메뉴 건너뛰기




Volumn 4, Issue 3, 1999, Pages 88-89

Generation of the oxidative burst - Scavenging for the truth [2]

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0033042738     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(99)01385-0     Document Type: Letter
Times cited : (15)

References (15)
  • 1
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: an early plant response to pathogen infection
    • P. Wojtaszek Oxidative burst: an early plant response to pathogen infection Biochem. J. 322 1997 681 692
    • (1997) Biochem. J. , vol.322 , pp. 681-692
    • Wojtaszek, P.1
  • 3
    • 85119541638 scopus 로고    scopus 로고
    • Use and misuse of peroxidase inhibitors
    • A.R. Barceló Use and misuse of peroxidase inhibitors Trends Plant Sci. 3 1998 418
    • (1998) Trends Plant Sci. , vol.3 , pp. 418
    • Barceló, A.R.1
  • 4
    • 0029411960 scopus 로고
    • The origin of the oxidative burst in plants
    • G.P. Bolwell The origin of the oxidative burst in plants Free Rad. Res. 23 1995 517 532
    • (1995) Free Rad. Res. , vol.23 , pp. 517-532
    • Bolwell, G.P.1
  • 5
    • 0031080649 scopus 로고    scopus 로고
    • Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv phaseolicola
    • C.S. Bestwick Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv phaseolicola Plant Cell 9 1997 209 221
    • (1997) Plant Cell , vol.9 , pp. 209-221
    • Bestwick, C.S.1
  • 6
    • 0027189961 scopus 로고
    • The biochemical basis of the NADPH oxidase of phagocytes
    • A. Segal A. Abo The biochemical basis of the NADPH oxidase of phagocytes Trends Biochem. Sci. 18 1993 43 47
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 43-47
    • Segal, A.1    Abo, A.2
  • 7
    • 0030979046 scopus 로고    scopus 로고
    • Reconstitution in vitro of the components and conditions required for the oxidative cross-linking of extracellular proteins in French bean (Phaseolus vulgaris L.)
    • P. Wojtaszek Reconstitution in vitro of the components and conditions required for the oxidative cross-linking of extracellular proteins in French bean ( Phaseolus vulgaris L.) FEBS Lett. 405 1997 95 98
    • (1997) FEBS Lett. , vol.405 , pp. 95-98
    • Wojtaszek, P.1
  • 8
    • 0031696590 scopus 로고    scopus 로고
    • Localization of components of the oxidative cross-linking of glycoproteins and of callose synthase in papillae formed during the interaction between non-pathogenic strains of Xanthomonas campestris and French bean mesophyll cells
    • I. Brown Localization of components of the oxidative cross-linking of glycoproteins and of callose synthase in papillae formed during the interaction between non-pathogenic strains of Xanthomonas campestris and French bean mesophyll cells Plant J. 15 1998 333 343
    • (1998) Plant J. , vol.15 , pp. 333-343
    • Brown, I.1
  • 9
    • 0001739265 scopus 로고    scopus 로고
    • Localized changes in peroxidase activity accompany hydrogen peroxide generation during the development of a nonhost hypersensitive reaction in lettuce
    • C.S. Bestwick Localized changes in peroxidase activity accompany hydrogen peroxide generation during the development of a nonhost hypersensitive reaction in lettuce Plant Physiol. 118 1998 1067 1078
    • (1998) Plant Physiol. , vol.118 , pp. 1067-1078
    • Bestwick, C.S.1
  • 10
    • 0000736219 scopus 로고    scopus 로고
    • Comparative biochemistry of the oxidative burst produced by rose and French bean cells reveals two distinct mechanisms
    • G.P. Bolwell Comparative biochemistry of the oxidative burst produced by rose and French bean cells reveals two distinct mechanisms Plant Physiol. 116 1998 1379 1385
    • (1998) Plant Physiol. , vol.116 , pp. 1379-1385
    • Bolwell, G.P.1
  • 11
    • 0032056337 scopus 로고    scopus 로고
    • Inhibition of O2-reducing activity of horseradish peroxidase by diphenyleneiodonium
    • 2-reducing activity of horseradish peroxidase by diphenyleneiodonium Phytochemistry 48 1998 223 227
    • (1998) Phytochemistry , vol.48 , pp. 223-227
    • Frahry, G.1    Schopfer, P.2
  • 12
    • 0025968709 scopus 로고
    • Inhibition of macrophage and endothelial cell nitric oxide synthase by diphenyleneiodonium and its analogs
    • D.J. Stuehr Inhibition of macrophage and endothelial cell nitric oxide synthase by diphenyleneiodonium and its analogs FASEB J. 5 1991 98 103
    • (1991) FASEB J. , vol.5 , pp. 98-103
    • Stuehr, D.J.1
  • 13
    • 0031733550 scopus 로고    scopus 로고
    • Apoplastic peroxidase generates superoxide anions in cells of cotton cotyledons undergoing the hypersensitive reaction to Xanthomonas campestris pv. malvaraceum race 18
    • C. Martinez Apoplastic peroxidase generates superoxide anions in cells of cotton cotyledons undergoing the hypersensitive reaction to Xanthomonas campestris pv. malvaraceum race 18 Mol. Plant–Microbe Interact. 11 1998 1038 1047
    • (1998) Mol. Plant–Microbe Interact. , vol.11 , pp. 1038-1047
    • Martinez, C.1
  • 14
    • 0031874855 scopus 로고    scopus 로고
    • Hydrogen peroxide production by roots and its stimulation by exogenous NADH
    • G. Frahry P. Schopfer Hydrogen peroxide production by roots and its stimulation by exogenous NADH Physiol. Plant. 103 1998 395 404
    • (1998) Physiol. Plant. , vol.103 , pp. 395-404
    • Frahry, G.1    Schopfer, P.2
  • 15
    • 0030824754 scopus 로고    scopus 로고
    • Superoxide generation in extracts from isolated plant cell walls is regulated by fungal signal molecules
    • A. Kiba Superoxide generation in extracts from isolated plant cell walls is regulated by fungal signal molecules Phytopathology 87 1997 846 852
    • (1997) Phytopathology , vol.87 , pp. 846-852
    • Kiba, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.