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Volumn 131, Issue 4, 2007, Pages 519-526

Characterization of cysteine protease induced by oxidative stress in cells of Chlamydomonas sp. strain W80

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; METABOLISM; MOLECULAR WEIGHT; OXIDATIVE STRESS; PEPTIDES;

EID: 35948956360     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2007.00981.x     Document Type: Article
Times cited : (20)

References (28)
  • 1
    • 0001656899 scopus 로고
    • Changes in the level of peptidase activities in pea ovaries during senescence and fruit set induced by gibberellic acid
    • Carrasco P, Cabonell J (1990) Changes in the level of peptidase activities in pea ovaries during senescence and fruit set induced by gibberellic acid. Plant Physiol 92: 1070 1074
    • (1990) Plant Physiol , vol.92 , pp. 1070-1074
    • Carrasco, P.1    Cabonell, J.2
  • 2
    • 0030912124 scopus 로고    scopus 로고
    • New bile pigment excreted by a Chlamydomonas reinhardtii mutant: A possible breakdown catabolite of chlorophyll a
    • Doi M, Shima S, Egashira T, Nakamura K, Okayama S (1997) New bile pigment excreted by a Chlamydomonas reinhardtii mutant: a possible breakdown catabolite of chlorophyll a. J Plant Physiol 150: 504 508
    • (1997) J Plant Physiol , vol.150 , pp. 504-508
    • Doi, M.1    Shima, S.2    Egashira, T.3    Nakamura, K.4    Okayama, S.5
  • 3
    • 35948992852 scopus 로고    scopus 로고
    • Cadmium response and redoxin targets in Chlamydomonas reinhardtii: A proteomic approach
    • Gillet S, Decottignies P, Chardonnet S, Maréchal PL (2006) Cadmium response and redoxin targets in Chlamydomonas reinhardtii: a proteomic approach. Photosyn Res 89: 201 211
    • (2006) Photosyn Res , vol.89 , pp. 201-211
    • Gillet, S.1    Decottignies, P.2    Chardonnet, S.3    Maréchal, P.L.4
  • 4
    • 0029959103 scopus 로고    scopus 로고
    • Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato
    • Gu YQ, Chao WS, Walling LL (1996) Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato. J Biol Chem 271: 25880 25887
    • (1996) J Biol Chem , vol.271 , pp. 25880-25887
    • Gu, Y.Q.1    Chao, W.S.2    Walling, L.L.3
  • 5
    • 19344365162 scopus 로고    scopus 로고
    • One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp
    • Gupta A, Roy I, Patel RK, Singh SP, Khare SK, Gupta MN (2005) One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp. J Chromatogr A1075: 103 108
    • (2005) J Chromatogr , vol.1075 , pp. 103-108
    • Gupta, A.1    Roy, I.2    Patel, R.K.3    Singh, S.P.4    Khare, S.K.5    Gupta, M.N.6
  • 6
    • 0001404343 scopus 로고
    • Purification and characterization of a membrane-bound protease from Chlamydomonas reinhardtii
    • Hoober JK, Hughes MJ (1992) Purification and characterization of a membrane-bound protease from Chlamydomonas reinhardtii. Plant Physiol 99: 932 937
    • (1992) Plant Physiol , vol.99 , pp. 932-937
    • Hoober, J.K.1    Hughes, M.J.2
  • 7
    • 0034149897 scopus 로고    scopus 로고
    • Effects of Tween 60 and Tween 80 on protease activity, thiol group reactivity, protein adsorption, and cellulose degradation by rumen microbial enzymes
    • Kamande GM, Baah J, Cheng K-J, McAllister TA, Shelford JA (2000) Effects of Tween 60 and Tween 80 on protease activity, thiol group reactivity, protein adsorption, and cellulose degradation by rumen microbial enzymes. J Dairy Sci 83: 536 542
    • (2000) J Dairy Sci , vol.83 , pp. 536-542
    • Kamande, G.M.1    Baah, J.2    Cheng, K.-J.3    McAllister, T.A.4    Shelford, J.A.5
  • 9
    • 0027274695 scopus 로고
    • Structure and expression of two genes that encode distinct drought-inducible cysteine proteases in Arabidopsis thaliana
    • Koizumi M, Yamaguchi-Shinozaki K, Tsuji K, Shinozaki K (1993) Structure and expression of two genes that encode distinct drought-inducible cysteine proteases in Arabidopsis thaliana. Gene 129: 175 182
    • (1993) Gene , vol.129 , pp. 175-182
    • Koizumi, M.1    Yamaguchi-Shinozaki, K.2    Tsuji, K.3    Shinozaki, K.4
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 12
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • Mackinney G (1941) Absorption of light by chlorophyll solutions. J Biol Chem 140: 315 322
    • (1941) J Biol Chem , vol.140 , pp. 315-322
    • MacKinney, G.1
  • 14
    • 0001360267 scopus 로고
    • Isolation and characterization of a unicellular marine green alga exhibiting high activity in dark hydrogen production
    • Miura Y, Ohta S, Mano M, Miyamoto K (1986) Isolation and characterization of a unicellular marine green alga exhibiting high activity in dark hydrogen production. Agric Biol Chem 50: 2837 2844
    • (1986) Agric Biol Chem , vol.50 , pp. 2837-2844
    • Miura, Y.1    Ohta, S.2    Mano, M.3    Miyamoto, K.4
  • 16
    • 0034098640 scopus 로고    scopus 로고
    • Isolation of several anti-stress genes from the halotolerant green alga Chlamydomonas by simple functional expression screening with Escherichia coli
    • Miyasaka H, Kanaboshi H, Ikeda K (2000) Isolation of several anti-stress genes from the halotolerant green alga Chlamydomonas by simple functional expression screening with Escherichia coli. World J Microbiol Biotechnol 16: 23 29
    • (2000) World J Microbiol Biotechnol , vol.16 , pp. 23-29
    • Miyasaka, H.1    Kanaboshi, H.2    Ikeda, K.3
  • 17
    • 0000577688 scopus 로고
    • Mechanisms of action of herbicides
    • Moreland DE (1980) Mechanisms of action of herbicides. Annu Rev Plant Physiol 31: 597 638
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 597-638
    • Moreland, D.E.1
  • 18
    • 12744268546 scopus 로고    scopus 로고
    • Leucine aminopeptidase from etiolated barley seedlings: Characterization and partial purification of isoforms
    • Ogiwara N, Amano T, Satoh M, Shioi Y (2005) Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms. Plant Sci 168: 575 581
    • (2005) Plant Sci , vol.168 , pp. 575-581
    • Ogiwara, N.1    Amano, T.2    Satoh, M.3    Shioi, Y.4
  • 19
    • 0027490705 scopus 로고
    • Leucine aminopeptidase: An inducible component of the defense response in Lycopersicon esculentum (tomato)
    • Pautot V, Holzer FM, Reisch B, Walling LL (1993) Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato). Proc Natl Acad Sci U S A 90: 9906 9910
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 9906-9910
    • Pautot, V.1    Holzer, F.M.2    Reisch, B.3    Walling, L.L.4
  • 20
    • 0033679681 scopus 로고    scopus 로고
    • Chloroplasts of the green alga Chlamydomonas reinhardtii possess at least four distinct stromal processing proteases
    • Rüfenacht A, Boschetti A (2000) Chloroplasts of the green alga Chlamydomonas reinhardtii possess at least four distinct stromal processing proteases. Photosyn Res 63: 249 258
    • (2000) Photosyn Res , vol.63 , pp. 249-258
    • Rüfenacht, A.1    Boschetti, A.2
  • 21
    • 0001540727 scopus 로고
    • Analysis of mRNAs that accumulate in response to low temperature identifies a thiol protease gene in tomato
    • Schaffer MA, Fisher RL (1988) Analysis of mRNAs that accumulate in response to low temperature identifies a thiol protease gene in tomato. Plant Physiol 87: 431 436
    • (1988) Plant Physiol , vol.87 , pp. 431-436
    • Schaffer, M.A.1    Fisher, R.L.2
  • 22
    • 34247884580 scopus 로고    scopus 로고
    • A novel gene with antisalt and anticadmium stress activities from a halotolerant marine green alga Chlamydomonas sp. W80
    • Tanaka S, Suda Y, Ikeda K, Ono M, Miyasaka H, Watanabe M, Sasaki K, Hirata K (2007) A novel gene with antisalt and anticadmium stress activities from a halotolerant marine green alga Chlamydomonas sp. W80. FEMS Microbiol Lett 271: 48 52
    • (2007) FEMS Microbiol Lett , vol.271 , pp. 48-52
    • Tanaka, S.1    Suda, Y.2    Ikeda, K.3    Ono, M.4    Miyasaka, H.5    Watanabe, M.6    Sasaki, K.7    Hirata, K.8
  • 23
    • 1842677796 scopus 로고
    • Multiple forms of aminopeptidase in Euonymus leaves
    • Tazaki K, Ishikura N (1983) Multiple forms of aminopeptidase in Euonymus leaves. Plant Cell Physiol 24: 1263 1268
    • (1983) Plant Cell Physiol , vol.24 , pp. 1263-1268
    • Tazaki, K.1    Ishikura, N.2
  • 25
    • 0037316022 scopus 로고    scopus 로고
    • Cadmium-dependent generation of reactive oxygen species and mitochondrial DNA breaks in photosynthetic and non-photosynthetic strains of Euglena gracilis
    • Watanabe M, Henmi K, Ogawa K, Suzuki T (2003) Cadmium-dependent generation of reactive oxygen species and mitochondrial DNA breaks in photosynthetic and non-photosynthetic strains of Euglena gracilis. Comp Biochem Physiol C Toxicol Pharmacol 134: 227 234
    • (2003) Comp Biochem Physiol C Toxicol Pharmacol , vol.134 , pp. 227-234
    • Watanabe, M.1    Henmi, K.2    Ogawa, K.3    Suzuki, T.4
  • 26
    • 0031945147 scopus 로고    scopus 로고
    • Role of proline accumulation in response to toxic copper in Chlorella sp. (Chlorophyceae) cells
    • Wu J-T, Hsieh M-T, Kow L-C (1998) Role of proline accumulation in response to toxic copper in Chlorella sp. (Chlorophyceae) cells. J Phycol 34: 113 117
    • (1998) J Phycol , vol.34 , pp. 113-117
    • Wu, J.-T.1    Hsieh, M.-T.2    Kow, L.-C.3
  • 28
    • 0034924125 scopus 로고    scopus 로고
    • Isolation of the protease component of maize cysteine protease-cystatin complex: Release of cystatin is not crucial for the activation of the cysteine protease
    • Yamada T, Kondo A, Ohta H, Masuda T, Shimada H, Takamiya K (2001) Isolation of the protease component of maize cysteine protease-cystatin complex: release of cystatin is not crucial for the activation of the cysteine protease. Plant Cell Physiol 42: 710 716
    • (2001) Plant Cell Physiol , vol.42 , pp. 710-716
    • Yamada, T.1    Kondo, A.2    Ohta, H.3    Masuda, T.4    Shimada, H.5    Takamiya, K.6


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