메뉴 건너뛰기




Volumn 40, Issue 15, 2009, Pages 1777-1784

Physicochemical responses of Pythium porphyrae (Oomycota), the causative organism of red rot disease in Porphyra to acidification

Author keywords

Acid stress; Acid tolerance; Fungicide; Porphyra; Pythium porphyrae; Red rot disease

Indexed keywords

ACIDIFICATION; ADAPTATION; AMINO ACID; DISEASE CONTROL; EUKARYOTE; FUNGAL DISEASE; FUNGICIDE; PH; RED ALGA; TOLERANCE;

EID: 70350158230     PISSN: 1355557X     EISSN: 13652109     Source Type: Journal    
DOI: 10.1111/j.1365-2109.2009.02284.x     Document Type: Article
Times cited : (11)

References (28)
  • 1
    • 0027179674 scopus 로고
    • Survival and growth of Escherichia coli O157:H7 in ground, roasted beef as affected by pH, acidulants, and temperature
    • Abdul-Raouf U.M., Beuchat L.R. Ammar M.S. (1993) Survival and growth of Escherichia coli O157:H7 in ground, roasted beef as affected by pH, acidulants, and temperature. Applied Environmental Microbiology 59, 2364 2368.
    • (1993) Applied Environmental Microbiology , vol.59 , pp. 2364-2368
    • Abdul-Raouf, U.M.1    Beuchat, L.R.2    Ammar, M.S.3
  • 2
    • 51249161878 scopus 로고
    • Immunological detection of the fungal parasite, Pythium sp.; The causative organism of red rot disease in Porphyra yezoensis
    • Amano H., Suginaga R., Arashima K. Noda H. (1995) Immunological detection of the fungal parasite, Pythium sp.; the causative organism of red rot disease in Porphyra yezoensis. Journal of Applied Phycology 7, 53 58.
    • (1995) Journal of Applied Phycology , vol.7 , pp. 53-58
    • Amano, H.1    Suginaga, R.2    Arashima, K.3    Noda, H.4
  • 3
    • 0002636424 scopus 로고
    • Studies on red rot of Porphyra tenera
    • Arasaki S. (1947) Studies on red rot of Porphyra tenera. Nippon Suisan Gakkaishi 13, 74 90.
    • (1947) Nippon Suisan Gakkaishi , vol.13 , pp. 74-90
    • Arasaki, S.1
  • 4
    • 0000282879 scopus 로고
    • A comparison of some physiological aspects in a marine Pythium on the host and on the artificial medium
    • Arasaki S., Akino K. Tomiyama T. (1968) A comparison of some physiological aspects in a marine Pythium on the host and on the artificial medium. Bulletin Misaki Marine Biology Institute Kyoto University 12, 203 206.
    • (1968) Bulletin Misaki Marine Biology Institute Kyoto University , vol.12 , pp. 203-206
    • Arasaki, S.1    Akino, K.2    Tomiyama, T.3
  • 6
    • 0022457545 scopus 로고
    • Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci
    • Bender G.R., Sutton S.V.W. Marquis R.E. (1986) Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci. Infection Immunology 53, 331 338.
    • (1986) Infection Immunology , vol.53 , pp. 331-338
    • Bender, G.R.1    Sutton, S.V.W.2    Marquis, R.E.3
  • 8
    • 0014984448 scopus 로고
    • Effects of temperature and pH on growth and composition of Pythium irregulare and Pythium vexans
    • Cantrell H.F. Dowler W.M. (1971) Effects of temperature and pH on growth and composition of Pythium irregulare and Pythium vexans. Mycologia 63, 31 37.
    • (1971) Mycologia , vol.63 , pp. 31-37
    • Cantrell, H.F.1    Dowler, W.M.2
  • 9
    • 70350188570 scopus 로고
    • Studies on the control of disease and diatoms on laver using mixed solutions of organic acids and trace metals
    • Chung Y.K., Choi J.I. Kim G.J. (1992) Studies on the control of disease and diatoms on laver using mixed solutions of organic acids and trace metals. Bulletin National Fisheries Research and Development Agency 96, 215 226.
    • (1992) Bulletin National Fisheries Research and Development Agency , vol.96 , pp. 215-226
    • Chung, Y.K.1    Choi, J.I.2    Kim, G.J.3
  • 10
    • 0033037702 scopus 로고    scopus 로고
    • The response to stationary phase stress conditions in Escherichia coli: Role and regulation of the glutamic acid decarboxylase system
    • De Biase D., Tramonti A., Bossa F. Visca P. (1999) The response to stationary phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system. Molecular Microbiology 32, 1198 1211.
    • (1999) Molecular Microbiology , vol.32 , pp. 1198-1211
    • De Biase, D.1    Tramonti, A.2    Bossa, F.3    Visca, P.4
  • 11
    • 0025719985 scopus 로고
    • Salmonella acid shock proteins are required for the adaptive acid tolerance response
    • Foster J.W. (1991) Salmonella acid shock proteins are required for the adaptive acid tolerance response. Journal of Bacteriology 173, 6896 6902.
    • (1991) Journal of Bacteriology , vol.173 , pp. 6896-6902
    • Foster, J.W.1
  • 12
    • 0025037611 scopus 로고
    • Adaptive acidification tolerance response of Salmonella typhimurium
    • Foster J.W. Hall H.K. (1990) Adaptive acidification tolerance response of Salmonella typhimurium. Journal of Bacteriology 172, 771 778.
    • (1990) Journal of Bacteriology , vol.172 , pp. 771-778
    • Foster, J.W.1    Hall, H.K.2
  • 13
    • 85008008176 scopus 로고
    • Studies on pathogenic Pythium of laver red rot in Ariake sea Farm-I. General mycological characteristic
    • Fujita Y. Zenitani B. (1976) Studies on pathogenic Pythium of laver red rot in Ariake sea Farm-I. General mycological characteristic. Nippon Suisan Gakkaishi 42, 1183 1188.
    • (1976) Nippon Suisan Gakkaishi , vol.42 , pp. 1183-1188
    • Fujita, Y.1    Zenitani, B.2
  • 14
    • 84996351473 scopus 로고
    • Studies on pathogenic Pythium of laver red rot in Ariake sea farm-II. Experimental conditions and nutritional requirements for growth
    • Fujita Y. Zenitani B. (1977) Studies on pathogenic Pythium of laver red rot in Ariake sea farm-II. Experimental conditions and nutritional requirements for growth. Nippon Suisan Gakkaishi 43, 89 95.
    • (1977) Nippon Suisan Gakkaishi , vol.43 , pp. 89-95
    • Fujita, Y.1    Zenitani, B.2
  • 15
    • 0002116418 scopus 로고
    • The bacterial amino acid decarboxylases
    • Gale E.F. (1946) The bacterial amino acid decarboxylases. Advanced Enzymology 6, 1 2.
    • (1946) Advanced Enzymology , vol.6 , pp. 1-2
    • Gale, E.F.1
  • 18
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by two-dimentional gel electrophoresis
    • Hurkman W.J. Tanaka C.K. (1986) Solubilization of plant membrane proteins for analysis by two-dimentional gel electrophoresis. Plant Physiology 81, 802 806.
    • (1986) Plant Physiology , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 19
    • 0033014685 scopus 로고    scopus 로고
    • Survival of low-pH stress by Escherichia coli O157:H7: Correlation between alterations in the cell envelope and increased acid tolerance
    • Jordan K.N., Oxford L. O'Byrne C.B. (1999) Survival of low-pH stress by Escherichia coli O157:H7: correlation between alterations in the cell envelope and increased acid tolerance. Applied Environmental Microbiology 65, 3048 3055.
    • (1999) Applied Environmental Microbiology , vol.65 , pp. 3048-3055
    • Jordan, K.N.1    Oxford, L.2    O'Byrne, C.B.3
  • 20
    • 0005906225 scopus 로고
    • Mineral nutrition of Pythium marinum, a marine facultative parasite
    • Kazama F.Y. Fuller M.S. (1973) Mineral nutrition of Pythium marinum, a marine facultative parasite. Canadian Journal Botany 51, 693 699.
    • (1973) Canadian Journal Botany , vol.51 , pp. 693-699
    • Kazama, F.Y.1    Fuller, M.S.2
  • 22
    • 0015833084 scopus 로고
    • Acid-base titration of streptocooci and physical states of intracelluar ions
    • Marquis R.E., Porterfield N. Matsumura P. (1973) Acid-base titration of streptocooci and physical states of intracelluar ions. Journal of Bacteriology 114, 491 498.
    • (1973) Journal of Bacteriology , vol.114 , pp. 491-498
    • Marquis, R.E.1    Porterfield, N.2    Matsumura, P.3
  • 23
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. Journal of Biological Chemistry 262, 10035 10038.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 24
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. (1975) High resolution two-dimensional electrophoresis of proteins. Journal of Biological Chemistry 250, 4007 4021.
    • (1975) Journal of Biological Chemistry , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 25
    • 0003287466 scopus 로고    scopus 로고
    • Comparison of the morphological and physiological features of the red rot disease fungus Pythium sp., isolated from Porphyra yezoensis from Korea and Japan
    • Park C.S., Sakaguchi M., Kakinuma M. Amano H. (2000) Comparison of the morphological and physiological features of the red rot disease fungus Pythium sp., isolated from Porphyra yezoensis from Korea and Japan. Fisheries Science 66, 261 269.
    • (2000) Fisheries Science , vol.66 , pp. 261-269
    • Park, C.S.1    Sakaguchi, M.2    Kakinuma, M.3    Amano, H.4
  • 26
    • 0013866506 scopus 로고
    • Membrane properties of living mammalian cells as studied by enzymatic hydrolysis of fluorogenic esters
    • Rotma B. Papermaster B.W. (1966) Membrane properties of living mammalian cells as studied by enzymatic hydrolysis of fluorogenic esters. Biochemistry 55, 134 141.
    • (1966) Biochemistry , vol.55 , pp. 134-141
    • Rotma, B.1    Papermaster, B.W.2
  • 27
    • 0000194337 scopus 로고
    • Composition of medium and cultural temperature of Pythium sp., a pathogenic fungus, of the 'Akagusare' disease of cultivated Porphyra
    • Sasaki M. Sato S. (1969) Composition of medium and cultural temperature of Pythium sp., a pathogenic fungus, of the 'Akagusare' disease of cultivated Porphyra. Bulletin Tohoku Regional National Fisheries Research Institute 29, 125 132.
    • (1969) Bulletin Tohoku Regional National Fisheries Research Institute , vol.29 , pp. 125-132
    • Sasaki, M.1    Sato, S.2
  • 28
    • 0026641173 scopus 로고
    • Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci
    • Smith D.K., Kassam T., Singh B. Elliott J.F. (1992) Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci. Journal of Bacteriology 174, 5820 5826.
    • (1992) Journal of Bacteriology , vol.174 , pp. 5820-5826
    • Smith, D.K.1    Kassam, T.2    Singh, B.3    Elliott, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.