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Volumn 75, Issue 3, 2011, Pages 90-99

Proteomic analysis of grapevine stem in response to Xylella fastidiosa inoculation

Author keywords

Grapevine; Mass spectrometry; Pierce's disease; Proteins; Resistance; Susceptible; Two dimensional gel electrophoresis

Indexed keywords

BACTERIA (MICROORGANISMS); VITACEAE; VITIS; VITIS ARIZONICA; VITIS RUPESTRIS; XYLELLA FASTIDIOSA;

EID: 79151475543     PISSN: 08855765     EISSN: 10961178     Source Type: Journal    
DOI: 10.1016/j.pmpp.2010.11.002     Document Type: Article
Times cited : (43)

References (82)
  • 1
    • 0036792413 scopus 로고    scopus 로고
    • Xylella fastidiosa: cause of Pierce's disease of grapevine and other emergent diseases
    • Hopkins D.L., Purcell A.H. Xylella fastidiosa: cause of Pierce's disease of grapevine and other emergent diseases. Plant Dis 2002, 86:1056-1066.
    • (2002) Plant Dis , vol.86 , pp. 1056-1066
    • Hopkins, D.L.1    Purcell, A.H.2
  • 3
    • 0348096277 scopus 로고
    • Origin and significance of Florida hybrid bunch grapes and rootstocks
    • Halbrooks M.C., Mortensen J.A. Origin and significance of Florida hybrid bunch grapes and rootstocks. HortScience 1989, 24:546-550.
    • (1989) HortScience , vol.24 , pp. 546-550
    • Halbrooks, M.C.1    Mortensen, J.A.2
  • 4
    • 33645386128 scopus 로고    scopus 로고
    • Identification and molecular mapping of PdR1, a primary resistance gene to Pierce's disease in Vitis
    • Krivanek A.F., Riaz S., Walker M.A. Identification and molecular mapping of PdR1, a primary resistance gene to Pierce's disease in Vitis. Theor Appl Genet 2006, 112:1125-1131.
    • (2006) Theor Appl Genet , vol.112 , pp. 1125-1131
    • Krivanek, A.F.1    Riaz, S.2    Walker, M.A.3
  • 5
    • 33750173828 scopus 로고    scopus 로고
    • Refined mapping of the Pierce's disease resistance locus, PdR1 and Sex on an extended genetic map of Vitis rupestris × Vitis arizonica
    • Riaz S., Krivanek A.F., Xu K., Walker M.A. Refined mapping of the Pierce's disease resistance locus, PdR1 and Sex on an extended genetic map of Vitis rupestris × Vitis arizonica. Theor Appl Genet 2006, 113:1317-1329.
    • (2006) Theor Appl Genet , vol.113 , pp. 1317-1329
    • Riaz, S.1    Krivanek, A.F.2    Xu, K.3    Walker, M.A.4
  • 6
    • 50249167664 scopus 로고    scopus 로고
    • Fine-scale genetic mapping of two Pierce's disease resistance loci and a major segregation distortion region on chromosome 14 of grape
    • Riaz S., Tenscher A.C., Rubin J., Graziani R., Pao S.S., Walker M.A. Fine-scale genetic mapping of two Pierce's disease resistance loci and a major segregation distortion region on chromosome 14 of grape. Theor Appl Genet 2008, 117:671-681.
    • (2008) Theor Appl Genet , vol.117 , pp. 671-681
    • Riaz, S.1    Tenscher, A.C.2    Rubin, J.3    Graziani, R.4    Pao, S.S.5    Walker, M.A.6
  • 7
    • 79151472539 scopus 로고    scopus 로고
    • Identification and functional annotation of unique EST sequences between Vitis shuttleworthii and V. vinifera grapes. Plant & Animal Genomes XIV Conference. p18, San Diego, CA, January 14-18.
    • Lu J, Huang H, Bradeley F, Huanter W, Dang P. Identification and functional annotation of unique EST sequences between Vitis shuttleworthii and V. vinifera grapes. Plant & Animal Genomes XIV Conference. p18, San Diego, CA, 2006. January 14-18.
    • (2006)
    • Lu, J.1    Huang, H.2    Bradeley, F.3    Huanter, W.4    Dang, P.5
  • 8
    • 33947220315 scopus 로고    scopus 로고
    • Comparative analysis of ESTs involved in grape responses to Xylella fastidiosa infection
    • Lin H., Doddapaneni H., Takahashi Y., Walker M.A. Comparative analysis of ESTs involved in grape responses to Xylella fastidiosa infection. BMC Plant Biol 2007, 7:8.
    • (2007) BMC Plant Biol , vol.7 , pp. 8
    • Lin, H.1    Doddapaneni, H.2    Takahashi, Y.3    Walker, M.A.4
  • 9
    • 41249098849 scopus 로고    scopus 로고
    • A high quality draft consensus sequence of the genome of a heterozygous grapevine variety
    • Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D., et al. A high quality draft consensus sequence of the genome of a heterozygous grapevine variety. PLoS ONE 2007, 2:e1326.
    • (2007) PLoS ONE , vol.2
    • Velasco, R.1    Zharkikh, A.2    Troggio, M.3    Cartwright, D.A.4    Cestaro, A.5    Pruss, D.6
  • 11
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L., Seilhamer J. A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 1997, 18:533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 12
    • 37249020912 scopus 로고    scopus 로고
    • The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream of group C mitogen-activated protein kinases and participates in pathogen signaling
    • Dóczi R., Brader G., Pettkó-Szandtner A., Rajh I., Djamei A., Pitzschke A., et al. The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream of group C mitogen-activated protein kinases and participates in pathogen signaling. Plant Cell 2007, 19:3266-3279.
    • (2007) Plant Cell , vol.19 , pp. 3266-3279
    • Dóczi, R.1    Brader, G.2    Pettkó-Szandtner, A.3    Rajh, I.4    Djamei, A.5    Pitzschke, A.6
  • 13
    • 33750117539 scopus 로고    scopus 로고
    • Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging
    • Jones A.M., Bennett M.H., Mansfield J.W., Grant M. Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging. Proteomics 2006, 6:4155-4165.
    • (2006) Proteomics , vol.6 , pp. 4155-4165
    • Jones, A.M.1    Bennett, M.H.2    Mansfield, J.W.3    Grant, M.4
  • 15
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the Ubiquitin-Proteasome pathway in normal and disease states
    • Lecker S.H., Goldberg A.L., Mitch W.E. Protein degradation by the Ubiquitin-Proteasome pathway in normal and disease states. Am Soc Nephrol 2006, 17:1807-1819.
    • (2006) Am Soc Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 16
    • 33846378524 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis
    • Xiong Y., Contento A.L., Nguyen P.Q., Bassham D.C. Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis. Plant Phys 2007, 143:291-299.
    • (2007) Plant Phys , vol.143 , pp. 291-299
    • Xiong, Y.1    Contento, A.L.2    Nguyen, P.Q.3    Bassham, D.C.4
  • 17
    • 0000024413 scopus 로고
    • Effect of light on incompatible interactions between Xanthomonas oryzae pv oryzae and rice
    • Guo A., Reimers P.J., Leach J.E. Effect of light on incompatible interactions between Xanthomonas oryzae pv oryzae and rice. Physiol Mol Plant Pathol 1993, 42:413-425.
    • (1993) Physiol Mol Plant Pathol , vol.42 , pp. 413-425
    • Guo, A.1    Reimers, P.J.2    Leach, J.E.3
  • 18
    • 0029278767 scopus 로고
    • Rice Cationic peroxidase accumulates in xylem vessels during incompatible interactions with Xanthomonas oryzae Pv. oryzae.
    • Young S.A., Cuo A., Cuikema J.A., Whit F.F., Leach J.E. Rice Cationic peroxidase accumulates in xylem vessels during incompatible interactions with Xanthomonas oryzae Pv. oryzae. Plant Physiol 1995, 107:1333-1341.
    • (1995) Plant Physiol , vol.107 , pp. 1333-1341
    • Young, S.A.1    Cuo, A.2    Cuikema, J.A.3    Whit, F.F.4    Leach, J.E.5
  • 19
    • 0142057020 scopus 로고    scopus 로고
    • Understanding the functions of plant disease resistance proteins
    • Martin G.B., Bogdanove A.J., Sessa G. Understanding the functions of plant disease resistance proteins. Annu Rev Plant Biol 2003, 54:23-61.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 23-61
    • Martin, G.B.1    Bogdanove, A.J.2    Sessa, G.3
  • 20
    • 0010466085 scopus 로고    scopus 로고
    • Proteomics: an infinite problem with infinite potential
    • Speicher D.W. Proteomics: an infinite problem with infinite potential. The Scientist 2002, 16:12.
    • (2002) The Scientist , vol.16 , pp. 12
    • Speicher, D.W.1
  • 23
    • 0033150514 scopus 로고    scopus 로고
    • Accumulation of small heat-shock protein homologs in the endoplasmic reticulum of cortical parenchyma cells in mulberry in association with seasonal cold acclimation
    • Ukaji N., Kuwabara C., Takezawa D., Arakawa K., Yoshida S., Fujikawa S. Accumulation of small heat-shock protein homologs in the endoplasmic reticulum of cortical parenchyma cells in mulberry in association with seasonal cold acclimation. Plant Physiol 1999, 120:481-490.
    • (1999) Plant Physiol , vol.120 , pp. 481-490
    • Ukaji, N.1    Kuwabara, C.2    Takezawa, D.3    Arakawa, K.4    Yoshida, S.5    Fujikawa, S.6
  • 24
    • 0031992030 scopus 로고    scopus 로고
    • Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by iron deficiency in barley roots
    • Suzuki K., Itai R., Suzuki K., Nakanishi H., Nishizawa N.K., Yoshimura E., et al. Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by iron deficiency in barley roots. Plant Physiol 1998, 116:725-732.
    • (1998) Plant Physiol , vol.116 , pp. 725-732
    • Suzuki, K.1    Itai, R.2    Suzuki, K.3    Nakanishi, H.4    Nishizawa, N.K.5    Yoshimura, E.6
  • 25
    • 0038558610 scopus 로고    scopus 로고
    • Defence/stress responses elicited in rice seedlings exposed to the gaseous air pollutant sulfurdioxide
    • Rakwal R., Agrawal G.K., Kubo A., Yonekura M., Tamogami S., Saji H., et al. Defence/stress responses elicited in rice seedlings exposed to the gaseous air pollutant sulfurdioxide. Env Exp Bot 2003, 49:223-235.
    • (2003) Env Exp Bot , vol.49 , pp. 223-235
    • Rakwal, R.1    Agrawal, G.K.2    Kubo, A.3    Yonekura, M.4    Tamogami, S.5    Saji, H.6
  • 27
    • 34248668486 scopus 로고    scopus 로고
    • Proteomic analysis of rice plasma membrane reveals proteins involved in early defense response to bacterial blight
    • Chen F., Yuan Y., Li Q., He Z. Proteomic analysis of rice plasma membrane reveals proteins involved in early defense response to bacterial blight. Proteomics 2007, 7:1529-1539.
    • (2007) Proteomics , vol.7 , pp. 1529-1539
    • Chen, F.1    Yuan, Y.2    Li, Q.3    He, Z.4
  • 28
    • 34250635038 scopus 로고    scopus 로고
    • Coca M Sucrose-mediated priming of plant defense responses and broad-spectrum disease resistance nby overexpression of the maize pathogenesis-related PRms protein in rice plants
    • Gómez-Ariza J., Campo S., Rufat M., Estopà M., Messeguer J., Segundo B.S. Coca M Sucrose-mediated priming of plant defense responses and broad-spectrum disease resistance nby overexpression of the maize pathogenesis-related PRms protein in rice plants. MPMI 2007, 20:832-842.
    • (2007) MPMI , vol.20 , pp. 832-842
    • Gómez-Ariza, J.1    Campo, S.2    Rufat, M.3    Estopà, M.4    Messeguer, J.5    Segundo, B.S.6
  • 29
    • 33845970196 scopus 로고    scopus 로고
    • Proteome analysis of plant-virus interactome: comprehensive data for virus multiplication inside their hosts
    • Brizard J.P., Carapito C., Delalande F., Van Dorsselaer A., Brugidou C. Proteome analysis of plant-virus interactome: comprehensive data for virus multiplication inside their hosts. Mol Cell Proteom 2006, 5:2279-2297.
    • (2006) Mol Cell Proteom , vol.5 , pp. 2279-2297
    • Brizard, J.P.1    Carapito, C.2    Delalande, F.3    Van Dorsselaer, A.4    Brugidou, C.5
  • 30
    • 33645470420 scopus 로고    scopus 로고
    • Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction
    • Rampitsch C., Bykova N.V., McCallum B., Beimcik E., Ens W. Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction. Proteomics 2006, 6:1897-1907.
    • (2006) Proteomics , vol.6 , pp. 1897-1907
    • Rampitsch, C.1    Bykova, N.V.2    McCallum, B.3    Beimcik, E.4    Ens, W.5
  • 31
    • 27144505199 scopus 로고    scopus 로고
    • Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress
    • Castro A.J., Carapito C., Zorn N., Magné C., Leize E., Van Dorsselaer A., et al. Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress. J Exp Bot 2005, 56:2783-2795.
    • (2005) J Exp Bot , vol.56 , pp. 2783-2795
    • Castro, A.J.1    Carapito, C.2    Zorn, N.3    Magné, C.4    Leize, E.5    Van Dorsselaer, A.6
  • 32
    • 0037328264 scopus 로고    scopus 로고
    • Proteome analysis of the plant pathogen Xylella fastidiosa reveals major cellular and extracellular proteins and a peculiar codon bias distribution
    • Smolka M.B., Martins D., Winck F.V., Santoro C.E., Castellari R.R., Ferrari F., et al. Proteome analysis of the plant pathogen Xylella fastidiosa reveals major cellular and extracellular proteins and a peculiar codon bias distribution. Proteomics 2003, 3:224-237.
    • (2003) Proteomics , vol.3 , pp. 224-237
    • Smolka, M.B.1    Martins, D.2    Winck, F.V.3    Santoro, C.E.4    Castellari, R.R.5    Ferrari, F.6
  • 35
    • 34848929004 scopus 로고    scopus 로고
    • Xylella fastidiosa disturbs nitrogen metabolism and causes a stress response in sweet orange Citrus sinensis cv. Pêra
    • Purcino R.P., Medina C.L., de Souza D.M., Winck F.V., Machado E.C., Novello J.C., et al. Xylella fastidiosa disturbs nitrogen metabolism and causes a stress response in sweet orange Citrus sinensis cv. Pêra. J Exp Bot 2007, 58:2733-2744.
    • (2007) J Exp Bot , vol.58 , pp. 2733-2744
    • Purcino, R.P.1    Medina, C.L.2    de Souza, D.M.3    Winck, F.V.4    Machado, E.C.5    Novello, J.C.6
  • 37
    • 34250247622 scopus 로고
    • Axenic culture of the bacteria associated with phony disease of peach and plum leaf scald
    • Davis M.J., French W.J., Schaad N.W. Axenic culture of the bacteria associated with phony disease of peach and plum leaf scald. Curr Microbiol 1981, 5:311-316.
    • (1981) Curr Microbiol , vol.5 , pp. 311-316
    • Davis, M.J.1    French, W.J.2    Schaad, N.W.3
  • 38
    • 0018410271 scopus 로고
    • Presence of a major (storage) protein in dormant spores of the fungus Botryodiplodia theobromae
    • Van Etten J.L., Freer S.N., McCune B.K. Presence of a major (storage) protein in dormant spores of the fungus Botryodiplodia theobromae. J Bacteriol 1979, 138:650-652.
    • (1979) J Bacteriol , vol.138 , pp. 650-652
    • Van Etten, J.L.1    Freer, S.N.2    McCune, B.K.3
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification data
    • Craig R., Cortens J.P., Beavis R.C. Open source system for analyzing, validating, and storing protein identification data. J Proteome Res 2004, 3:1234-1242.
    • (2004) J Proteome Res , vol.3 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 42
    • 11244296642 scopus 로고    scopus 로고
    • Vitis resistance to Pierce's disease is characterized by differential Xylella fastidiosa populations in stems and leaves
    • Kirvanek A.F., Walker M.A. Vitis resistance to Pierce's disease is characterized by differential Xylella fastidiosa populations in stems and leaves. Phytopathology 2005, 95:44-52.
    • (2005) Phytopathology , vol.95 , pp. 44-52
    • Kirvanek, A.F.1    Walker, M.A.2
  • 43
    • 33846591963 scopus 로고    scopus 로고
    • CTrans: generating polypeptide databases from cDNA sequences
    • Xu H., Yang L., Xu P., Tao Y., Ma Z. cTrans: generating polypeptide databases from cDNA sequences. Proteomics 2007, 7:177-179.
    • (2007) Proteomics , vol.7 , pp. 177-179
    • Xu, H.1    Yang, L.2    Xu, P.3    Tao, Y.4    Ma, Z.5
  • 44
    • 0033819987 scopus 로고    scopus 로고
    • Characterization of an apoplastic basic thaumatin-like protein from recalcitrant chestnut seeds
    • Garcia-Casado G., Collada C., Allona I., Soto A., Casado R., Rodriguez-Cerezo E., et al. Characterization of an apoplastic basic thaumatin-like protein from recalcitrant chestnut seeds. Physiol Plant 2001, 110:172-180.
    • (2001) Physiol Plant , vol.110 , pp. 172-180
    • Garcia-Casado, G.1    Collada, C.2    Allona, I.3    Soto, A.4    Casado, R.5    Rodriguez-Cerezo, E.6
  • 45
    • 0344064153 scopus 로고    scopus 로고
    • Osmotin and thaumatin from grape: a putative general defense mechanism against pathogenic fungi
    • Monteiro S., Barakat M., Piçarra-Pereira M.A., Teixeira A.R., Ferreira R.B. Osmotin and thaumatin from grape: a putative general defense mechanism against pathogenic fungi. Phytopathol 2003, 93:1505-1512.
    • (2003) Phytopathol , vol.93 , pp. 1505-1512
    • Monteiro, S.1    Barakat, M.2    Piçarra-Pereira, M.A.3    Teixeira, A.R.4    Ferreira, R.B.5
  • 46
    • 0024871855 scopus 로고
    • Xylella fastidiosa: xylem-limited bacterial pathogen of plants
    • Hopkins D.L. Xylella fastidiosa: xylem-limited bacterial pathogen of plants. Annu Rev Phytopathol 1989, 27:271-290.
    • (1989) Annu Rev Phytopathol , vol.27 , pp. 271-290
    • Hopkins, D.L.1
  • 47
    • 33645348516 scopus 로고    scopus 로고
    • Pierce's disease symptoms: comparison with symptoms of water deficit and the impact of water deficits
    • Thorne E.T., Stevenson J.F., Rost T.L., Labavitch J.M., Matthews M.A. Pierce's disease symptoms: comparison with symptoms of water deficit and the impact of water deficits. Am J Enol Vitic 2006, 57:1-11.
    • (2006) Am J Enol Vitic , vol.57 , pp. 1-11
    • Thorne, E.T.1    Stevenson, J.F.2    Rost, T.L.3    Labavitch, J.M.4    Matthews, M.A.5
  • 48
    • 77949288004 scopus 로고    scopus 로고
    • Proteomics approach to identify unique xylem sap proteins in Pierce's disease-tolerant Vitis species
    • Basha S.M., Mazhar H., Vasanthaiah H.K. Proteomics approach to identify unique xylem sap proteins in Pierce's disease-tolerant Vitis species. Appl Biochem Biotechnol 2010, 160(3):932-944.
    • (2010) Appl Biochem Biotechnol , vol.160 , Issue.3 , pp. 932-944
    • Basha, S.M.1    Mazhar, H.2    Vasanthaiah, H.K.3
  • 49
    • 33845195949 scopus 로고    scopus 로고
    • Proteomic analysis of bacterial blight defense-responsive proteins in rice leaf blades
    • Mahmood T., Jan A., Kakishima M., Komatsu S. Proteomic analysis of bacterial blight defense-responsive proteins in rice leaf blades. Proteomics 2006, 6:6053-6065.
    • (2006) Proteomics , vol.6 , pp. 6053-6065
    • Mahmood, T.1    Jan, A.2    Kakishima, M.3    Komatsu, S.4
  • 50
    • 70349311699 scopus 로고    scopus 로고
    • Proteomic analysis of bacterial blight defence signalling pathway using transgenic rice overexpressing thaumatin-like protein
    • Mahmood T., Jan A., Komatsu S. Proteomic analysis of bacterial blight defence signalling pathway using transgenic rice overexpressing thaumatin-like protein. Biol Plant 2009, 53:285-293.
    • (2009) Biol Plant , vol.53 , pp. 285-293
    • Mahmood, T.1    Jan, A.2    Komatsu, S.3
  • 51
    • 32644485468 scopus 로고    scopus 로고
    • Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome
    • Finnie C., Bak-Jensen K.S., Laugesen S., Roepstorff P., Svensson B. Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome. Plant Sci 2006, 170:4808-4821.
    • (2006) Plant Sci , vol.170 , pp. 4808-4821
    • Finnie, C.1    Bak-Jensen, K.S.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 53
    • 0034968063 scopus 로고    scopus 로고
    • Drechslera teres-infected barley (Hordeum vulgare L.) leaves accumulated eight isoforms of thaumatin-like proteins
    • Reiss E., Horstmann C. Drechslera teres-infected barley (Hordeum vulgare L.) leaves accumulated eight isoforms of thaumatin-like proteins. Physiol Mol Plant Pathol 2001, 58:183-188.
    • (2001) Physiol Mol Plant Pathol , vol.58 , pp. 183-188
    • Reiss, E.1    Horstmann, C.2
  • 54
    • 0030220102 scopus 로고    scopus 로고
    • Isolation and expression of a host response gene family encoding thaumatin-like proteins in incompatible oat-stem rust fungus intersections
    • Lin K.C., Bushnell W.R., Szabo L.J., Smith A.G. Isolation and expression of a host response gene family encoding thaumatin-like proteins in incompatible oat-stem rust fungus intersections. Molec Plant-Microbe Intera 1996, 9:511-522.
    • (1996) Molec Plant-Microbe Intera , vol.9 , pp. 511-522
    • Lin, K.C.1    Bushnell, W.R.2    Szabo, L.J.3    Smith, A.G.4
  • 55
    • 33750967667 scopus 로고    scopus 로고
    • A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity
    • Chadha P., Das R.H. A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity. Planta 2006, 225:213-222.
    • (2006) Planta , vol.225 , pp. 213-222
    • Chadha, P.1    Das, R.H.2
  • 57
    • 1642564546 scopus 로고    scopus 로고
    • Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway
    • Park C.J., Kim K.J., Shin R., Park J.M., Shin Y.C., Paek K.H. Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway. Plant J 2004, 37:186-198.
    • (2004) Plant J , vol.37 , pp. 186-198
    • Park, C.J.1    Kim, K.J.2    Shin, R.3    Park, J.M.4    Shin, Y.C.5    Paek, K.H.6
  • 58
    • 0033767809 scopus 로고    scopus 로고
    • Differential screening indicates a dramatic change in mRNA profiles during grape berry ripening. Cloning and characterization of cDNAs encoding putative cell wall and stress response proteins
    • Davies C., Robinson S.P. Differential screening indicates a dramatic change in mRNA profiles during grape berry ripening. Cloning and characterization of cDNAs encoding putative cell wall and stress response proteins. Plant Physiol 2000, 122:803-812.
    • (2000) Plant Physiol , vol.122 , pp. 803-812
    • Davies, C.1    Robinson, S.P.2
  • 59
    • 0034079835 scopus 로고    scopus 로고
    • Isolation of cDNA clones corresponding to genes expressed during fruit ripening in Japanese pear (Pyrus pyrifolia Nakai): involvement of the ethylene signal transduction pathway in their expression
    • Itai A., Tanabe K., Tamura F., Tanaka T. Isolation of cDNA clones corresponding to genes expressed during fruit ripening in Japanese pear (Pyrus pyrifolia Nakai): involvement of the ethylene signal transduction pathway in their expression. J Exp Bot 2000, 51:1163-1166.
    • (2000) J Exp Bot , vol.51 , pp. 1163-1166
    • Itai, A.1    Tanabe, K.2    Tamura, F.3    Tanaka, T.4
  • 61
    • 0029360442 scopus 로고
    • Characterization of a family of genes encoding a fruit-specific wound-stimulated protein of bell pepper (Capsicum annuum): identification of a new family of transposable elements
    • Pozueta-Romero J., Klein M., Houlné G., Schantz M.L., Meyer B., Schantz R. Characterization of a family of genes encoding a fruit-specific wound-stimulated protein of bell pepper (Capsicum annuum): identification of a new family of transposable elements. Plant Mol Biol 1995, 28:1011-1025.
    • (1995) Plant Mol Biol , vol.28 , pp. 1011-1025
    • Pozueta-Romero, J.1    Klein, M.2    Houlné, G.3    Schantz, M.L.4    Meyer, B.5    Schantz, R.6
  • 62
    • 0030997975 scopus 로고    scopus 로고
    • Characterization of two cDNA clones for mRNAs expressed during ripening of melon (Cucumis melo L.) fruits
    • Aggelis A., John I., Karvouni Z., Grierson D. Characterization of two cDNA clones for mRNAs expressed during ripening of melon (Cucumis melo L.) fruits. Plant Mol Biol 1997, 3:313-322.
    • (1997) Plant Mol Biol , vol.3 , pp. 313-322
    • Aggelis, A.1    John, I.2    Karvouni, Z.3    Grierson, D.4
  • 63
    • 0027639774 scopus 로고
    • Tomato (Lycopersicon esculentum) transcript induced by water deficit and ripening
    • Iusem N.D., Bartholomew D.M., Hitz W.D., Scolnik P.A. Tomato (Lycopersicon esculentum) transcript induced by water deficit and ripening. Plant Physiol 1993, 102:1353-1354.
    • (1993) Plant Physiol , vol.102 , pp. 1353-1354
    • Iusem, N.D.1    Bartholomew, D.M.2    Hitz, W.D.3    Scolnik, P.A.4
  • 64
    • 0000382475 scopus 로고    scopus 로고
    • Protein changes in response to progressive water deficit in maize. Quantitative variation and polypeptide identification
    • Riccardi F., Gazeau P., de Vienne D., Zivy M. Protein changes in response to progressive water deficit in maize. Quantitative variation and polypeptide identification. Plant Physiol 1998, 117:1253-1263.
    • (1998) Plant Physiol , vol.117 , pp. 1253-1263
    • Riccardi, F.1    Gazeau, P.2    de Vienne, D.3    Zivy, M.4
  • 65
    • 33845793939 scopus 로고    scopus 로고
    • Microarray analysis of Fusarium graminearum-induced wheat genes: identification of organ-specific and differentiallyexpressed genes
    • Golkari S., Gilbert J., Prashar S., Procunier J.D. Microarray analysis of Fusarium graminearum-induced wheat genes: identification of organ-specific and differentiallyexpressed genes. Plant Biotechnol J 2007, 5:38-49.
    • (2007) Plant Biotechnol J , vol.5 , pp. 38-49
    • Golkari, S.1    Gilbert, J.2    Prashar, S.3    Procunier, J.D.4
  • 66
    • 0035991175 scopus 로고    scopus 로고
    • Functional and comparative bioinformatic analysis of expressed genes from wheat spikes infected with Fusarium graminearum
    • Kruger W.M., Pritsch C., Chao S., Muehlbauer G.J. Functional and comparative bioinformatic analysis of expressed genes from wheat spikes infected with Fusarium graminearum. Mol Plant Microbe Interact 2002, 15:445-455.
    • (2002) Mol Plant Microbe Interact , vol.15 , pp. 445-455
    • Kruger, W.M.1    Pritsch, C.2    Chao, S.3    Muehlbauer, G.J.4
  • 67
    • 79151484086 scopus 로고    scopus 로고
    • A truncated form of ribosomal protein l3 eliminates ribosome depurination and cell death caused by pokeweed antiviral protein and confers resistance to trichothecene mycotoxins. In: Proceedings of the 2nd International Symposium on Fusarium Head Blight Incorporating the 8th European Fusarium Seminar, Orlando, FL.
    • Di R, TumerNE. A truncated form of ribosomal protein l3 eliminates ribosome depurination and cell death caused by pokeweed antiviral protein and confers resistance to trichothecene mycotoxins. In: Proceedings of the 2nd International Symposium on Fusarium Head Blight Incorporating the 8th European Fusarium Seminar, Orlando, FL, 2004; 1:242.
    • (2004) , vol.1 , Issue.242
    • Di, R.1    Tumer, N.E.2
  • 69
    • 0031757704 scopus 로고    scopus 로고
    • The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress
    • Heckathorn S.A., Downs C.A., Sharkey T.D., Coleman J.S. The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress. Plant Physiol 1998, 116:439-444.
    • (1998) Plant Physiol , vol.116 , pp. 439-444
    • Heckathorn, S.A.1    Downs, C.A.2    Sharkey, T.D.3    Coleman, J.S.4
  • 70
    • 79151485591 scopus 로고    scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U., Gaestel M., Engel K., Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem 2009, 50:4734-4742.
    • (2009) J Biol Chem , vol.50 , pp. 4734-4742
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 71
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee G.J., Pokala N., Vierling E. Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J Biol Chem 1995, 270:10432-10438.
    • (1995) J Biol Chem , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 72
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E.R., Lee G.J., Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 1996, 47:325-338.
    • (1996) J Exp Bot , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 73
    • 0242416497 scopus 로고    scopus 로고
    • Heat-shock proteins are induced in unstressed leaves of Nicotiana attenuate (Solanaceae) when distant leaves are stressed
    • Hamilton E.W., Coleman J.S. Heat-shock proteins are induced in unstressed leaves of Nicotiana attenuate (Solanaceae) when distant leaves are stressed. Am J Bot 2001, 88:950-955.
    • (2001) Am J Bot , vol.88 , pp. 950-955
    • Hamilton, E.W.1    Coleman, J.S.2
  • 74
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L., Nykänen P., Sistonen L. Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 2001, 15:1118-1131.
    • (2001) FASEB J , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykänen, P.2    Sistonen, L.3
  • 76
    • 0010756341 scopus 로고
    • Effect of a fungal disease on extension, the plant cell wall glycoprotein
    • Esquerré-Tugayé M.T., Mazaud D. Effect of a fungal disease on extension, the plant cell wall glycoprotein. J Exp Bot 1974, 3:509-513.
    • (1974) J Exp Bot , vol.3 , pp. 509-513
    • Esquerré-Tugayé, M.T.1    Mazaud, D.2
  • 77
    • 0034106377 scopus 로고    scopus 로고
    • The Arabidopsis thaliana ATP-binding cassette proteins: an emerging superfamily
    • Davies T.G.E., Coleman J.O.D. The Arabidopsis thaliana ATP-binding cassette proteins: an emerging superfamily. Plant Cell Environ 2001, 23:431-443.
    • (2001) Plant Cell Environ , vol.23 , pp. 431-443
    • Davies, T.G.E.1    Coleman, J.O.D.2
  • 79
    • 0034460090 scopus 로고    scopus 로고
    • YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168
    • Prágai Z., Harwood C.R. YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168. J Bacteriol 2000, 182:6819-6823.
    • (2000) J Bacteriol , vol.182 , pp. 6819-6823
    • Prágai, Z.1    Harwood, C.R.2
  • 80
    • 33646565646 scopus 로고    scopus 로고
    • Molecular cloning and expression of a small GTP-binding protein of the Rop family from mung bean
    • Eom E.M., Cho J.K., Lim S.O., Byun Y.J., Lee D.H. Molecular cloning and expression of a small GTP-binding protein of the Rop family from mung bean. Plant Sci 2006, 171:41-51.
    • (2006) Plant Sci , vol.171 , pp. 41-51
    • Eom, E.M.1    Cho, J.K.2    Lim, S.O.3    Byun, Y.J.4    Lee, D.H.5
  • 82
    • 33745662410 scopus 로고    scopus 로고
    • Reactive oxygen species signaling in response to pathogens
    • Torres M.A., Jones J.D.G., Dangl J.L. Reactive oxygen species signaling in response to pathogens. Plant Physiol 2006, 141:373-378.
    • (2006) Plant Physiol , vol.141 , pp. 373-378
    • Torres, M.A.1    Jones, J.D.G.2    Dangl, J.L.3


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