, K.1    Monod, M.2    Barblan, J.3    Potts, A.4    Waridel, P.5    Zaugg, C.6    Quadroni, M.7
  • 85
    • 33746420068 scopus 로고    scopus 로고
    • Purification and characterization of a 315 kDa keratinolytic subtilisin-like serine protease from Microsporum canis and evidence of its secretion in naturally infected cats
    • Mignon B, Swinnen M, Bouchara JP, Hofinger M, Nikkels A, Pierard G, Gerday C, Losson B. Purification and characterization of a 315 kDa keratinolytic subtilisin-like serine protease from Microsporum canis and evidence of its secretion in naturally infected cats. Med Mycol. 1998; 36: 395-404.
    • (1998) Med Mycol , vol.36 , pp. 395-404
    • Mignon, B.1    Swinnen, M.2    Bouchara, J.P.3    Hofinger, M.4    Nikkels, A.5    Pierard, G.6    Gerday, C.7    Losson, B.8
  • 86
    • 0034955223 scopus 로고    scopus 로고
    • Purification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis
    • Brouta F, Descamps F, Fett T, Losson B, Gerday C, Mignon B. Purification and characterization of a 43. 5 kDa keratinolytic metalloprotease from Microsporum canis. Med Mycol. 2001; 39: 269-75.
    • (2001) Med Mycol , vol.39 , pp. 269-275
    • Brouta, F.1    Descamps, F.2    Fett, T.3    Losson, B.4    Gerday, C.5    Mignon, B.6
  • 87
  • 89
    • 77749339883 scopus 로고    scopus 로고
    • Differential gene expression in the pathogenic dermatophyte Arthroderma benhamiae in vitro versus during infection
    • Staib P, Zaugg C, Mignon B, Weber J, Grumbt M, Pradervand S, Harshman K, Monod M. Differential gene expression in the pathogenic dermatophyte Arthroderma benhamiae in vitro versus during infection. Microbiology. 2010; 156: 884-95.
    • (2010) Microbiology , vol.156 , pp. 884-895
    • Staib, P.1    Zaugg, C.2    Mignon, B.3    Weber, J.4    Grumbt, M.5    Pradervand, S.6    Harshman, K.7    Monod, M.8
  • 91
    • 0025847569 scopus 로고
    • Isolation and characterization of an extracellular alkaline protease of Aspergillusfumigatus
    • Monod M, Togni G, Rahalison L, Frenk E. Isolation and characterization of an extracellular alkaline protease of Aspergillusfumigatus. J Med Microbiol. 1991; 35: 23-8.
    • (1991) J Med Microbiol , vol.35 , pp. 23-28
    • Monod, M.1    Togni, G.2    Rahalison, L.3    Frenk, E.4
  • 92
    • 55449083640 scopus 로고    scopus 로고
    • Investigation of extracellular elastase, acid proteinase and phospholipase activities as putative virulence factors in clinical isolates of Aspergillus species
    • Alp S, Arikan S. Investigation of extracellular elastase, acid proteinase and phospholipase activities as putative virulence factors in clinical isolates of Aspergillus species. J Basic Microbiol. 2008; 48: 331-7.
    • (2008) J Basic Microbiol , vol.48 , pp. 331-337
    • Alp, S.1    Arikan, S.2
  • 93
    • 0035423126 scopus 로고    scopus 로고
    • The pathobiology of Aspergillus fumigatus
    • Latgé J-P. The pathobiology of Aspergillus fumigatus. Trends Microbiol. 2001; 9: 382-9.
    • (2001) Trends Microbiol , vol.9 , pp. 382-389
    • Latgé, J.-P.1
  • 94
    • 0021349201 scopus 로고
    • Correlation of elastase production by some strains of Aspergillus fumigatus with ability to cause pulmonary invasive aspergillosis in mice
    • Kothary MH, Chase T, Macmillan JD. Correlation of elastase production by some strains of Aspergillus fumigatus with ability to cause pulmonary invasive aspergillosis in mice. Infect Immun. 1984; 43: 320-5.
    • (1984) Infect Immun , vol.43 , pp. 320-325
    • Kothary, M.H.1    Chase, T.2    Macmillan, J.D.3
  • 95
    • 0029889602 scopus 로고    scopus 로고
    • Disruption of the serine proteinase gene (sep) in Aspergillusflavus leads to a compensatory increase in the expression of a metalloproteinase gene (mep20)
    • Ramesh MV, Kolattukudy PE. Disruption of the serine proteinase gene (sep) in Aspergillusflavus leads to a compensatory increase in the expression of a metalloproteinase gene (mep20). J Bacteriol. 1996; 178: 3899-907.
    • (1996) J Bacteriol , vol.178 , pp. 3899-3907
    • Ramesh, M.V.1    Kolattukudy, P.E.2
  • 96
    • 69049108738 scopus 로고    scopus 로고
    • Transcription factor PrtT controls expression of multiple secreted proteases in the human pathogenic mold Aspergillus fumigatus
    • Sharon H, Hagag S, Osherov N. Transcription factor PrtT controls expression of multiple secreted proteases in the human pathogenic mold Aspergillus fumigatus. Infect Immun. 2009; 77: 4051-60.
    • (2009) Infect Immun , vol.77 , pp. 4051-4060
    • Sharon, H.1    Hagag, S.2    Osherov, N.3
  • 97
    • 69049101198 scopus 로고    scopus 로고
    • A regulator of Aspergillus fumigatus extracellular proteolytic activity is dispensable for virulence
    • Bergmann A, Hartmann T, Cairns T, Bignell EM, Krappmann S. A regulator of Aspergillus fumigatus extracellular proteolytic activity is dispensable for virulence. Infect Immun. 2009; 77: 4041-50.
    • (2009) Infect Immun , vol.77 , pp. 4041-4050
    • Bergmann, A.1    Hartmann, T.2    Cairns, T.3    Bignell, E.M.4    Krappmann, S.5
  • 98
    • 0026454973 scopus 로고
    • Lack of vessel wall elastolysis in human invasive aspergillosis
    • Jenning DW, Ward PN, Fenelon LE, Benbow EW. Lack of vessel wall elastolysis in human invasive aspergillosis. Infect Immun. 1992; 60: 5153-6.
    • (1992) Infect Immun , vol.60 , pp. 5153-5156
    • Jenning, D.W.1    Ward, P.N.2    Fenelon, L.E.3    Benbow, E.W.4
  • 99
    • 0028379683 scopus 로고
    • The effect of elastase-specific monoclonal and polyclonal antibodies on the virulence of Aspergillus fumigatus in immunocompromised mice
    • Frosco MT, Chase T, Macmillan JD. The effect of elastase-specific monoclonal and polyclonal antibodies on the virulence of Aspergillus fumigatus in immunocompromised mice. Mycopathologia. 1994; 125: 65-76.
    • (1994) Mycopathologia , vol.125 , pp. 65-76
    • Frosco, M.T.1    Chase, T.2    Macmillan, J.D.3
  • 100
    • 0025348952 scopus 로고
    • Effect of proteolytic activity on virulence of Candidaalbicans in burned mice
    • Neely AN, Holder IA. Effect of proteolytic activity on virulence of Candidaalbicans in burned mice. Infect Immun. 1990; 58: 1527-31.
    • (1990) Infect Immun , vol.58 , pp. 1527-1531
    • Neely, A.N.1    Holder, I.A.2
  • 102
    • 67650723299 scopus 로고    scopus 로고
    • Differential expression of Candida dubliniensis-secreted aspartyl proteinase genes (CdSAP1-4) under different physiological conditions and during infection of a keratinocyte culture
    • Loaiza-Loeza S, Parra-Ortega B, Cancino-Díaz JC, Illades-Aguiar B, Hernández-Rodríguez CH, Villa-Tanaca L. Differential expression of Candida dubliniensis-secreted aspartyl proteinase genes (CdSAP1-4) under different physiological conditions and during infection of a keratinocyte culture. FEMS Immunol Med Microbiol. 2009; 56: 212-22.
    • (2009) FEMS Immunol Med Microbiol , vol.56 , pp. 212-222
    • Loaiza-Loeza, S.1    Parra-Ortega, B.2    Cancino-Díaz, J.C.3    Illades-Aguiar, B.4    Hernández-Rodríguez, C.H.5    Villa-Tanaca, L.6
  • 103
    • 77951635702 scopus 로고    scopus 로고
    • Examination of potential virulence factors of Candida tropicalis clinical isolates from hospitalized patients
    • Negri M, Martins M, Henriques M, Svidzinski TI, Azeredo J, Oliveira R. Examination of potential virulence factors of Candida tropicalis clinical isolates from hospitalized patients. Mycopathologia. 2010; 169: 175-82.
    • (2010) Mycopathologia , vol.169 , pp. 175-182
    • Negri, M.1    Martins, M.2    Henriques, M.3    Svidzinski, T.I.4    Azeredo, J.5    Oliveira, R.6
  • 104
    • 57349131646 scopus 로고    scopus 로고
    • Secreted aspartic proteases are not required for invasion of reconstituted human epithelia by Candidaalbicans
    • Lermann U, Morschhäuser J. Secreted aspartic proteases are not required for invasion of reconstituted human epithelia by Candidaalbicans. Microbiology. 2008; 154: 3281-95.
    • (2008) Microbiology , vol.154 , pp. 3281-3295
    • Lermann, U.1    Morschhäuser, J.2
  • 107
    • 34548505283 scopus 로고    scopus 로고
    • Inflammatory effect of environmental proteases on airway mucosa
    • Reed CE. Inflammatory effect of environmental proteases on airway mucosa. Curr Allergy Asthma Rep. 2007; 7: 368-74.
    • (2007) Curr Allergy Asthma Rep , vol.7 , pp. 368-374
    • Reed, C.E.1
  • 109
    • 0031846001 scopus 로고    scopus 로고
    • Interactions between inhalant allergen extracts and airway epithelial cells: effect on cytokine production and cell detachment
    • Tomee JF, van Weissenbruch R, de Monchy JG, Kauffman HF. Interactions between inhalant allergen extracts and airway epithelial cells: effect on cytokine production and cell detachment. J Allergy Clin Immunol. 1998; 102: 75-85.
    • (1998) J Allergy Clin Immunol , vol.102 , pp. 75-85
    • Tomee, J.F.1    van Weissenbruch, R.2    de Monchy, J.G.3    Kauffman, H.F.4
  • 110
    • 0033933005 scopus 로고    scopus 로고
    • Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production
    • Kauffman HK, Tomee JFC, Marjolein A, van de Riet A, Timmerman JB, Borger P. Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production. J Allergy Clin Immunol. 2000; 105: 1185-93.
    • (2000) J Allergy Clin Immunol , vol.105 , pp. 1185-1193
    • Kauffman, H.K.1    Tomee, J.F.C.2    Marjolein, A.3    van de Riet, A.4    Timmerman, J.B.5    Borger, P.6
  • 112
    • 27544480438 scopus 로고    scopus 로고
    • A vacuolar serine protease (Rho m 2) is a major allergen of Rhodotorula mucilaginosa and belongs to a class of highly conserved pan-fungal allergens
    • Chou H, Tam MF, Lee SS, Tai HY, Chang CY, Chou CT, Shen HD. A vacuolar serine protease (Rho m 2) is a major allergen of Rhodotorula mucilaginosa and belongs to a class of highly conserved pan-fungal allergens. Int Arch Allergy Immunol. 2005; 138: 134-41.
    • (2005) Int Arch Allergy Immunol , vol.138 , pp. 134-141
    • Chou, H.1    Tam, M.F.2    Lee, S.S.3    Tai, H.Y.4    Chang, C.Y.5    Chou, C.T.6    Shen, H.D.7
  • 114
    • 0033118837 scopus 로고    scopus 로고
    • Pen c 1, a novel enzymic allergen protein from Penicilliumcitrinum. Purification, characterization, cloning and expression
    • Su NY, Yu CJ, Shen HD, Pan FM, Chow LP. Pen c 1, a novel enzymic allergen protein from Penicilliumcitrinum. Purification, characterization, cloning and expression. Eur J Biochem. 1999; 261: 115-23.
    • (1999) Eur J Biochem , vol.261 , pp. 115-123
    • Su, N.Y.1    Yu, C.J.2    Shen, H.D.3    Pan, F.M.4    Chow, L.P.5
  • 116
    • 0036121042 scopus 로고    scopus 로고
    • cDNA cloning, biological and immunological characterization of the alkaline serine protease major allergen from Penicillium chrysogenum
    • Chou H, Lai HY, Tam MF, Chou MY, Wang SR, Han SH, Shen HD. cDNA cloning, biological and immunological characterization of the alkaline serine protease major allergen from Penicillium chrysogenum. Int Arch Allergy Immunol. 2002; 127: 15-26.
    • (2002) Int Arch Allergy Immunol , vol.127 , pp. 15-26
    • Chou, H.1    Lai, H.Y.2    Tam, M.F.3    Chou, M.Y.4    Wang, S.R.5    Han, S.H.6    Shen, H.D.7
  • 117
    • 34250324671 scopus 로고    scopus 로고
    • Lys, pro and trp are critical core amino acid residues recognized by FUM20, a monoclonal antibody against serine protease pan-fungal allergens
    • Lee LH, Tam MF, Chou H, Tai HY, Shen HD. Lys, pro and trp are critical core amino acid residues recognized by FUM20, a monoclonal antibody against serine protease pan-fungal allergens. Int Arch Allergy Immunol. 2007; 143: 194-200.
    • (2007) Int Arch Allergy Immunol , vol.143 , pp. 194-200
    • Lee, L.H.1    Tam, M.F.2    Chou, H.3    Tai, H.Y.4    Shen, H.D.5
  • 118
    • 11144293555 scopus 로고    scopus 로고
    • Molecular and structural analysis of immunoglobulin E-binding epitopes of Pen ch 13, an alkaline serine protease major allergen from Penicilliumchrysogenum
    • Lai HY, Tam MF, Chou H, Lee SS, Tai HY, Shen HD. Molecular and structural analysis of immunoglobulin E-binding epitopes of Pen ch 13, an alkaline serine protease major allergen from Penicilliumchrysogenum. Clin Exp Allergy. 2004; 34: 1926-33.
    • (2004) Clin Exp Allergy , vol.34 , pp. 1926-1933
    • Lai, H.Y.1    Tam, M.F.2    Chou, H.3    Lee, S.S.4    Tai, H.Y.5    Shen, H.D.6
  • 120
    • 0037111369 scopus 로고    scopus 로고
    • A protease-activated pathway underlying Th cell type 2 activation and allergic lung disease
    • Kheradmand F, Kiss A, Xu J, Lee S-H, Kolattukudy PE, Corry DB. A protease-activated pathway underlying Th cell type 2 activation and allergic lung disease. J Immunol. 2002; 169: 5904-11.
    • (2002) J Immunol , vol.169 , pp. 5904-5911
    • Kheradmand, F.1    Kiss, A.2    Xu, J.3    Lee, S.-H.4    Kolattukudy, P.E.5    Corry, D.B.6
  • 121
    • 67349158914 scopus 로고    scopus 로고
    • Serine protease activity of Cur l 1 from Curvularia lunata augments Th2 response in mice
    • Tripathi P, Kukreja N, Singh BP, Arora N. Serine protease activity of Cur l 1 from Curvularia lunata augments Th2 response in mice. J Clin Immunol. 2009; 29: 292-302.
    • (2009) J Clin Immunol , vol.29 , pp. 292-302
    • Tripathi, P.1    Kukreja, N.2    Singh, B.P.3    Arora, N.4
  • 122
    • 53349118360 scopus 로고    scopus 로고
    • Effect of proteolytic activity of Epicoccum purpurescens major allergen, Epi p 1 in allergic inflammation
    • Kukreja N, Sridhara S, Singh BP, Arora N. Effect of proteolytic activity of Epicoccum purpurescens major allergen, Epi p 1 in allergic inflammation. Clin Exp Immunol. 2008; 154: 162-71.
    • (2008) Clin Exp Immunol , vol.154 , pp. 162-171
    • Kukreja, N.1    Sridhara, S.2    Singh, B.P.3    Arora, N.4
  • 123
    • 70049101757 scopus 로고    scopus 로고
    • Biology of lung dendritic cells at the origin of asthma
    • Lambrecht BN, Hammad H. Biology of lung dendritic cells at the origin of asthma. Immunity. 2009; 31: 412-24.
    • (2009) Immunity , vol.31 , pp. 412-424
    • Lambrecht, B.N.1    Hammad, H.2
  • 125
    • 40349085619 scopus 로고    scopus 로고
    • Proteinases and signaling: pathophysiological and therapeutic implications via PARs and more
    • Ramachandran R, Hollenberg MD. Proteinases and signaling: pathophysiological and therapeutic implications via PARs and more. Br J Pharmacol. 2008; 153: S263-82.
    • (2008) Br J Pharmacol , vol.153
    • Ramachandran, R.1    Hollenberg, M.D.2
  • 127
    • 34250878934 scopus 로고    scopus 로고
    • A novel therapeutic target in various lung diseases: airway proteases and protease-activated receptors
    • Sokolova E, Reiser G. A novel therapeutic target in various lung diseases: airway proteases and protease-activated receptors. Pharmacol Ther. 2007; 115: 70-83.
    • (2007) Pharmacol Ther , vol.115 , pp. 70-83
    • Sokolova, E.1    Reiser, G.2
  • 128
    • 0035184146 scopus 로고    scopus 로고
    • Protease activated receptors in human airways: upregulation of PAR-2 in respiratory epithelial cells from patients with asthma
    • Knight DA, Lim S, Scaffidi AK, Roche N, Chung KF, Stewart GA, Thompson PJ. Protease activated receptors in human airways: upregulation of PAR-2 in respiratory epithelial cells from patients with asthma. J Allergy Clin Immunol. 2001; 108: 797-803.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 797-803
    • Knight, D.A.1    Lim, S.2    Scaffidi, A.K.3    Roche, N.4    Chung, K.F.5    Stewart, G.A.6    Thompson, P.J.7
  • 129
    • 7944224566 scopus 로고    scopus 로고
    • The role of protease activation of inflammation in allergic respiratory diseases
    • Reed CE, Kita H. The role of protease activation of inflammation in allergic respiratory diseases. J Allergy Clin Immunol. 2004; 114: 997-1008.
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 997-1008
    • Reed, C.E.1    Kita, H.2
  • 132
    • 0035879347 scopus 로고    scopus 로고
    • Interaction of mite allergens Der p3 and Der p9 with protease-activated receptor-2 expressed by lung epithelial cells
    • Sun G, Stacey MA, Schmidt M, Mori L, Mattoli S. Interaction of mite allergens Der p3 and Der p9 with protease-activated receptor-2 expressed by lung epithelial cells. J Immunol. 2001; 167: 1014-21.
    • (2001) J Immunol , vol.167 , pp. 1014-1021
    • Sun, G.1    Stacey, M.A.2    Schmidt, M.3    Mori, L.4    Mattoli, S.5
  • 133
    • 0346995204 scopus 로고    scopus 로고
    • Cockroach proteases increase IL-8 expression in human bronchial epithelial cells via activation of protease-activated receptor-2 and extracellular-signal-regulated kinase
    • Page K, Strunk VS, Hershenson MB. Cockroach proteases increase IL-8 expression in human bronchial epithelial cells via activation of protease-activated receptor-2 and extracellular-signal-regulated kinase. J Allergy Clin Immunol. 2003; 112: 1112-8.
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 1112-1118
    • Page, K.1    Strunk, V.S.2    Hershenson, M.B.3
  • 134
    • 34247121961 scopus 로고    scopus 로고
    • Mold allergen, Pen c13, induced IL-8 expression in human airway epithelial cells by activating protease-activated receptor 1 and 2
    • Chiu L, Perng DW, Yu CH, Su SN, Chow LP. Mold allergen, Pen c13, induced IL-8 expression in human airway epithelial cells by activating protease-activated receptor 1 and 2. J Immunol. 2007; 178: 5237-44.
    • (2007) J Immunol , vol.178 , pp. 5237-5244
    • Chiu, L.1    Perng, D.W.2    Yu, C.H.3    Su, S.N.4    Chow, L.P.5
  • 135
    • 33751073431 scopus 로고    scopus 로고
    • Protease-dependent activation of nasal polyp epithelial cells by airborne fungi leads to migration of eosinophils and neutrophils
    • Shin SH, Lee YH, Jeon CH. Protease-dependent activation of nasal polyp epithelial cells by airborne fungi leads to migration of eosinophils and neutrophils. Acta Otolaryngol. 2006; 126: 1286-94.
    • (2006) Acta Otolaryngol , vol.126 , pp. 1286-1294
    • Shin, S.H.1    Lee, Y.H.2    Jeon, C.H.3
  • 136
    • 0036014824 scopus 로고    scopus 로고
    • Protease-activated receptor-2 activating peptide SLIGRL inhibits bacterial lipopolysaccharide-induced recruitment of polymorphonuclear leukocytes into the airways of mice
    • Moffatt JD, Jeffrey K, Cocks TM. Protease-activated receptor-2 activating peptide SLIGRL inhibits bacterial lipopolysaccharide-induced recruitment of polymorphonuclear leukocytes into the airways of mice. Am J Respir Cell Mol Biol. 2002; 26: 680-4.
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 680-684
    • Moffatt, J.D.1    Jeffrey, K.2    Cocks, T.M.3
  • 137
    • 73449084116 scopus 로고    scopus 로고
    • Candida albicans releases soluble factors that potentiate cytokine production by human cells through a protease-activated receptor 1- and 2-independent pathway
    • Cheng SC, Chai LY, Joosten LA, Vecchiarelli A, Hube B, van Der Meer JW, Kullberg BJ, Netea MG. Candida albicans releases soluble factors that potentiate cytokine production by human cells through a protease-activated receptor 1- and 2-independent pathway. Infect Immun. 2010; 78: 393-9.
    • (2010) Infect Immun , vol.78 , pp. 393-399
    • Cheng, S.C.1    Chai, L.Y.2    Joosten, L.A.3    Vecchiarelli, A.4    Hube, B.5    van der Meer, J.W.6    Kullberg, B.J.7    Netea, M.G.8
  • 138
    • 77249092615 scopus 로고    scopus 로고
    • New insights into innate immune mechanisms underlying allergenicity
    • Wills-Karp M, Nathan A, Page K, Karp CL. New insights into innate immune mechanisms underlying allergenicity. Mucosal Immunol. 2010; 3: 104-10.
    • (2010) Mucosal Immunol , vol.3 , pp. 104-110
    • Wills-Karp, M.1    Nathan, A.2    Page, K.3    Karp, C.L.4
  • 139
    • 70049100374 scopus 로고    scopus 로고
    • Innate cells and T helper 2 cell immunity in airway inflammation
    • Barrett NA, Austen KF. Innate cells and T helper 2 cell immunity in airway inflammation. Immunity. 2009; 31: 425-37.
    • (2009) Immunity , vol.31 , pp. 425-437
    • Barrett, N.A.1    Austen, K.F.2
  • 140
    • 70249093313 scopus 로고    scopus 로고
    • Proteases induce production of thymic stromal lymphopoietin by airway epithelial cells through protease-activated receptor-2
    • Kouzaki H, O'Grady SM, Lawrence CB, Kita H. Proteases induce production of thymic stromal lymphopoietin by airway epithelial cells through protease-activated receptor-2. J Immunol. 2009; 183: 1427-34.
    • (2009) J Immunol , vol.183 , pp. 1427-1434
    • Kouzaki, H.1    O'Grady, S.M.2    Lawrence, C.B.3    Kita, H.4
  • 141
    • 0036467527 scopus 로고    scopus 로고
    • Dendritic cells transport conidia and hyphae of Aspergillus fumigatus from the airways to the draining lymph nodes and initiate disparate Th responses to the fungus
    • Bozza S, Gaziano R, Spreca A, Bacci A, Montagnoli C, di Francesco P, Romani L. Dendritic cells transport conidia and hyphae of Aspergillus fumigatus from the airways to the draining lymph nodes and initiate disparate Th responses to the fungus. J Immunol. 2002; 168: 1362-71.
    • (2002) J Immunol , vol.168 , pp. 1362-1371
    • Bozza, S.1    Gaziano, R.2    Spreca, A.3    Bacci, A.4    Montagnoli, C.5    Di Francesco, P.6    Romani, L.7
  • 143
    • 44449153130 scopus 로고    scopus 로고
    • Fungal proteases induce Th2 polarization through limited dendritic cell maturation and reduced production of IL-12
    • Lamhamedi-Cherradi S-E, Martin RE, Ito T, Kheradmand F, Corry DB, Liu Y-J, Moyle M. Fungal proteases induce Th2 polarization through limited dendritic cell maturation and reduced production of IL-12. J Immunol. 2008; 180: 6000-9.
    • (2008) J Immunol , vol.180 , pp. 6000-6009
    • Lamhamedi-Cherradi, S.-E.1    Martin, R.E.2    Ito, T.3    Kheradmand, F.4    Corry, D.B.5    Liu, Y.-J.6    Moyle, M.7
  • 144
    • 77249166498 scopus 로고    scopus 로고
    • Role of basophils in the initiation of Th2 responses
    • Sokol CL, Medzhitov R. Role of basophils in the initiation of Th2 responses. Curr Opin Immunol. 2010; 22: 73-7.
    • (2010) Curr Opin Immunol , vol.22 , pp. 73-77
    • Sokol, C.L.1    Medzhitov, R.2
  • 145
    • 39449133957 scopus 로고    scopus 로고
    • A mechanism for the initiation of allergen-induced T helper type 2 responses
    • Sokol CL, Barton GM, Farr AG, Medzhitov R. A mechanism for the initiation of allergen-induced T helper type 2 responses. Nat Immunol. 2008; 9: 310-8.
    • (2008) Nat Immunol , vol.9 , pp. 310-318
    • Sokol, C.L.1    Barton, G.M.2    Farr, A.G.3    Medzhitov, R.4
  • 146
    • 0036413568 scopus 로고    scopus 로고
    • The proteolytic activity of the major dust mite allergen Der p 1 conditions dendritic cells to produce less interleukin-12: allergen-induced Th2 bias determined at the dendritic cell level
    • Ghaemmaghami AM, Gough L, Sewell HF, Shakib F. The proteolytic activity of the major dust mite allergen Der p 1 conditions dendritic cells to produce less interleukin-12: allergen-induced Th2 bias determined at the dendritic cell level. Clin Exp Allergy. 2002; 32: 1468-75.
    • (2002) Clin Exp Allergy , vol.32 , pp. 1468-1475
    • Ghaemmaghami, A.M.1    Gough, L.2    Sewell, H.F.3    Shakib, F.4
  • 147
    • 0031975246 scopus 로고    scopus 로고
    • Proteolytic cleavage of CD25, the alpha subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity
    • Schulz O, Sewell HF, Shakib F. Proteolytic cleavage of CD25, the alpha subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity. J Exp Med. 1998; 187: 271-5.
    • (1998) J Exp Med , vol.187 , pp. 271-275
    • Schulz, O.1    Sewell, H.F.2    Shakib, F.3
  • 148
    • 0028871972 scopus 로고
    • Der p 1, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23)
    • Schulz O, Laing P, Sewell HF, Shakib F. Der p 1, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23). Eur J Immunol. 1995; 25: 3191-4.
    • (1995) Eur J Immunol , vol.25 , pp. 3191-3194
    • Schulz, O.1    Laing, P.2    Sewell, H.F.3    Shakib, F.4
  • 151
    • 0035110656 scopus 로고    scopus 로고
    • Surfactant proteins A and D protect mice against pulmonary hypersensitivity induced by Aspergillus fumigatus antigens and allergens
    • Madan T, Kishore U, Singh M, Strong P, Clark H, Hussain EM, Reid KB, Sarma PU. Surfactant proteins A and D protect mice against pulmonary hypersensitivity induced by Aspergillus fumigatus antigens and allergens. J Clin Invest. 2001; 107: 467-75.
    • (2001) J Clin Invest , vol.107 , pp. 467-475
    • Madan, T.1    Kishore, U.2    Singh, M.3    Strong, P.4    Clark, H.5    Hussain, E.M.6    Reid, K.B.7    Sarma, P.U.8
  • 153
    • 33644908476 scopus 로고    scopus 로고
    • Pen ch 13 allergen induces secretion of mediators and degradation of occludin protein of human lung epithelial cells
    • Tai HY, Tam MF, Chou H, Peng HJ, Su SN, Perng DW, Shen HD. Pen ch 13 allergen induces secretion of mediators and degradation of occludin protein of human lung epithelial cells. Allergy. 2006; 61: 382-8.
    • (2006) Allergy , vol.61 , pp. 382-388
    • Tai, H.Y.1    Tam, M.F.2    Chou, H.3    Peng, H.J.4    Su, S.N.5    Perng, D.W.6    Shen, H.D.7
  • 154
    • 2542463854 scopus 로고    scopus 로고
    • Involvement of secreted Aspergillus fumigatus proteases in disruption of the actin fiber cytoskeleton and loss of focal adhesion sites in infected A549 lung pneumocytes
    • Kogan TV, Jadoun J, Mittelman L, Hirschberg K, Osherov N. Involvement of secreted Aspergillus fumigatus proteases in disruption of the actin fiber cytoskeleton and loss of focal adhesion sites in infected A549 lung pneumocytes. J Infect Dis. 2004; 189: 1965-73.
    • (2004) J Infect Dis , vol.189 , pp. 1965-1973
    • Kogan, T.V.1    Jadoun, J.2    Mittelman, L.3    Hirschberg, K.4    Osherov, N.5
  • 155
    • 0033120966 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma
    • Kumagai K, Ohno I, Okada S, Ohkawara Y, Suzuki K, Shinya T, Nagase H, Iwata K, Shirato K. Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma. J Immunol. 1999; 162: 4212-9.
    • (1999) J Immunol , vol.162 , pp. 4212-4219
    • Kumagai, K.1    Ohno, I.2    Okada, S.3    Ohkawara, Y.4    Suzuki, K.5    Shinya, T.6    Nagase, H.7    Iwata, K.8    Shirato, K.9
  • 158
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell. 2010; 140: 805-20.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 159
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune response
    • Iwasaki A, Medzhitov R. Toll-like receptor control of the adaptive immune response. Nat Immunol. 2004; 5: 987-95.
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 160
    • 1542674589 scopus 로고    scopus 로고
    • Immunity to fungal infections
    • Romani L. Immunity to fungal infections. Nat Rev Immunol. 2004; 4: 1-23.
    • (2004) Nat Rev Immunol , vol.4 , pp. 1-23
    • Romani, L.1
  • 162
    • 36349013892 scopus 로고    scopus 로고
    • PAR-2 activation and LPS synergistically enhance inflammatory signaling in airway epithelial cells by raising PAR expression level and interleukin 8- release
    • Ostrowska E, Sokolova E, Reiser G. PAR-2 activation and LPS synergistically enhance inflammatory signaling in airway epithelial cells by raising PAR expression level and interleukin 8- release. Am J Physiol Lung Cell Mol Physiol. 2007; 293: L1208-18.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.293
    • Ostrowska, E.1    Sokolova, E.2    Reiser, G.3
  • 168
    • 63449096467 scopus 로고    scopus 로고
    • Combined sensitization of mice to extracts of dust mite, ragweed, and Aspergillus species breaks through tolerance and establishes chronic features of asthma
    • Goplen N, Karim MZ, Liang Q, Gorska MM, Rozario S, Guo L, Alam R. Combined sensitization of mice to extracts of dust mite, ragweed, and Aspergillus species breaks through tolerance and establishes chronic features of asthma. J Allergy Clin Immunol. 2009; 123: 925-32.
    • (2009) J Allergy Clin Immunol , vol.123 , pp. 925-932
    • Goplen, N.1    Karim, M.Z.2    Liang, Q.3    Gorska, M.M.4    Rozario, S.5    Guo, L.6    Alam, R.7
  • 169
    • 0030254305 scopus 로고    scopus 로고
    • Effects of mold proteases on the biological activity of allergenic pollen extracts
    • Rosenbaum MR, Esch RE, Schwartzman RM. Effects of mold proteases on the biological activity of allergenic pollen extracts. Am J Vet Res. 1996; 57: 1447-52.
    • (1996) Am J Vet Res , vol.57 , pp. 1447-1452
    • Rosenbaum, M.R.1    Esch, R.E.2    Schwartzman, R.M.3
  • 170
    • 63849109933 scopus 로고    scopus 로고
    • Chronic intranasal administration of Aspergillus fumigatus spores leads to aggravation of airway inflammation and remodelling in asthmatic rats
    • Gao FS, Qiao JO, Zhang Y, Jin XQ. Chronic intranasal administration of Aspergillus fumigatus spores leads to aggravation of airway inflammation and remodelling in asthmatic rats. Respirology. 2009; 14: 360-70.
    • (2009) Respirology , vol.14 , pp. 360-370
    • Gao, F.S.1    Qiao, J.O.2    Zhang, Y.3    Jin, X.Q.4
  • 171
    • 0036104682 scopus 로고    scopus 로고
    • Animal models of allergic bronchopulmonary aspergillosis
    • Kurup VP, Grunig G. Animal models of allergic bronchopulmonary aspergillosis. Mycopathologia. 2002; 153: 165-77.
    • (2002) Mycopathologia , vol.153 , pp. 165-177
    • Kurup, V.P.1    Grunig, G.2
  • 174
    • 0034307654 scopus 로고    scopus 로고
    • Modulation of hemostatic mechanisms in bacterial infectious diseases
    • Tapper H, Herwald H. Modulation of hemostatic mechanisms in bacterial infectious diseases. Blood. 2000; 96: 2329-37.
    • (2000) Blood , vol.96 , pp. 2329-2337
    • Tapper, H.1    Herwald, H.2
  • 175
    • 1642506320 scopus 로고    scopus 로고
    • Stimulated human neutrophils form biologically active kinin peptides from high and low molecular weight kininogens
    • Stuardo M, Gonzalez CB, Nualart F, Boric M, Corthorn J, Bhoola KD, Figueroa CD. Stimulated human neutrophils form biologically active kinin peptides from high and low molecular weight kininogens. J Leukoc Biol. 2004; 75: 631-40.
    • (2004) J Leukoc Biol , vol.75 , pp. 631-640
    • Stuardo, M.1    Gonzalez, C.B.2    Nualart, F.3    Boric, M.4    Corthorn, J.5    Bhoola, K.D.6    Figueroa, C.D.7
  • 176
    • 62249183099 scopus 로고    scopus 로고
    • The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
    • Barbasz A, Kozik A. The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells. Biol Chem. 2009; 390: 269-75.
    • (2009) Biol Chem , vol.390 , pp. 269-275
    • Barbasz, A.1    Kozik, A.2
  • 177
    • 0035115246 scopus 로고    scopus 로고
    • Activation of the kinin-forming cascade on the surface of endothelial cells
    • Joseph K, Ghebrehiwet B, Kaplan AP. Activation of the kinin-forming cascade on the surface of endothelial cells. Biol Chem. 2001; 382: 71-5.
    • (2001) Biol Chem , vol.382 , pp. 71-75
    • Joseph, K.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 178
    • 0026487005 scopus 로고
    • Bradykinin and asthma
    • Barnes PJ. Bradykinin and asthma. Thorax. 1992; 47: 979-83.
    • (1992) Thorax , vol.47 , pp. 979-983
    • Barnes, P.J.1
  • 179
    • 10044233762 scopus 로고    scopus 로고
    • Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases
    • Imamura T, Potempa J, Travis J. Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases. Biol Chem. 2004; 385: 989-96.
    • (2004) Biol Chem , vol.385 , pp. 989-996
    • Imamura, T.1    Potempa, J.2    Travis, J.3
  • 180
    • 19344378755 scopus 로고    scopus 로고
    • Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus
    • Imamura T, Tanase S, Szmyd G, Kozik A, Travis J, Potempa J. Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus. J Exp Med. 2005; 201: 1669-76.
    • (2005) J Exp Med , vol.201 , pp. 1669-1676
    • Imamura, T.1    Tanase, S.2    Szmyd, G.3    Kozik, A.4    Travis, J.5    Potempa, J.6
  • 182
    • 0027305768 scopus 로고
    • Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity
    • Maruo K, Akaike T, Inada Y, Ohkubo I, Ono T, Maeda H. Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity. J Biol Chem. 1993; 268: 17711-5.
    • (1993) J Biol Chem , vol.268 , pp. 17711-17715
    • Maruo, K.1    Akaike, T.2    Inada, Y.3    Ohkubo, I.4    Ono, T.5    Maeda, H.6
  • 183
    • 0024340635 scopus 로고
    • Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases
    • Molla A, Yamamoto T, Akaike T, Miyoshi S, Maeda H. Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases. J Biol Chem. 1989; 264: 10589-94.
    • (1989) J Biol Chem , vol.264 , pp. 10589-10594
    • Molla, A.1    Yamamoto, T.2    Akaike, T.3    Miyoshi, S.4    Maeda, H.5
  • 184
    • 0025354608 scopus 로고
    • Activation of the plasma kallikrein-kinin system by Candida albicans proteinase
    • Kaminishi H, Tanaka M, Cho T, Maeda H, Hagihara Y. Activation of the plasma kallikrein-kinin system by Candida albicans proteinase. Infect Immun. 1990; 58: 2139-43.
    • (1990) Infect Immun , vol.58 , pp. 2139-2143
    • Kaminishi, H.1    Tanaka, M.2    Cho, T.3    Maeda, H.4    Hagihara, Y.5
  • 186
    • 0036137146 scopus 로고    scopus 로고
    • Isolation properties of stachyrase A, a chymotrypsin-like serine proteinase from Stachybotrys chartarum
    • Kordula T, Banbula A, Macomson J, Travis J. Isolation properties of stachyrase A, a chymotrypsin-like serine proteinase from Stachybotrys chartarum. Infect Immun. 2002; 70: 419-21.
    • (2002) Infect Immun , vol.70 , pp. 419-421
    • Kordula, T.1    Banbula, A.2    Macomson, J.3    Travis, J.4
  • 187
    • 0017650779 scopus 로고
    • Fungal proteases and the mammalian kinin system: I. Brinolase-catalyzed kinin formation and S2160 hydrolysis
    • Freedman HJ, Wilkens HJ, Back N. Fungal proteases and the mammalian kinin system: I. Brinolase-catalyzed kinin formation and S2160 hydrolysis. Res Commun Chem Pathol Pharmacol. 1977; 18: 543-60.
    • (1977) Res Commun Chem Pathol Pharmacol , vol.18 , pp. 543-560
    • Freedman, H.J.1    Wilkens, H.J.2    Back, N.3
  • 188
    • 0016772678 scopus 로고
    • Thrombolytic treatment with i.v. brinase of advanced arterial obliterative disease of the limbs
    • Lund F, Ekeström S, Frisch EP, Magaard F. Thrombolytic treatment with i. v. brinase of advanced arterial obliterative disease of the limbs. Angiology. 1975; 26: 534-56.
    • (1975) Angiology , vol.26 , pp. 534-556
    • Lund, F.1    Ekeström, S.2    Frisch, E.P.3    Magaard, F.4
  • 189
    • 36148973934 scopus 로고    scopus 로고
    • The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB
    • Sugimoto S, Fujii T, Morimiya T, Johodo O, Nakamura T. The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB. Biosci Biotechnol Biochem. 2007; 71: 2184-9.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 2184-2189
    • Sugimoto, S.1    Fujii, T.2    Morimiya, T.3    Johodo, O.4    Nakamura, T.5
  • 190
    • 34548665723 scopus 로고    scopus 로고
    • The dual role of the contact system in bacterial infectious disease
    • Frick IM, Björck L, Herwald H. The dual role of the contact system in bacterial infectious disease. Thromb Haemost. 2007; 98: 497-502.
    • (2007) Thromb Haemost , vol.98 , pp. 497-502
    • Frick, I.M.1    Björck, L.2    Herwald, H.3
  • 191
    • 75149138719 scopus 로고    scopus 로고
    • Binding and activation of the human plasma kinin-forming system on the cell walls of Candida albicans and Candida tropicalis
    • Karkowska-Kuleta J, Kozik A, Rapala-Kozik M. Binding and activation of the human plasma kinin-forming system on the cell walls of Candida albicans and Candida tropicalis. Biol Chem. 2010; 391: 97-103.
    • (2010) Biol Chem , vol.391 , pp. 97-103
    • Karkowska-Kuleta, J.1    Kozik, A.2    Rapala-Kozik, M.3
  • 192
    • 33750296886 scopus 로고    scopus 로고
    • Cooperative activation of TLR2 and bradykinin B2 receptor is required for induction of type 1 immunity in a mouse model of subcutaneous infection by Trypanosoma cruzi
    • Scharfstein J. Cooperative activation of TLR2 and bradykinin B2 receptor is required for induction of type 1 immunity in a mouse model of subcutaneous infection by Trypanosoma cruzi. J Immunol. 2006; 177: 6325-35.
    • (2006) J Immunol , vol.177 , pp. 6325-6335
    • Scharfstein, J.1
  • 193
    • 0037514586 scopus 로고    scopus 로고
    • Cutting edge: bradykinin induces IL-12 production by dendritic cells: a danger signal that drives TH1 polarization
    • Aliberti J, Viola JP, Vieira-de-Abreu A, Bozza PT, Sher A, Scharfstein J. Cutting edge: bradykinin induces IL-12 production by dendritic cells: a danger signal that drives TH1 polarization. J Immunol. 2003; 170: 5349-53.
    • (2003) J Immunol , vol.170 , pp. 5349-5353
    • Aliberti, J.1    Viola, J.P.2    Vieira-de-Abreu, A.3    Bozza, P.T.4    Sher, A.5    Scharfstein, J.6
  • 195
    • 77649221516 scopus 로고    scopus 로고
    • Cross-talk between bradykinin and epidermal growth factor in regulating IL-6 production in human airway smooth muscle cells
    • Feng PH, Hsiung TC, Kuo HP, Huang CD. Cross-talk between bradykinin and epidermal growth factor in regulating IL-6 production in human airway smooth muscle cells. Chang Gung Med J. 2010; 33: 92-9.
    • (2010) Chang Gung Med J , vol.33 , pp. 92-99
    • Feng, P.H.1    Hsiung, T.C.2    Kuo, H.P.3    Huang, C.D.4
  • 197
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann S, Hammerschmidt S. Fibrinolysis and host response in bacterial infections. Thromb Haemost. 2007; 98: 512-20.
    • (2007) Thromb Haemost , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 198
    • 1842536362 scopus 로고    scopus 로고
    • Salivary secretory leukocyte protease inhibitor and oral candidiasis in human immunodeficiency virus type 1-infected persons
    • Chattopadhyay A, Gray LR, Patton LL, Caplan DJ, Slade GD, Tien HC, Shugars DC. Salivary secretory leukocyte protease inhibitor and oral candidiasis in human immunodeficiency virus type 1-infected persons. Infect Immun. 2004; 72: 1956-63.
    • (2004) Infect Immun , vol.72 , pp. 1956-1963
    • Chattopadhyay, A.1    Gray, L.R.2    Patton, L.L.3    Caplan, D.J.4    Slade, G.D.5    Tien, H.C.6    Shugars, D.C.7
  • 199
    • 0034467924 scopus 로고    scopus 로고
    • The proteolytic activity of the recombinant cryptic human fibronectin type IV collagenase from E. coli expression
    • Schnepel J, Tschesche H. The proteolytic activity of the recombinant cryptic human fibronectin type IV collagenase from E. coli expression. J Prot Chem. 2000; 19: 685-92.
    • (2000) J Prot Chem , vol.19 , pp. 685-692
    • Schnepel, J.1    Tschesche, H.2
  • 200
    • 58249085290 scopus 로고    scopus 로고
    • Should we target allergen protease activity to decrease the burden of allergic airway inflammation?
    • Vliagoftis H, Forsythe P. Should we target allergen protease activity to decrease the burden of allergic airway inflammation? Inflamm Allergy Drug Targets. 2008; 7: 288-95.
    • (2008) Inflamm Allergy Drug Targets , vol.7 , pp. 288-295
    • Vliagoftis, H.1    Forsythe, P.2
  • 201
    • 69449086811 scopus 로고    scopus 로고
    • Characterization and identification of proteases secreted by Aspergillus fumigatus using free flow electrophoresis and MS
    • Neustadt M, Costina V, Kupfahl C, Buchheidt D, Eckerskorn C, Neumaier M, Findeisen P. Characterization and identification of proteases secreted by Aspergillus fumigatus using free flow electrophoresis and MS. Electrophoresis. 2009; 30: 2142-50.
    • (2009) Electrophoresis , vol.30 , pp. 2142-2150
    • Neustadt, M.1    Costina, V.2    Kupfahl, C.3    Buchheidt, D.4    Eckerskorn, C.5    Neumaier, M.6    Findeisen, P.7
  • 202
    • 35148890727 scopus 로고    scopus 로고
    • Systematic identification of substrates for profiling of secreted proteases from Aspergillus species
    • Schaal R, Kupfahl C, Buchheidt D, Neumaier M, Findeisen P. Systematic identification of substrates for profiling of secreted proteases from Aspergillus species. J Microbiol Methods. 2007; 71: 93-100.
    • (2007) J Microbiol Methods , vol.71 , pp. 93-100
    • Schaal, R.1    Kupfahl, C.2    Buchheidt, D.3    Neumaier, M.4    Findeisen, P.5
  • 203
    • 33846167705 scopus 로고    scopus 로고
    • Activity based probes for proteases: application to biomarker discovery, molecular imaging and drug screening
    • Fonović M, Bogyo M. Activity based probes for proteases: application to biomarker discovery, molecular imaging and drug screening. Curr Pharm Des. 2007; 13: 253-61.
    • (2007) Curr Pharm Des , vol.13 , pp. 253-261
    • Fonović, M.1    Bogyo, M.2
  • 205
    • 65549158784 scopus 로고    scopus 로고
    • Purification and identification of proteolytic enzymes from Aspergillus oryzae capable of producing the antihypertensive peptide Ile-Pro-Pro
    • Gotou T, Shinoda T, Mizuno S, Yamamoto M. Purification and identification of proteolytic enzymes from Aspergillus oryzae capable of producing the antihypertensive peptide Ile-Pro-Pro. J Biosci Bioeng. 2009; 107: 615-9.
    • (2009) J Biosci Bioeng , vol.107 , pp. 615-619
    • Gotou, T.1    Shinoda, T.2    Mizuno, S.3    Yamamoto, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.