메뉴 건너뛰기




Volumn 91, Issue , 2013, Pages 605-618

The plasma membrane proteome of maize roots grown under low and high iron conditions

Author keywords

Iron deficiency; Iron toxicity; Plasma membrane proteome; Redox systems; Zea mays

Indexed keywords

ACTIN; AQUAPORIN; ARABINOGALACTAN; AUXIN; CALRETICULIN; CHAPERONE; ELONGATION FACTOR 1; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 2; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCAN ENDO 1,3 BETA GLUCOSIDASE; HEME; IRON; JASMONIC ACID; LECTIN; LIPOXYGENASE; LONG CHAIN FATTY ACID COENZYME A LIGASE; MALATE DEHYDROGENASE; METHIONINE ADENOSYLTRANSFERASE; NUCLEOSOME ASSEMBLY PROTEIN 1; PEPSIN A; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PROTEIN KINASE; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); RIBOSOME PROTEIN; RICIN; STEROID BINDING PROTEIN; THIOREDOXIN H; TUBULIN;

EID: 84887175550     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.01.006     Document Type: Article
Times cited : (48)

References (93)
  • 3
    • 0033039643 scopus 로고    scopus 로고
    • Mechanisms and regulation of reduction-based iron uptake in plants
    • Schmidt W. Mechanisms and regulation of reduction-based iron uptake in plants. New Phytol 1999, 141:1-26.
    • (1999) New Phytol , vol.141 , pp. 1-26
    • Schmidt, W.1
  • 4
    • 0033080541 scopus 로고    scopus 로고
    • Cloning of nicotianamine synthase, novel genes involved in the biosynthesis of phytosiderophores
    • Higuchi K., Suzuki K., Nakanishi H., Yamaguchi H., Nishizawa N.K., Mori S. Cloning of nicotianamine synthase, novel genes involved in the biosynthesis of phytosiderophores. Plant Physiol 1999, 119:471-480.
    • (1999) Plant Physiol , vol.119 , pp. 471-480
    • Higuchi, K.1    Suzuki, K.2    Nakanishi, H.3    Yamaguchi, H.4    Nishizawa, N.K.5    Mori, S.6
  • 5
    • 0033230799 scopus 로고    scopus 로고
    • Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants
    • Takahashi M., Yamaguchi H., Nakanishi H., Nishizawa N.K., Mori S. Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants. Plant Physiol 1999, 121:947-956.
    • (1999) Plant Physiol , vol.121 , pp. 947-956
    • Takahashi, M.1    Yamaguchi, H.2    Nakanishi, H.3    Nishizawa, N.K.4    Mori, S.5
  • 6
    • 0033675662 scopus 로고    scopus 로고
    • Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores
    • Nakanishi H., Yamaguchi H., Sasakuma T., Nishizawa N.K., Mori S. Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores. Plant Mol Biol 2000, 44:199-207.
    • (2000) Plant Mol Biol , vol.44 , pp. 199-207
    • Nakanishi, H.1    Yamaguchi, H.2    Sasakuma, T.3    Nishizawa, N.K.4    Mori, S.5
  • 7
    • 33845948186 scopus 로고    scopus 로고
    • Cloning ad characterization of deoxymugineic acid synthase genes from Graminaceous plants
    • Bashir K., Inoue H., Nagasaka S., Takahashi M., Nakanishi H., Mori S., et al. Cloning ad characterization of deoxymugineic acid synthase genes from Graminaceous plants. J Biol Chem 2006, 281:32395-32402.
    • (2006) J Biol Chem , vol.281 , pp. 32395-32402
    • Bashir, K.1    Inoue, H.2    Nagasaka, S.3    Takahashi, M.4    Nakanishi, H.5    Mori, S.6
  • 8
    • 0035905794 scopus 로고    scopus 로고
    • Maize yellow stripe1 encodes a membrane protein directly involved in Fe (III) uptake
    • Curie C., Panaviene Z., Loulergue C., Dellaporta S.L., Briat J.F., Walker E.L. Maize yellow stripe1 encodes a membrane protein directly involved in Fe (III) uptake. Nature 2001, 409:346-349.
    • (2001) Nature , vol.409 , pp. 346-349
    • Curie, C.1    Panaviene, Z.2    Loulergue, C.3    Dellaporta, S.L.4    Briat, J.F.5    Walker, E.L.6
  • 9
    • 3843129548 scopus 로고    scopus 로고
    • OsYSL2 is a rice metal-nicotianamine transporter that is regulated by iron and expressed in the phloem
    • Koike S., Inoue H., Mizuno D., Takahashi M., Nakanishi H., Mori S., et al. OsYSL2 is a rice metal-nicotianamine transporter that is regulated by iron and expressed in the phloem. Plant J 2004, 39:415-424.
    • (2004) Plant J , vol.39 , pp. 415-424
    • Koike, S.1    Inoue, H.2    Mizuno, D.3    Takahashi, M.4    Nakanishi, H.5    Mori, S.6
  • 10
    • 33646240063 scopus 로고    scopus 로고
    • A specific transporter for iron (III)-phytosiderophore in barley roots
    • Murata Y., Ma J.F., Yamaji N., Ueno D., Nomoto K., Iwashita T. A specific transporter for iron (III)-phytosiderophore in barley roots. Plant J 2006, 46:563-572.
    • (2006) Plant J , vol.46 , pp. 563-572
    • Murata, Y.1    Ma, J.F.2    Yamaji, N.3    Ueno, D.4    Nomoto, K.5    Iwashita, T.6
  • 11
    • 36949088391 scopus 로고
    • Physiological disease of rice attributable to iron toxicity
    • Ponnamperuma F.N., Bradfield R., Peech M. Physiological disease of rice attributable to iron toxicity. Nature 1955, 175:265.
    • (1955) Nature , vol.175 , pp. 265
    • Ponnamperuma, F.N.1    Bradfield, R.2    Peech, M.3
  • 12
    • 41349118761 scopus 로고    scopus 로고
    • Developmental characteristics and response to iron toxicity of root border cells in rice seedlings
    • Xing C.H., Zhu M.H., Cai M.Z., Liu P.Xu.G.D., Wu S.H. Developmental characteristics and response to iron toxicity of root border cells in rice seedlings. J Zhejiang Univ Sci B 2008, 9:261-264.
    • (2008) J Zhejiang Univ Sci B , vol.9 , pp. 261-264
    • Xing, C.H.1    Zhu, M.H.2    Cai, M.Z.3    Liu, P.4    Wu, S.H.5
  • 13
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • Lander H.M. An essential role for free radicals and derived species in signal transduction. FASEB J 1997, 11:118-124.
    • (1997) FASEB J , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 15
    • 41849137251 scopus 로고    scopus 로고
    • A proteomic study showing differential regulation of stress, redox regulation and peroxidase proteins by iron supply and transcription factor FER
    • Brumbarova T., Matros A., Mock H.P., Bauer P. A proteomic study showing differential regulation of stress, redox regulation and peroxidase proteins by iron supply and transcription factor FER. Plant J 2008, 54:321-334.
    • (2008) Plant J , vol.54 , pp. 321-334
    • Brumbarova, T.1    Matros, A.2    Mock, H.P.3    Bauer, P.4
  • 16
    • 79551697131 scopus 로고    scopus 로고
    • ITRAQ protein profile analysis of Arabidopsis roots reveals new aspects critical for iron homeostasis
    • Lan P., Li W., Wen T.N., Shiau J.Y., Wu Y.C., Lin W., et al. iTRAQ protein profile analysis of Arabidopsis roots reveals new aspects critical for iron homeostasis. Plant Physiol 2011, 155:821-834.
    • (2011) Plant Physiol , vol.155 , pp. 821-834
    • Lan, P.1    Li, W.2    Wen, T.N.3    Shiau, J.Y.4    Wu, Y.C.5    Lin, W.6
  • 18
    • 79955870864 scopus 로고    scopus 로고
    • Root responses of Medicago truncatula plants grown in two different iron deficiency conditions: changes in root protein profile and riboflavin biosynthesis
    • Rodríguez-Celma J., Lattanzio G., Grusak M.A., Abadía A., Abadía J., López-Millán A.F. Root responses of Medicago truncatula plants grown in two different iron deficiency conditions: changes in root protein profile and riboflavin biosynthesis. J Proteome Res 2011, 10:2590-2601.
    • (2011) J Proteome Res , vol.10 , pp. 2590-2601
    • Rodríguez-Celma, J.1    Lattanzio, G.2    Grusak, M.A.3    Abadía, A.4    Abadía, J.5    López-Millán, A.F.6
  • 19
    • 78649521637 scopus 로고    scopus 로고
    • Proteomic characterization of iron deficiency responses in Cucumis sativus L. roots
    • Donnini S., Prinsi B., Negri A.S., Vigani G., Espen L., Zocchi G. Proteomic characterization of iron deficiency responses in Cucumis sativus L. roots. BMC Plant Biol 2010, 10:268.
    • (2010) BMC Plant Biol , vol.10 , pp. 268
    • Donnini, S.1    Prinsi, B.2    Negri, A.S.3    Vigani, G.4    Espen, L.5    Zocchi, G.6
  • 20
    • 79960996033 scopus 로고    scopus 로고
    • Alteration of plasma membrane-bound redox systems of iron deficient pea roots by chitosan
    • Meisrimler C.N., Planchon S., Renaut J., Sergeant K., Lüthje S. Alteration of plasma membrane-bound redox systems of iron deficient pea roots by chitosan. J Proteomics 2011, 74:1437-1439.
    • (2011) J Proteomics , vol.74 , pp. 1437-1439
    • Meisrimler, C.N.1    Planchon, S.2    Renaut, J.3    Sergeant, K.4    Lüthje, S.5
  • 21
    • 34047142294 scopus 로고    scopus 로고
    • Protective effect of nitric oxide on iron deficiency-induced oxidative stress in maize (Zea mays)
    • Baoteng S., Yan J., Kunming C., Lili S., Fangjian C., Lixin Z. Protective effect of nitric oxide on iron deficiency-induced oxidative stress in maize (Zea mays). J Plant Physiol 2007, 164:536-543.
    • (2007) J Plant Physiol , vol.164 , pp. 536-543
    • Baoteng, S.1    Yan, J.2    Kunming, C.3    Lili, S.4    Fangjian, C.5    Lixin, Z.6
  • 23
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 24
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., Yates John R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 2004, 76:4193-4201.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 25
    • 52649132380 scopus 로고    scopus 로고
    • Integration of metabolomic and proteomic phenotypes-analysis of data-covariance dissects starch and RFO metabolism from low and high temperature compensation response in Arabidopsis thaliana
    • Wienkoop S., Morgenthal K., Wolschin F., Scholz M., Selbig J., Weckwerth W. Integration of metabolomic and proteomic phenotypes-analysis of data-covariance dissects starch and RFO metabolism from low and high temperature compensation response in Arabidopsis thaliana. Mol Cell Proteomics 2008, 7:1725-1736.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1725-1736
    • Wienkoop, S.1    Morgenthal, K.2    Wolschin, F.3    Scholz, M.4    Selbig, J.5    Weckwerth, W.6
  • 26
    • 84887160165 scopus 로고    scopus 로고
    • Extended abstract: constructing area-proportional Venn and Euler diagrams with three circles
    • Paris
    • Stirling Chow S., Peter Rodgers P. Extended abstract: constructing area-proportional Venn and Euler diagrams with three circles. Presented at Euler diagrams workshop 2005, Paris.
    • (2005) Presented at Euler diagrams workshop
    • Stirling Chow, S.1    Peter Rodgers, P.2
  • 27
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman D. Membranes are more mosaic than fluid. Nature 2005, 438:578-580.
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.1
  • 28
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 1998, 92:291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 29
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: heterogeneity on the high seas
    • Pike L. Lipid rafts: heterogeneity on the high seas. Biochem J 2004, 378:281-292.
    • (2004) Biochem J , vol.378 , pp. 281-292
    • Pike, L.1
  • 30
    • 0038268709 scopus 로고    scopus 로고
    • Soluble proteins, an often overlooked contaminant in plasma membrane preparations
    • Bérczi A., Asard H. Soluble proteins, an often overlooked contaminant in plasma membrane preparations. Trends Plant Sci 2003, 8:250-251.
    • (2003) Trends Plant Sci , vol.8 , pp. 250-251
    • Bérczi, A.1    Asard, H.2
  • 31
    • 76649093600 scopus 로고    scopus 로고
    • Proteomics of plasma membranes from poplar trees reveals tissue distribution of transporters, receptors, and proteins in cell wall formation
    • Nilsson R., Bernfur K., Gustavsson N., Bygdell J., Wingsle G., Larsson C. Proteomics of plasma membranes from poplar trees reveals tissue distribution of transporters, receptors, and proteins in cell wall formation. Mol Cell Proteomics 2010, 9:368-387.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 368-387
    • Nilsson, R.1    Bernfur, K.2    Gustavsson, N.3    Bygdell, J.4    Wingsle, G.5    Larsson, C.6
  • 32
    • 34250677613 scopus 로고    scopus 로고
    • Characterization of lipid rafts from Medicago truncatula root plasma membranes: a proteomic study reveals the presence of a raft-associated redox system
    • Lefebvre B., Furt F., Hartmann M.A., Michaelson L.V., Carde J.P., Sargueil-Boiron F., et al. Characterization of lipid rafts from Medicago truncatula root plasma membranes: a proteomic study reveals the presence of a raft-associated redox system. Plant Physiol 2007, 144:402-418.
    • (2007) Plant Physiol , vol.144 , pp. 402-418
    • Lefebvre, B.1    Furt, F.2    Hartmann, M.A.3    Michaelson, L.V.4    Carde, J.P.5    Sargueil-Boiron, F.6
  • 34
    • 84887181659 scopus 로고    scopus 로고
    • Sällman-Almen Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin
    • Sällman-Almen Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol 2009, 7:1-14.
    • (2009) BMC Biol , vol.7 , pp. 1-14
  • 36
    • 4344627295 scopus 로고    scopus 로고
    • Protein complexes of the plant plasma membrane resolved by Blue Native PAGE
    • Kjell J., Rasmusson A.G., Larsson H., Widell S. Protein complexes of the plant plasma membrane resolved by Blue Native PAGE. Physiol Plant 2004, 121:546-555.
    • (2004) Physiol Plant , vol.121 , pp. 546-555
    • Kjell, J.1    Rasmusson, A.G.2    Larsson, H.3    Widell, S.4
  • 37
    • 34248233008 scopus 로고    scopus 로고
    • Plant aquaporins: novel functions and regulation properties
    • Maurel C. Plant aquaporins: novel functions and regulation properties. FEBS Lett 2007, 581:2227-2236.
    • (2007) FEBS Lett , vol.581 , pp. 2227-2236
    • Maurel, C.1
  • 40
    • 83355161568 scopus 로고    scopus 로고
    • Hydrogen peroxide permeability of plasma membrane aquaporins of Arabidopsis thaliana
    • Hooijmaijers C., Rhee J.Y., Kwak K.J., Chung G.C., Horie T., Katsuhara M., et al. Hydrogen peroxide permeability of plasma membrane aquaporins of Arabidopsis thaliana. J Plant Res 2012, 125:147-153.
    • (2012) J Plant Res , vol.125 , pp. 147-153
    • Hooijmaijers, C.1    Rhee, J.Y.2    Kwak, K.J.3    Chung, G.C.4    Horie, T.5    Katsuhara, M.6
  • 41
    • 0026192024 scopus 로고
    • Evidence for a plasma membrane proton pump in phloem cells of higher plants
    • DeWitt N.D., Harper J.F., Sussman M.R. Evidence for a plasma membrane proton pump in phloem cells of higher plants. Plant J 1991, 1:121-128.
    • (1991) Plant J , vol.1 , pp. 121-128
    • DeWitt, N.D.1    Harper, J.F.2    Sussman, M.R.3
  • 42
    • 67650800353 scopus 로고    scopus 로고
    • Proton pump OsA8 is linked to phosphorus uptake and translocation in rice
    • Chunrong C., Yibing H., Shubin S., Yiyong Z., Guojie M., Guohua X. Proton pump OsA8 is linked to phosphorus uptake and translocation in rice. J Exp Bot 2009, 60(2):557-565.
    • (2009) J Exp Bot , vol.60 , Issue.2 , pp. 557-565
    • Chunrong, C.1    Yibing, H.2    Shubin, S.3    Yiyong, Z.4    Guojie, M.5    Guohua, X.6
  • 46
    • 0002286083 scopus 로고
    • Evidence for a specific uptake system for iron phytosiderophores in roots of grasses
    • Römheld V., Marschner H. Evidence for a specific uptake system for iron phytosiderophores in roots of grasses. Plant Physiol 1986, 80:175-180.
    • (1986) Plant Physiol , vol.80 , pp. 175-180
    • Römheld, V.1    Marschner, H.2
  • 47
    • 46049119887 scopus 로고    scopus 로고
    • Proteomic response to iron deficiency in tomato root
    • Li J., Wu X.D., Hao S.T., Wang X.J., Ling H.Q. Proteomic response to iron deficiency in tomato root. Proteomics 2008, 11:2299-2311.
    • (2008) Proteomics , vol.11 , pp. 2299-2311
    • Li, J.1    Wu, X.D.2    Hao, S.T.3    Wang, X.J.4    Ling, H.Q.5
  • 48
    • 33749137053 scopus 로고    scopus 로고
    • The monosaccharide transporter gene family in land plants is ancient and shows differential subfamily expression and expansion across lineages
    • Johnson D.A., Hill J.P., Thomas M.A. The monosaccharide transporter gene family in land plants is ancient and shows differential subfamily expression and expansion across lineages. BMC Evol Biol 2006, 6(64):1-20.
    • (2006) BMC Evol Biol , vol.6 , Issue.64 , pp. 1-20
    • Johnson, D.A.1    Hill, J.P.2    Thomas, M.A.3
  • 49
    • 67649467462 scopus 로고    scopus 로고
    • Increased hexose transport in the roots of tomato plants submitted to prolonged hypoxia
    • Gharbi I., Ricard B., Smiti S., Bizid E., Brouquisse R. Increased hexose transport in the roots of tomato plants submitted to prolonged hypoxia. Planta 2009, 230:441-448.
    • (2009) Planta , vol.230 , pp. 441-448
    • Gharbi, I.1    Ricard, B.2    Smiti, S.3    Bizid, E.4    Brouquisse, R.5
  • 50
    • 0037165641 scopus 로고    scopus 로고
    • Molecular and structural analyses of a novel temperature stress-induced lipocalin from wheat and Arabidopsis
    • Frenette Charron J.B., Breton G., Badawi M., Sarhan F. Molecular and structural analyses of a novel temperature stress-induced lipocalin from wheat and Arabidopsis. FEBS Lett 2002, 17(1-3):129-132.
    • (2002) FEBS Lett , vol.17 , Issue.1-3 , pp. 129-132
    • Frenette Charron, J.B.1    Breton, G.2    Badawi, M.3    Sarhan, F.4
  • 52
    • 66249117313 scopus 로고    scopus 로고
    • Temperature-induced lipocalin is required for basal and acquired thermotolerance in Arabidopsis
    • Wen-Tzu C., Fung R.W.M., Hsiang-Chin L., Ching-Chi H., Yee-Yung C. Temperature-induced lipocalin is required for basal and acquired thermotolerance in Arabidopsis. Plant Cell Environ 2009, 32:917-927.
    • (2009) Plant Cell Environ , vol.32 , pp. 917-927
    • Wen-Tzu, C.1    Fung, R.W.M.2    Hsiang-Chin, L.3    Ching-Chi, H.4    Yee-Yung, C.5
  • 53
    • 84870787658 scopus 로고    scopus 로고
    • Arabidopsis 14-3-3 proteins: fascinating and less fascinating aspects
    • Jaspert N., Throm C., Oecking C. Arabidopsis 14-3-3 proteins: fascinating and less fascinating aspects. Front Plant Sci 2011, 2(68):1-8.
    • (2011) Front Plant Sci , vol.2 , Issue.68 , pp. 1-8
    • Jaspert, N.1    Throm, C.2    Oecking, C.3
  • 54
    • 0036233852 scopus 로고    scopus 로고
    • From cytosol to organelles: 14-3-3 proteins as multifunctional regulators of plant cell
    • Aducci P., Camoni L., Marra M., Visconti S. From cytosol to organelles: 14-3-3 proteins as multifunctional regulators of plant cell. IUBMB Life 2002, 53:49-55.
    • (2002) IUBMB Life , vol.53 , pp. 49-55
    • Aducci, P.1    Camoni, L.2    Marra, M.3    Visconti, S.4
  • 56
  • 57
    • 36849029862 scopus 로고    scopus 로고
    • Signalling through kinase-defective domains: the prevalence of atypical receptor-like kinases in plants
    • Castells E., Casacuberta J.M. Signalling through kinase-defective domains: the prevalence of atypical receptor-like kinases in plants. J Exp Bot 2007, 58(13):3503-3511.
    • (2007) J Exp Bot , vol.58 , Issue.13 , pp. 3503-3511
    • Castells, E.1    Casacuberta, J.M.2
  • 58
    • 77955699070 scopus 로고    scopus 로고
    • Activation of plant immune responses by a gain-of-function mutation in an atypical receptor-like kinase
    • Dongling B., Yu Ti C., Xin L., Yuelin Z. Activation of plant immune responses by a gain-of-function mutation in an atypical receptor-like kinase. Plant Physiol 2010, 153:1771-1779.
    • (2010) Plant Physiol , vol.153 , pp. 1771-1779
    • Dongling, B.1    Yu Ti, C.2    Xin, L.3    Yuelin, Z.4
  • 59
    • 79956115499 scopus 로고    scopus 로고
    • Structure-function analysis of STRUBBELIG, an Arabidopsis atypical receptor-like kinase involved in tissue morphogenesis
    • Vaddepalli P., Fulton L., Batoux M., Yadav R.K., Schneitz K. Structure-function analysis of STRUBBELIG, an Arabidopsis atypical receptor-like kinase involved in tissue morphogenesis. PLoS One 2011, 6(5):1-19.
    • (2011) PLoS One , vol.6 , Issue.5 , pp. 1-19
    • Vaddepalli, P.1    Fulton, L.2    Batoux, M.3    Yadav, R.K.4    Schneitz, K.5
  • 61
    • 33750003671 scopus 로고    scopus 로고
    • The PTI1-like kinase ZmPti1a from maize (Zea mays L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
    • Herrmann M.M., Pinto S., Kluth J., Wienand U., Lorbiecke R. The PTI1-like kinase ZmPti1a from maize (Zea mays L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte. BMC Plant Biol 2006, 6:22.
    • (2006) BMC Plant Biol , vol.6 , pp. 22
    • Herrmann, M.M.1    Pinto, S.2    Kluth, J.3    Wienand, U.4    Lorbiecke, R.5
  • 62
    • 79952830764 scopus 로고    scopus 로고
    • The Arabidopsis protein kinase Pto-interacting 1-4 is a common target of the oxidative signal-inducible 1 and mitogen-activated protein kinases
    • Forzani C., Carreri A., de la Fuente van Bentem S., Lecourieux D., Lecourieux F., Hirt H. The Arabidopsis protein kinase Pto-interacting 1-4 is a common target of the oxidative signal-inducible 1 and mitogen-activated protein kinases. FEBS J 2011, 278:1126-1136.
    • (2011) FEBS J , vol.278 , pp. 1126-1136
    • Forzani, C.1    Carreri, A.2    de la Fuente van Bentem, S.3    Lecourieux, D.4    Lecourieux, F.5    Hirt, H.6
  • 63
    • 0037178776 scopus 로고    scopus 로고
    • BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling
    • Jia L., Jiangqi W., Lease K.A., Doke J.T., Tax F.E., Walker J.C. BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Cell 2002, 110:213-222.
    • (2002) Cell , vol.110 , pp. 213-222
    • Jia, L.1    Jiangqi, W.2    Lease, K.A.3    Doke, J.T.4    Tax, F.E.5    Walker, J.C.6
  • 64
    • 53949124557 scopus 로고    scopus 로고
    • Gibberellin signaling
    • Hartweck L.M. Gibberellin signaling. Planta 2008, 229:1-13.
    • (2008) Planta , vol.229 , pp. 1-13
    • Hartweck, L.M.1
  • 65
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis V.A., Malehorn D.E., Emr S.D., Greene R. The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J Cell Biol 1989, 108:1271-1281.
    • (1989) J Cell Biol , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 66
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis V.A., Aitken J.R., Cleves A.E., Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 1990, 347:561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 67
    • 84862116323 scopus 로고    scopus 로고
    • Heavy metal stress can prime for herbivore-induced plant volatile emission
    • Winter T.R., Borkowski L., Zeier J., Rostás M. Heavy metal stress can prime for herbivore-induced plant volatile emission. Plant Cell Environ 2012, 35:1287-1298.
    • (2012) Plant Cell Environ , vol.35 , pp. 1287-1298
    • Winter, T.R.1    Borkowski, L.2    Zeier, J.3    Rostás, M.4
  • 68
    • 2442466000 scopus 로고    scopus 로고
    • Biotic and heavy metal stress response in plants: evidence for common signals
    • Mithöfer A., Schulze B., Boland W. Biotic and heavy metal stress response in plants: evidence for common signals. FEBS Lett 2004, 566:1-5.
    • (2004) FEBS Lett , vol.566 , pp. 1-5
    • Mithöfer, A.1    Schulze, B.2    Boland, W.3
  • 69
    • 77950261904 scopus 로고    scopus 로고
    • Evolutionary history and stress regulation of the lectin superfamily in higher plants
    • Shu-Ye J., Zhigang M., Ramachandran S. Evolutionary history and stress regulation of the lectin superfamily in higher plants. BMC Evol Biol 2010, 10(79):1-24.
    • (2010) BMC Evol Biol , vol.10 , Issue.79 , pp. 1-24
    • Shu-Ye, J.1    Zhigang, M.2    Ramachandran, S.3
  • 70
    • 66649137700 scopus 로고    scopus 로고
    • Auxin-responsive genes AIR12 code for a new family of plasma membrane b-type cytochromes specific to flowering plants
    • Preger V., Tango N., Marchand C., Lemaire S.D., Carbonera D., Valentin M.D., et al. Auxin-responsive genes AIR12 code for a new family of plasma membrane b-type cytochromes specific to flowering plants. Plant Physiol 2009, 150:606-662.
    • (2009) Plant Physiol , vol.150 , pp. 606-662
    • Preger, V.1    Tango, N.2    Marchand, C.3    Lemaire, S.D.4    Carbonera, D.5    Valentin, M.D.6
  • 71
    • 0036742050 scopus 로고    scopus 로고
    • Plant lipoxygenases. Physiological and molecular features
    • Porta H., Rocha-Sosa M. Plant lipoxygenases. Physiological and molecular features. Plant Physiol 2002, 130:15-21.
    • (2002) Plant Physiol , vol.130 , pp. 15-21
    • Porta, H.1    Rocha-Sosa, M.2
  • 72
    • 0027134079 scopus 로고
    • Membrane-associated and soluble lipoxygenase isoforms in tomato pericarp
    • Droillard M.J., Rouet-Mayer M.A., Bureau J.M., Lauriere C. Membrane-associated and soluble lipoxygenase isoforms in tomato pericarp. Plant Physiol 1993, 103:1211-1219.
    • (1993) Plant Physiol , vol.103 , pp. 1211-1219
    • Droillard, M.J.1    Rouet-Mayer, M.A.2    Bureau, J.M.3    Lauriere, C.4
  • 74
    • 79251594548 scopus 로고    scopus 로고
    • Isolation and characterization of an apple cytosolic malate dehydrogenase gene reveal its function in malate synthesis
    • Yao Y.X., Li M., Zhai H., You C.X., Hao Y.J. Isolation and characterization of an apple cytosolic malate dehydrogenase gene reveal its function in malate synthesis. J Plant Physiol 2011, 168:474-480.
    • (2011) J Plant Physiol , vol.168 , pp. 474-480
    • Yao, Y.X.1    Li, M.2    Zhai, H.3    You, C.X.4    Hao, Y.J.5
  • 75
    • 68249140338 scopus 로고    scopus 로고
    • Apple sucrose transporter SUT1 and sorbitol transporter SOT6 interact with cytochrome b5 to regulate their affinity for substrate sugars
    • Fan R.C., Peng C.C., Xu Y.H., Wang X.F., Li Y., Shang Y., et al. Apple sucrose transporter SUT1 and sorbitol transporter SOT6 interact with cytochrome b5 to regulate their affinity for substrate sugars. Plant Physiol 2009, 150:1880-1901.
    • (2009) Plant Physiol , vol.150 , pp. 1880-1901
    • Fan, R.C.1    Peng, C.C.2    Xu, Y.H.3    Wang, X.F.4    Li, Y.5    Shang, Y.6
  • 76
    • 77649251362 scopus 로고    scopus 로고
    • A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication
    • Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B. A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication. Proc Natl Acad Sci U S A 2010, 107:83900-83905.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 83900-83905
    • Meng, L.1    Wong, J.H.2    Feldman, L.J.3    Lemaux, P.G.4    Buchanan, B.B.5
  • 77
    • 55749086024 scopus 로고    scopus 로고
    • Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice
    • Campanella M.E., Chu H., Wandersee N.J., Peters L.L., Mohandas N., Gilligan D.M., et al. Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice. Blood 2008, 112:3900-3906.
    • (2008) Blood , vol.112 , pp. 3900-3906
    • Campanella, M.E.1    Chu, H.2    Wandersee, N.J.3    Peters, L.L.4    Mohandas, N.5    Gilligan, D.M.6
  • 78
    • 84861065569 scopus 로고    scopus 로고
    • Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation
    • Sirover M.A. Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J Cell Biochem 2012, 113(7):2193-2200.
    • (2012) J Cell Biochem , vol.113 , Issue.7 , pp. 2193-2200
    • Sirover, M.A.1
  • 79
    • 0019847313 scopus 로고
    • Membrane-bound ATP fuels the Na/K Pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes
    • Mercer R.W., Dunham P.B. Membrane-bound ATP fuels the Na/K Pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes. J Gen Physiol 1981, 78:547-568.
    • (1981) J Gen Physiol , vol.78 , pp. 547-568
    • Mercer, R.W.1    Dunham, P.B.2
  • 80
    • 77956969589 scopus 로고    scopus 로고
    • Proteins as nitrogen source for plants. A short story about exudation of proteases by plant roots
    • Adamczyk B., Smolander A., Kitunen V., Godlewski M. Proteins as nitrogen source for plants. A short story about exudation of proteases by plant roots. Plant Signal Behav 2010, 5(7):817-819.
    • (2010) Plant Signal Behav , vol.5 , Issue.7 , pp. 817-819
    • Adamczyk, B.1    Smolander, A.2    Kitunen, V.3    Godlewski, M.4
  • 81
    • 43249086785 scopus 로고    scopus 로고
    • Mammalian long-chain Acyl-CoA synthetases
    • Soupene E., Kuypers F.A. Mammalian long-chain Acyl-CoA synthetases. Exp Biol Med 2008, 233:507-521.
    • (2008) Exp Biol Med , vol.233 , pp. 507-521
    • Soupene, E.1    Kuypers, F.A.2
  • 82
    • 0035032341 scopus 로고    scopus 로고
    • Iron stress-induced changes in root epidermal cell fate are regulated independently from physiological responses to low iron availability
    • Schikora A., Schmidt W. Iron stress-induced changes in root epidermal cell fate are regulated independently from physiological responses to low iron availability. Plant Physiol 2001, 125:1679-1687.
    • (2001) Plant Physiol , vol.125 , pp. 1679-1687
    • Schikora, A.1    Schmidt, W.2
  • 83
    • 74249105661 scopus 로고    scopus 로고
    • Differential gene expression analysis provides new insights into the molecular basis of iron deficiency stress response in the citrus rootstock Poncirus trifoliata (L.) Raf
    • Forner-Giner M.A., Llosá M.J., Carrasco J.L., Pérez-Amador M.A., Navarro L., Ancillo G. Differential gene expression analysis provides new insights into the molecular basis of iron deficiency stress response in the citrus rootstock Poncirus trifoliata (L.) Raf. J Exp Bot 2010, 61:483-490.
    • (2010) J Exp Bot , vol.61 , pp. 483-490
    • Forner-Giner, M.A.1    Llosá, M.J.2    Carrasco, J.L.3    Pérez-Amador, M.A.4    Navarro, L.5    Ancillo, G.6
  • 84
    • 54149119002 scopus 로고    scopus 로고
    • The glycerophosphoryl diester phosphodiesterase-like proteins SHV3 and its homologs play important roles in cell wall organization
    • Hayashi S., Ishii T., Matsunaga T., Tominaga R., Kuromori T., Wada T., et al. The glycerophosphoryl diester phosphodiesterase-like proteins SHV3 and its homologs play important roles in cell wall organization. Plant Cell Physiol 2008, 49:1522-1535.
    • (2008) Plant Cell Physiol , vol.49 , pp. 1522-1535
    • Hayashi, S.1    Ishii, T.2    Matsunaga, T.3    Tominaga, R.4    Kuromori, T.5    Wada, T.6
  • 85
    • 0034130986 scopus 로고    scopus 로고
    • Dirigent proteins and dirigent sites explain the mystery of specificity of radical precursor coupling in lignan and lignin biosynthesis
    • Davin L.B., Lewis N.G. Dirigent proteins and dirigent sites explain the mystery of specificity of radical precursor coupling in lignan and lignin biosynthesis. Plant Physiol 2000, 123:453-461.
    • (2000) Plant Physiol , vol.123 , pp. 453-461
    • Davin, L.B.1    Lewis, N.G.2
  • 86
    • 27644498836 scopus 로고    scopus 로고
    • AtFLA11, a fasciclin-like arabinogalactan-protein, specifically localized in sclerenchyma cells
    • Ito S., Suzuki Y., Miyamoto K., Ueda J., Yamaguchi I. AtFLA11, a fasciclin-like arabinogalactan-protein, specifically localized in sclerenchyma cells. Biosci Biotechnol Biochem 2005, 69:1963-1969.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 1963-1969
    • Ito, S.1    Suzuki, Y.2    Miyamoto, K.3    Ueda, J.4    Yamaguchi, I.5
  • 87
    • 0141674963 scopus 로고    scopus 로고
    • Class I chitinase and β-1,3-glucanase are differentially regulated by wounding, methyl jasmonate, ethylene, and gibberellin in tomato seeds and leaves
    • Wu C.T., Bradford K.J. Class I chitinase and β-1,3-glucanase are differentially regulated by wounding, methyl jasmonate, ethylene, and gibberellin in tomato seeds and leaves. Plant Physiol 2003, 133:263-273.
    • (2003) Plant Physiol , vol.133 , pp. 263-273
    • Wu, C.T.1    Bradford, K.J.2
  • 88
    • 69949165706 scopus 로고    scopus 로고
    • Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry
    • Stokasimov E., Rubenstein P.A. Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry. J Biol Chem 2009, 284(37):25421-25430.
    • (2009) J Biol Chem , vol.284 , Issue.37 , pp. 25421-25430
    • Stokasimov, E.1    Rubenstein, P.A.2
  • 90
    • 77955653234 scopus 로고    scopus 로고
    • Investigating the role of plant heat shock proteins during oxidative stress
    • Scarpeci T.E., Zanor M.I., Valle E.M. Investigating the role of plant heat shock proteins during oxidative stress. Plant Signal Behav 2008, 3:856-857.
    • (2008) Plant Signal Behav , vol.3 , pp. 856-857
    • Scarpeci, T.E.1    Zanor, M.I.2    Valle, E.M.3
  • 91
    • 14844295427 scopus 로고    scopus 로고
    • AtNAP1 represents an atypical SufB protein in Arabidopsis plastids
    • Xu X.M., Adams S., Chua N.H., Møller S.G. AtNAP1 represents an atypical SufB protein in Arabidopsis plastids. J Biol Chem 2005, 280:6648-6654.
    • (2005) J Biol Chem , vol.280 , pp. 6648-6654
    • Xu, X.M.1    Adams, S.2    Chua, N.H.3    Møller, S.G.4
  • 92
    • 67651092036 scopus 로고    scopus 로고
    • Remorin, a Solanaceae protein resident in membrane rafts and plasmodesmata, impairs potato virus X movement
    • Raffaele S., Emmanuelle Bayer E., Lafarge D., Cluzet S., Retana S.G., Boubekeur T., et al. Remorin, a Solanaceae protein resident in membrane rafts and plasmodesmata, impairs potato virus X movement. Plant Cell 2009, 21:1541-1555.
    • (2009) Plant Cell , vol.21 , pp. 1541-1555
    • Raffaele, S.1    Emmanuelle Bayer, E.2    Lafarge, D.3    Cluzet, S.4    Retana, S.G.5    Boubekeur, T.6
  • 93
    • 78650669818 scopus 로고    scopus 로고
    • Perspectives on remorin proteins, membrane rafts, and their role during plant-microbe interactions
    • Jarsch I.K., Ott T. Perspectives on remorin proteins, membrane rafts, and their role during plant-microbe interactions. Mol Plant Microbe Interact 2011, 1:7-12.
    • (2011) Mol Plant Microbe Interact , vol.1 , pp. 7-12
    • Jarsch, I.K.1    Ott, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.