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Volumn 54, Issue 2, 2009, Pages 105-109

PepJ is a new extracellular proteinase of Aspergillus nidulans

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; METALLOPROTEINASE;

EID: 65649126844     PISSN: 00155632     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12223-009-0015-8     Document Type: Article
Times cited : (14)

References (22)
  • 1
    • 0013789861 scopus 로고
    • Wild-type and mutant stocks of Aspergillus nidulans
    • R.W. Barratt G.B. Johnson W.N. Ogata 1965 Wild-type and mutant stocks of Aspergillus nidulans Genetics 52 233 246
    • (1965) Genetics , vol.52 , pp. 233-246
    • Barratt, R.W.1    Johnson, G.B.2    Ogata, W.N.3
  • 2
    • 17844381320 scopus 로고    scopus 로고
    • Production and purification of extracellular chitinases from Penicillium aculeatum NRRL 2129 under solid-state fermentation
    • DOI 10.1016/j.enzmictec.2004.12.031
    • P. Binod T. Pusztahelyi V. Nagy C. Sandhya G. Szakacs I. Pócsi A. Pandey 2005 Production and purification of extracellular chitinases from Penicillium aculeatum NRRL 2129 under solid-state fermentation Enzyme Microb.Technol. 36 880 887 (Pubitemid 40591704)
    • (2005) Enzyme and Microbial Technology , vol.36 , Issue.7 , pp. 880-887
    • Binod, P.1    Pusztahelyi, T.2    Nagy, V.3    Sandhya, C.4    Szakacs, G.5    Pocsi, I.6    Pandey, A.7
  • 6
    • 0034537067 scopus 로고    scopus 로고
    • The Aspergillus nidulans xprF gene encodes a hexokinase-like protein involved in the regulation of extracellular proteases
    • M.E. Katz A. Masoumi S.R. Burrows C.G. Shirtliff B.F. Cheetham 2000 The Aspergillus nidulans xprF gene encodes a hexokinase-like protein involved in the regulation of extracellular proteases Genetics 156 1559 1571 (Pubitemid 32001225)
    • (2000) Genetics , vol.156 , Issue.4 , pp. 1559-1571
    • Katz, M.E.1    Masomi, A.2    Burrows, S.R.3    Shirtliff, C.G.4    Cheetham, B.F.5
  • 7
    • 33644828993 scopus 로고    scopus 로고
    • The Aspergillus nidulans xprG (phoG) gene encodes a putative transcriptional activator involved in the response to nutrient limitation
    • DOI 10.1016/j.fgb.2005.12.001, PII S1087184505001799
    • M.E. Katz K.A. Gray B.F. Cheetham 2006 The Aspergillus nidulans xprG (phoG) gene encodes a putative transcriptional activator involved in the response to nutrient limitation Fungal Genet.Biol. 43 190 199 (Pubitemid 43357969)
    • (2006) Fungal Genetics and Biology , vol.43 , Issue.3 , pp. 190-199
    • Katz, M.E.1    Gray, K.-A.2    Cheetham, B.F.3
  • 8
    • 47249132823 scopus 로고    scopus 로고
    • The interaction of induction, repression and starvation in the regulation of extracellular proteases in Aspergillus nidulans: Evidence for a role for CreA in the response to carbon starvation
    • M.E. Katz S.M. Bernardo B.F. Cheetham 2008 The interaction of induction, repression and starvation in the regulation of extracellular proteases in Aspergillus nidulans: evidence for a role for CreA in the response to carbon starvation Curr.Genet. 54 47 55
    • (2008) Curr.Genet. , vol.54 , pp. 47-55
    • Katz, M.E.1    Bernardo, S.M.2    Cheetham, B.F.3
  • 9
    • 0033854144 scopus 로고    scopus 로고
    • Analysis of two aspergillus nidulans genes encoding extracellular proteases
    • DOI 10.1006/fgbi.2000.1195
    • P.A. vanKuyk B.F. Cheetham M.E. Katz 2000 Analysis of two Aspergillus nidulans genes encoding extracellular proteases Fungal Genet.Biol. 29 201 210 (Pubitemid 30601396)
    • (2000) Fungal Genetics and Biology , vol.29 , Issue.3 , pp. 201-210
    • Vankuyk, P.A.1    Cheetham, B.F.2    Katz, M.E.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0023517606 scopus 로고
    • Identification of multiple glutathione S-transferases from Daphnia magna
    • G.A. LeBlanc B.J. Cochrane 1987 Identification of multiple glutathione S-transferases from Daphnia magna Comp.Biochem.Physiol. 88B 39 45
    • (1987) Comp.Biochem.Physiol. , vol.88 B , pp. 39-45
    • Leblanc, G.A.1    Cochrane, B.J.2
  • 12
    • 0027931263 scopus 로고
    • Molecular cloning and nucleotide sequence of the complementary DNA for penicillolysin gene, plnC, an 18kDa metalloendopeptidase gene from Penicillium citrinum
    • DOI 10.1016/0167-4781(94)90209-7
    • K. Matsumoto M. Yamaguchi E. Ichishima 1994 Molecular cloning and nucleotide sequence of the complementary DNA for penicillolysin gene, plnC, and 18 kDa metalloendopeptidase gene from Penicillium citrinum Biochim.Biophys.Acta 1218 469 472 (Pubitemid 124009537)
    • (1994) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1218 , Issue.3 , pp. 469-472
    • Matsumoto, K.1    Yamaguchi, M.2    Ichishima, E.3
  • 13
    • 0037428329 scopus 로고    scopus 로고
    • Microcystin-LR alters the growth, anthocyanin content and single-stranded DNase enzyme activities in Sinapis alba L. seedlings
    • DOI 10.1016/S0166-445X(01)00273-9, PII S0166445X01002739
    • M. M-Hamvas Cs. Máth E. Molnár G. Vasas I. Grigorszky Gy. Borbély 2003 Microcystin-LR alters the growth, anthocyanin content and single-stranded DNase enzyme activities in Sinapis alba L. seedlings Aquat.Toxicol. 62 1 9 (Pubitemid 36159005)
    • (2003) Aquatic Toxicology , vol.62 , Issue.1 , pp. 1-9
    • M-Hamvas, M.1    Mathe, C.2    Molnar, E.3    Vasas, G.4    Grigorszky, I.5    Borbely, G.6
  • 14
    • 33845636634 scopus 로고    scopus 로고
    • Effects of mutations in the GanB/RgsA G protein mediated signaling on the autolysis of Aspergillus nidulans
    • Zs. Molnár T. Emri E. Zavaczki T. Pusztehelyi I. Pócsi 2006 Effects of mutations in the GanB/RgsA G protein mediated signaling on the autolysis of Aspergillus nidulans J.Basic Microbiol. 46 495 603
    • (2006) J.Basic Microbiol. , vol.46 , pp. 495-603
    • Molnár, Zs.1    Emri, T.2    Zavaczki, E.3    Pusztehelyi, T.4    Pócsi, I.5
  • 15
    • 40549101853 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans
    • C. Peña-Montes A. González D. Castro-Ochoa A. Farrés 2008 Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans Appl.Microbiol.Biotechnol. 78 603 612
    • (2008) Appl.Microbiol.Biotechnol. , vol.78 , pp. 603-612
    • Peña-Montes, C.1    González, A.2    Castro-Ochoa, D.3    Farrés, A.4
  • 16
    • 33847216229 scopus 로고    scopus 로고
    • Comparative studies of differential expression of chitinolytic enzymes encoded by chiA, chiB, chiC and nagA genes in Aspergillus nidulans
    • T. Pusztahelyi Zs. Molnár T. Emri Klement M. Miskei J. Kerékgyártó J. Balla I. Pócsi 2006 Comparative studies on differential expression of chitinolytic enzymes encoded by chiA, chiB, chiC and nagA genes in Aspergillus nidulans Folia Microbiol. 51 547 554 (Pubitemid 46304629)
    • (2006) Folia Microbiologica , vol.51 , Issue.6 , pp. 547-554
    • Pusztahelyi, T.1    Molnar, Z.2    Emri, T.3    Klement, E.4    Miskei, M.5    Kerekgyarto, J.6    Balla, J.7    Pocsi, I.8
  • 17
    • 65649095071 scopus 로고    scopus 로고
    • An introduction to peptidases and the MEROPS database
    • J. Polonia, A.P. MacCabe (Eds) Springer
    • Rawlings N.D., Morton F.R., Barrett A.J.: An introduction to peptidases and the MEROPS database, pp. 161-179 in J. Polonia, A.P. MacCabe (Eds): Industrial Enzymes. Springer 2007.
    • (2007) Industrial Enzymes , pp. 161-179
    • Rawlings, N.D.1    Morton, F.R.2    Barrett, A.J.3
  • 18
    • 0033883450 scopus 로고    scopus 로고
    • Comparison of globulin mobilization and cysteine proteinases in embryonic axes and cotyledons during germination and seedling growth of vetch (Vicia sativa L.)
    • A. Schlereth C. Becker C. Horstmann J. Tiedemann K. Müntz 2000 Comparison of globulin mobilization and cysteine proteinases in embryogenic axes and cotyledons during germination and seedling growth of vetch (Vicia sativa L.) J.Exp.Bot. 51 1423 1433 (Pubitemid 30627058)
    • (2000) Journal of Experimental Botany , vol.51 , Issue.349 , pp. 1423-1433
    • Schlereth, A.1    Becker, C.2    Horstmann, C.3    Tiedemann, J.4    Muntz, K.5
  • 19
    • 0004500831 scopus 로고
    • Neutral proteinases i and II of Aspergillus sojae
    • H. Sekine 1972 Neutral proteinases I and II of Aspergillus sojae Agric.Biol.Chem. 36 2143 2150
    • (1972) Agric.Biol.Chem. , vol.36 , pp. 2143-2150
    • Sekine, H.1
  • 21
    • 78651007343 scopus 로고
    • The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity
    • R.M. Tomarelli J. Charney M.L. Harding 1949 The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity J.Lab.Clin.Med. 34 428 433
    • (1949) J.Lab.Clin.Med. , vol.34 , pp. 428-433
    • Tomarelli, R.M.1    Charney, J.2    Harding, M.L.3
  • 22
    • 0027651593 scopus 로고
    • Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum
    • M. Yamaguchi S. Hanzawa K. Hirano Y. Yamagata E. Ichishima 1993 Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum Phytochemistry 33 1317 1321
    • (1993) Phytochemistry , vol.33 , pp. 1317-1321
    • Yamaguchi, M.1    Hanzawa, S.2    Hirano, K.3    Yamagata, Y.4    Ichishima, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.