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Volumn 24, Issue 11, 2012, Pages 4465-4482

Protein-protein and protein-membrane associations in the lignin pathwayw oa

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; NICOTIANA BENTHAMIANA;

EID: 84871883667     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.112.102566     Document Type: Article
Times cited : (125)

References (81)
  • 1
    • 11144265587 scopus 로고    scopus 로고
    • Colocalization of L-phenylalanine ammonia-lyase and cin-namate 4-hydroxylase for metabolic channeling in phenylpropanoid biosynthesis
    • Achnine, L., Blancaflor, E.B., Rasmussen, S., and Dixon, R.A. (2004). Colocalization of L-phenylalanine ammonia-lyase and cin-namate 4-hydroxylase for metabolic channeling in phenylpropanoid biosynthesis. Plant Cell 16: 3098-3109.
    • (2004) Plant Cell , vol.16 , pp. 3098-3109
    • Achnine, L.1    Blancaflor, E.B.2    Rasmussen, S.3    Dixon, R.A.4
  • 2
    • 0037459094 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conforma-tional fluctuations
    • Azoulay, J., Clamme, J.P., Darlix, J.L., Roques, B.P., and Mély, Y. (2003). Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conforma-tional fluctuations. J. Mol. Biol. 326: 691-700.
    • (2003) J. Mol. Biol. , vol.326 , pp. 691-700
    • Azoulay, J.1    Clamme, J.P.2    Darlix, J.L.3    Roques, B.P.4    Mély, Y.5
  • 3
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes, W.L., and Kelley, R.W. (2003). Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol. Ther. 98: 221-233.
    • (2003) Pharmacol. Ther , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 4
    • 84860216728 scopus 로고    scopus 로고
    • A novel method for monitoring the localization of cytochromes P450 and other endoplasmic reticulum membrane associated proteins: A tool for investigating the formation of metabolons
    • Bassard, J.-E., Mutterer, J., Duval, F., and Werck-Reichhart, D. (2012). A novel method for monitoring the localization of cytochromes P450 and other endoplasmic reticulum membrane associated proteins: A tool for investigating the formation of metabolons. FEBS J. 279: 1576-1583.
    • (2012) FEBS J , vol.279 , pp. 1576-1583
    • Bassard, J.E.1    Mutterer, J.2    Duval, F.3    Werck-Reichhart, D.4
  • 5
    • 0037076392 scopus 로고    scopus 로고
    • Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks
    • Bayburt, T.H., and Sligar, S.G. (2002). Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks. Proc. Natl. Acad. Sci. USA 99: 6725-6730.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 6725-6730
    • Bayburt, T.H.1    Sligar, S.G.2
  • 6
    • 70349235411 scopus 로고    scopus 로고
    • The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3) converts cysteine-indole-3-acetonitrile to camalexin in the indole-3-acetonitrile metabolic network of Arabidopsis thaliana
    • Böttcher, C., Westphal, L., Schmotz, C., Prade, E., Scheel, D., and Glawischnig, E. (2009). The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3) converts cysteine-indole-3-acetonitrile to camalexin in the indole-3-acetonitrile metabolic network of Arabidopsis thaliana. Plant Cell 21: 1830-1845.
    • (2009) Plant Cell , vol.21 , pp. 1830-1845
    • Böttcher, C.1    Westphal, L.2    Schmotz, C.3    Prade, E.4    Scheel, D.5    Glawischnig, E.6
  • 7
    • 48549107461 scopus 로고    scopus 로고
    • Tobacco mosaic virus movement protein interacts with green fluorescent protein-tagged microtubule end-binding protein 1
    • Brandner, K., Sambade, A., Boutant, E., Didier, P., Mély, Y., Ritzenthaler, C., and Heinlein, M. (2008). Tobacco mosaic virus movement protein interacts with green fluorescent protein-tagged microtubule end-binding protein 1. Plant Physiol. 147: 611-623.
    • (2008) Plant Physiol , vol.147 , pp. 611-623
    • Brandner, K.1    Sambade, A.2    Boutant, E.3    Didier, P.4    Mély, Y.5    Ritzenthaler, C.6    Heinlein, M.7
  • 8
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman, D.T., Resek, M.E., Zajchowski, L.D., and Robbins, S.M. (2006). Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J. Cell Sci. 119: 3149-3160.
    • (2006) J. Cell Sci , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 10
    • 0036741602 scopus 로고    scopus 로고
    • The identification of CVP1 reveals a role for sterols in vascular patterning
    • Carland, F.M., Fujioka, S., Takatsuto, S., Yoshida, S., and Nelson, T. (2002). The identification of CVP1 reveals a role for sterols in vascular patterning. Plant Cell 14: 2045-2058.
    • (2002) Plant Cell , vol.14 , pp. 2045-2058
    • Carland, F.M.1    Fujioka, S.2    Takatsuto, S.3    Yoshida, S.4    Nelson, T.5
  • 11
    • 0035198219 scopus 로고    scopus 로고
    • Evidence supporting the interaction of CYP2B4 and CYP1A2 in microsomal preparations. Drug Metab
    • Cawley, G.F., Zhang, S., Kelley, R.W., and Backes, W.L. (2001). Evidence supporting the interaction of CYP2B4 and CYP1A2 in microsomal preparations. Drug Metab. Dispos. 29: 1529-1534.
    • (2001) Dispos , vol.29 , pp. 1529-1534
    • Cawley, G.F.1    Zhang, S.2    Kelley, R.W.3    Backes, W.L.4
  • 12
    • 84862908469 scopus 로고    scopus 로고
    • Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis
    • Chen, H.C., Li, Q., Shuford, C.M., Liu, J., Muddiman, D.C., Sederoff, R.R., and Chiang, V.L. (2011). Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis. Proc. Natl. Acad. Sci. USA 108: 21253-21258.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 21253-21258
    • Chen, H.C.1    Li, Q.2    Shuford, C.M.3    Liu, J.4    Muddiman, D.C.5    Sederoff, R.R.6    Chiang, V.L.7
  • 14
    • 24344488486 scopus 로고    scopus 로고
    • Characterization in vitro and in vivo of the putative multigene 4-coumarate:CoA ligase network in Arabidopsis: Syringyl lignin and sinapate/sinapyl alcohol derivative formation
    • Costa, M.A., et al. (2005). Characterization in vitro and in vivo of the putative multigene 4-coumarate:CoA ligase network in Arabidopsis: Syringyl lignin and sinapate/sinapyl alcohol derivative formation. Phytochemistry 66: 2072-2091.
    • (2005) Phytochemistry , vol.66 , pp. 2072-2091
    • Costa, M.A.1
  • 15
    • 0023142377 scopus 로고
    • Inhibition of action polymerization by latrunculin
    • Coué, M., Brenner, S.L., Spector, I., and Korn, E.D. (1987). Inhibition of action polymerization by latrunculin A. FEBS Lett. 213: 316-318.
    • (1987) A. FEBS Lett , vol.213 , pp. 316-318
    • Coué, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 16
    • 0001312365 scopus 로고
    • Formation of p-coumaric acid and o-coumaric acid from L-phenylalanine by microsomal membrane fractions from potato: Evidence of membrane-bound enzyme complexes
    • Czichi, U., and Kindl, H. (1975). Formation of p-coumaric acid and o-coumaric acid from L-phenylalanine by microsomal membrane fractions from potato: Evidence of membrane-bound enzyme complexes. Planta 125: 115-125.
    • (1975) Planta , vol.125 , pp. 115-125
    • Czichi, U.1    Kindl, H.2
  • 17
    • 0000521129 scopus 로고
    • Phenylalanine ammonia-lyase and cinnamic acid hydroxylase as assembled consecutive enzymes on microsomal membranes of cucumber cotyledons: Cooperation and subcellular distribution
    • Czichi, U., and Kindl, H. (1977). Phenylalanine ammonia-lyase and cinnamic acid hydroxylase as assembled consecutive enzymes on microsomal membranes of cucumber cotyledons: Cooperation and subcellular distribution. Planta 134: 133-143.
    • (1977) Planta , vol.134 , pp. 133-143
    • Czichi, U.1    Kindl, H.2
  • 18
    • 0027332736 scopus 로고
    • A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding
    • Davletov, B.A., and Südhof, T.C. (1993). A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. J. Biol. Chem. 268: 26386-26390.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26386-26390
    • Davletov, B.A.1    Südhof, T.C.2
  • 19
    • 27144459868 scopus 로고    scopus 로고
    • Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization
    • Davydov, D.R., Fernando, H., Baas, B.J., Sligar, S.G., and Halpert, J.R. (2005). Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization. Biochemistry 44: 13902-13913.
    • (2005) Biochemistry , vol.44 , pp. 13902-13913
    • Davydov, D.R.1    Fernando, H.2    Baas, B.J.3    Sligar, S.G.4    Halpert, J.R.5
  • 20
    • 0034610011 scopus 로고    scopus 로고
    • Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy
    • Davydov, D.R., Petushkova, N.A., Archakov, A.I., and Hoa, G.H. (2000). Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy. Biochem. Biophys. Res. Commun. 276: 1005-1012.
    • (2000) Biochem. Biophys. Res. Commun , vol.276 , pp. 1005-1012
    • Davydov, D.R.1    Petushkova, N.A.2    Archakov, A.I.3    Hoa, G.H.4
  • 21
    • 0033582147 scopus 로고    scopus 로고
    • A cytochrome b5 is required for full activity of flavonoid 39,59-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors
    • de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J., and Koes, R. (1999). A cytochrome b5 is required for full activity of flavonoid 39,59-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96: 778-783.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 778-783
    • de Vetten, N.1    Ter, H.J.2    van Schaik, H.P.3    de Boer, A.4    Mol, J.5    Koes, R.6
  • 22
    • 0037240794 scopus 로고    scopus 로고
    • The resident endoplasmic reticulum protein, BAP31, associates with gamma-action and myosin B heavy chain
    • Ducret, A., Nguyen, M., Breckenridge, D.G., and Shore, G.C. (2003). The resident endoplasmic reticulum protein, BAP31, associates with gamma-action and myosin B heavy chain. Eur. J. Bio-chem. 270: 342-349.
    • (2003) Eur. J. Bio-chem , vol.270 , pp. 342-349
    • Ducret, A.1    Nguyen, M.2    Breckenridge, D.G.3    Shore, G.C.4
  • 23
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting, J., Büttner, D., Wang, Q., Douglas, C.J., Somssich, I.E., and Kombrink, E. (1999). Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J. 19: 9-20.
    • (1999) Plant J , vol.19 , pp. 9-20
    • Ehlting, J.1    Büttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 24
    • 0034788886 scopus 로고    scopus 로고
    • Identification of 4-coumarate:Coenzyme A ligase (4CL) substrate recognition domains
    • Ehlting, J., Shin, J.J., and Douglas, C.J. (2001). Identification of 4-coumarate:coenzyme A ligase (4CL) substrate recognition domains. Plant J. 27: 455-465.
    • (2001) Plant J , vol.27 , pp. 455-465
    • Ehlting, J.1    Shin, J.J.2    Douglas, C.J.3
  • 25
    • 34249854159 scopus 로고    scopus 로고
    • USER fusion: A rapid and efficient method for simultaneous fusion and cloning of multiple PCR products
    • Geu-Flores, F., Nour-Eldin, H.H., Nielsen, M.T., and Halkier, B.A. (2007). USER fusion: A rapid and efficient method for simultaneous fusion and cloning of multiple PCR products. Nucleic Acids Res. 35: e55.
    • (2007) Nucleic Acids Res. , vol.35
    • Geu-Flores, F.1    Nour-Eldin, H.H.2    Nielsen, M.T.3    Halkier, B.A.4
  • 27
    • 77955890410 scopus 로고    scopus 로고
    • Networking in the endoplasmic reticulum
    • Griffing, L.R. (2010). Networking in the endoplasmic reticulum. Bio-chem. Soc. Trans. 38: 747-753.
    • (2010) Bio-chem. Soc. Trans , vol.38 , pp. 747-753
    • Griffing, L.R.1
  • 28
    • 1242296765 scopus 로고    scopus 로고
    • The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapate-activating and three commonly occurring isoenzymes
    • Hamberger, B., and Hahlbrock, K. (2004). The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapate-activating and three commonly occurring isoenzymes. Proc. Natl. Acad. Sci. USA 101: 2209-2214.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 2209-2214
    • Hamberger, B.1    Hahlbrock, K.2
  • 29
    • 11144328243 scopus 로고    scopus 로고
    • Interactions between CYP2C9 and CYP2C19 in reconstituted binary systems influence their catalytic activity: Possible rationale for the inability of CYP2C19 to catalyze methoxychlor demethylation in human liver microsomes
    • Hazai, E., and Kupfer, D. (2005). Interactions between CYP2C9 and CYP2C19 in reconstituted binary systems influence their catalytic activity: Possible rationale for the inability of CYP2C19 to catalyze methoxychlor demethylation in human liver microsomes. Drug Metab. Dispos. 33: 157-164.
    • (2005) Drug Metab. Dispos , vol.33 , pp. 157-164
    • Hazai, E.1    Kupfer, D.2
  • 30
    • 0008251657 scopus 로고    scopus 로고
    • Wound-induced lignin and su-berin deposition in a woody angiosperm (Eucalyptus gunnii Hook.): Histochemistry of early changes in young plants
    • Hawkins, S., and Boudet, A. (1996). Wound-induced lignin and su-berin deposition in a woody angiosperm (Eucalyptus gunnii Hook.): Histochemistry of early changes in young plants. Protoplasma 191: 96-104.
    • (1996) Protoplasma , vol.191 , pp. 96-104
    • Hawkins, S.1    Boudet, A.2
  • 31
    • 65549153205 scopus 로고    scopus 로고
    • Distinct regions within the erlins are required for oligo-merization and association with high molecular weight complexes
    • Hoegg, M.B., Browman, D.T., Resek, M.E., and Robbins, S.M. (2009). Distinct regions within the erlins are required for oligo-merization and association with high molecular weight complexes. J. Biol. Chem. 284: 7766-7776.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7766-7776
    • Hoegg, M.B.1    Browman, D.T.2    Resek, M.E.3    Robbins, S.M.4
  • 32
    • 2942633712 scopus 로고    scopus 로고
    • Silencing of hydroxy-cinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis
    • Hoffmann, L., Besseau, S., Geoffroy, P., Ritzenthaler, C., Meyer, D., Lapierre, C., Pollet, B., and Legrand, M. (2004). Silencing of hydroxy-cinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis. Plant Cell 16: 1446-1465.
    • (2004) Plant Cell , vol.16 , pp. 1446-1465
    • Hoffmann, L.1    Besseau, S.2    Geoffroy, P.3    Ritzenthaler, C.4    Meyer, D.5    Lapierre, C.6    Pollet, B.7    Legrand, M.8
  • 33
    • 0037414824 scopus 로고    scopus 로고
    • Purification, cloning, and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenyl-propanoid metabolism
    • Hoffmann, L., Maury, S., Martz, F., Geoffroy, P., and Legrand, M. (2003). Purification, cloning, and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenyl-propanoid metabolism. J. Biol. Chem. 278: 95-103.
    • (2003) J. Biol. Chem. , vol.278 , pp. 95-103
    • Hoffmann, L.1    Maury, S.2    Martz, F.3    Geoffroy, P.4    Legrand, M.5
  • 34
    • 0022425458 scopus 로고
    • Metabolic pathways as enzyme complexes: Evidence for the synthesis of phenylpropanoids and flavonoids on membrane associated enzyme complexes. Arch. Biochem
    • Hrazdina, G., and Wagner, G.J. (1985). Metabolic pathways as enzyme complexes: Evidence for the synthesis of phenylpropanoids and flavonoids on membrane associated enzyme complexes. Arch. Biochem. Biophys. 237: 88-100.
    • (1985) Biophys , vol.237 , pp. 88-100
    • Hrazdina, G.1    Wagner, G.J.2
  • 35
    • 78049388318 scopus 로고    scopus 로고
    • CYP2C8 exists as a dimer in natural membranes
    • Hu, G., Johnson, E.F., and Kemper, B. (2010). CYP2C8 exists as a dimer in natural membranes. Drug Metab. Dispos. 38: 1976-1983.
    • (2010) Drug Metab. Dispos , vol.38 , pp. 1976-1983
    • Hu, G.1    Johnson, E.F.2    Kemper, B.3
  • 36
    • 80053634615 scopus 로고    scopus 로고
    • Homology modeling of the three membrane proteins of the dhurrin metabolon: Catalytic sites, membrane surface association and protein-protein interactions
    • Jensen, K., Osmani, S.A., Hamann, T., Naur, P., and Møller, B.L. (2011). Homology modeling of the three membrane proteins of the dhurrin metabolon: Catalytic sites, membrane surface association and protein-protein interactions. Phytochemistry 72: 2113-2123.
    • (2011) Phytochemistry , vol.72 , pp. 2113-2123
    • Jensen, K.1    Osmani, S.A.2    Hamann, T.3    Naur, P.4    Møller, B.L.5
  • 38
    • 33845538326 scopus 로고    scopus 로고
    • A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation
    • Kumar, R., Wallis, J.G., Skidmore, C., and Browse, J. (2006). A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation. Plant J. 48: 920-932.
    • (2006) Plant J , vol.48 , pp. 920-932
    • Kumar, R.1    Wallis, J.G.2    Skidmore, C.3    Browse, J.4
  • 39
    • 79960770015 scopus 로고    scopus 로고
    • Identification of cytochrome P450 2C2 protein complexes in mouse liver
    • Li, B., Yau, P., and Kemper, B. (2011). Identification of cytochrome P450 2C2 protein complexes in mouse liver. Proteomics 11: 3359-3368.
    • (2011) Proteomics , vol.11 , pp. 3359-3368
    • Li, B.1    Yau, P.2    Kemper, B.3
  • 40
    • 24344479212 scopus 로고    scopus 로고
    • Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex
    • Mo, C., and Bard, M. (2005). Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex. J. Lipid Res. 46: 1991-1998.
    • (2005) J. Lipid Res , vol.46 , pp. 1991-1998
    • Mo, C.1    Bard, M.2
  • 41
    • 7444226466 scopus 로고    scopus 로고
    • The ERG28-encoded protein, Erg28p, interacts with both the sterol C-4 demethylation enzyme complex as well as the late biosynthetic protein, the C-24 sterol methyltransferase (Erg6p)
    • Mo, C., Valachovic, M., and Bard, M. (2004). The ERG28-encoded protein, Erg28p, interacts with both the sterol C-4 demethylation enzyme complex as well as the late biosynthetic protein, the C-24 sterol methyltransferase (Erg6p). Biochim. Biophys. Acta 1686: 30-36.
    • (2004) Biochim. Biophys. Acta , vol.1686 , pp. 30-36
    • Mo, C.1    Valachovic, M.2    Bard, M.3
  • 42
    • 77952935279 scopus 로고    scopus 로고
    • Abiotic and biotic stresses and changes in the lignin content and composition in plants
    • Moura, J.C., Bonine, C.A., de Oliveira Fernandes Viana, J., Dornelas, M.C., and Mazzafera, P. (2010). Abiotic and biotic stresses and changes in the lignin content and composition in plants. J. Integr. Plant Biol. 52: 360-376.
    • (2010) J. Integr. Plant Biol , vol.52 , pp. 360-376
    • Moura, J.C.1    Bonine, C.A.2    De, O.F.3    Viana, J.4    Dornelas, M.C.5    Mazzafera, P.6
  • 43
    • 0025046798 scopus 로고
    • Immobilized cytochrome P-450LM2. Dissociation and reassociation of oligomers
    • Myasoedova, K.N., and Berndt, P. (1990). Immobilized cytochrome P-450LM2. Dissociation and reassociation of oligomers. FEBS Lett. 270: 177-180.
    • (1990) FEBS Lett , vol.270 , pp. 177-180
    • Myasoedova, K.N.1    Berndt, P.2
  • 44
    • 0036742670 scopus 로고    scopus 로고
    • Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast
    • Nair, R.B., Xia, Q., Kartha, C.J., Kurylo, E., Hirji, R.N., Datla, R., and Selvaraj, G. (2002). Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast. Plant Physiol. 130: 210-220.
    • (2002) Plant Physiol , vol.130 , pp. 210-220
    • Nair, R.B.1    Xia, Q.2    Kartha, C.J.3    Kurylo, E.4    Hirji, R.N.5    Datla, R.6    Selvaraj, G.7
  • 45
  • 46
    • 60149110302 scopus 로고    scopus 로고
    • Functions of reticulons in plants: What we can learn from animals and yeasts
    • Nziengui, H., and Schoefs, B. (2009). Functions of reticulons in plants: What we can learn from animals and yeasts. Cell. Mol. Life Sci. 66: 584-595.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 584-595
    • Nziengui, H.1    Schoefs, B.2
  • 47
    • 20444438444 scopus 로고    scopus 로고
    • Regulation of secondary cell wall development by cortical microtubules during tra-cheary element differentiation in Arabidopsis cell suspensions
    • Oda, Y., Mimura, T., and Hasezawa, S. (2005). Regulation of secondary cell wall development by cortical microtubules during tra-cheary element differentiation in Arabidopsis cell suspensions. Plant Physiol. 137: 1027-1036.
    • (2005) Plant Physiol , vol.137 , pp. 1027-1036
    • Oda, Y.1    Mimura, T.2    Hasezawa, S.3
  • 48
    • 23944462892 scopus 로고    scopus 로고
    • Bi-molecular fluorescence complementation analysis of cytochrome p450 2c2, 2e1, and NADPH-cytochrome p450 reductase molecular interactions in living cells
    • Ozalp, C., Szczesna-Skorupa, E., and Kemper, B. (2005). Bi-molecular fluorescence complementation analysis of cytochrome p450 2c2, 2e1, and NADPH-cytochrome p450 reductase molecular interactions in living cells. Drug Metab. Dispos. 33: 1382-1390.
    • (2005) Drug Metab. Dispos , vol.33 , pp. 1382-1390
    • Ozalp, C.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 49
    • 0017112947 scopus 로고
    • Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 reductase: Cytochrome P-450 interaction
    • Peterson, J.A., Ebel, R.E., O'Keeffe, D.H., Matsubara, T., and Estabrook, R.W. (1976). Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 reductase: cytochrome P-450 interaction. J. Biol. Chem. 251: 4010-4016.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4010-4016
    • Peterson, J.A.1    Ebel, R.E.2    O'Keeffe, D.H.3    Matsubara, T.4    Estabrook, R.W.5
  • 50
    • 70450248395 scopus 로고    scopus 로고
    • Organization of cytochrome P450 enzymes involved in sex steroid synthesis: Protein-Protein Interactions in Lipid Membranes
    • Praporski, S., Ng, S.M., Nguyen, A.D., Corbin, C.J., Mechler, A., Zheng, J., Conley, A.J., and Martin, L.L. (2009). Organization of cytochrome P450 enzymes involved in sex steroid synthesis: Protein-Protein Interactions in Lipid Membranes. J. Biol. Chem. 284: 33224-33232.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33224-33232
    • Praporski, S.1    Ng, S.M.2    Nguyen, A.D.3    Corbin, C.J.4    Mechler, A.5    Zheng, J.6    Conley, A.J.7    Martin, L.L.8
  • 51
    • 33845452245 scopus 로고    scopus 로고
    • Metabolons involving plant cyto-chrome P450
    • Ralston, L., and Yu, O. (2006). Metabolons involving plant cyto-chrome P450. Phytochem. Rev. 5: 459-472.
    • (2006) Phytochem. Rev. , vol.5 , pp. 459-472
    • Ralston, L.1    Yu, O.2
  • 52
    • 0032725627 scopus 로고    scopus 로고
    • Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway
    • Rasmussen, S., and Dixon, R.A. (1999). Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway. Plant Cell 11: 1537-1552.
    • (1999) Plant Cell , vol.11 , pp. 1537-1552
    • Rasmussen, S.1    Dixon, R.A.2
  • 53
    • 84856488429 scopus 로고    scopus 로고
    • Formation of P450 $ P450 complexes and their effect on P450 function
    • Reed, J.R., and Backes, W.L. (2012). Formation of P450 $ P450 complexes and their effect on P450 function. Pharmacol. Ther. 133: 299-310.
    • (2012) Pharmacol. Ther , vol.133 , pp. 299-310
    • Reed, J.R.1    Backes, W.L.2
  • 54
    • 1642576078 scopus 로고    scopus 로고
    • Reconstitution of the entry point of plant phenylpropanoid metabolism in yeast (Saccharomyces cerevisiae): Implications for control of metabolic flux into the phe-nylpropanoid pathway
    • Ro, D.K., and Douglas, C.J. (2004). Reconstitution of the entry point of plant phenylpropanoid metabolism in yeast (Saccharomyces cerevisiae): Implications for control of metabolic flux into the phe-nylpropanoid pathway. J. Biol. Chem. 279: 2600-2607.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2600-2607
    • Ro, D.K.1    Douglas, C.J.2
  • 55
    • 29344456761 scopus 로고    scopus 로고
    • Photo-activation of GFP reveals protein dynamics within the endoplasmic reticulum membrane
    • Runions, J., Brach, T., Kühner, S., and Hawes, C. (2006). Photo-activation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J. Exp. Bot. 57: 43-50.
    • (2006) J. Exp. Bot. , vol.57 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kühner, S.3    Hawes, C.4
  • 56
    • 66249114650 scopus 로고    scopus 로고
    • The targeting of the oxysterol-binding protein ORP3a to the endoplasmic reticulum relies on the plant VAP33 homolog PVA12
    • Saravanan, R.S., Slabaugh, E., Singh, V.R., Lapidus, L.J., Haas, T., and Brandizzi, F. (2009). The targeting of the oxysterol-binding protein ORP3a to the endoplasmic reticulum relies on the plant VAP33 homolog PVA12. Plant J. 58: 817-830.
    • (2009) Plant J , vol.58 , pp. 817-830
    • Saravanan, R.S.1    Slabaugh, E.2    Singh, V.R.3    Lapidus, L.J.4    Haas, T.5    Brandizzi, F.6
  • 57
    • 0035049995 scopus 로고    scopus 로고
    • The ratio of campesterol to sitosterol that modulates growth in Arabidopsis is controlled by Sterol Methyltransferase 2;1
    • Schaeffer, A., Bronner, R., Benveniste, P., and Schaller, H. (2001). The ratio of campesterol to sitosterol that modulates growth in Arabidopsis is controlled by Sterol Methyltransferase 2;1. Plant J. 25: 605-615.
    • (2001) Plant J , vol.25 , pp. 605-615
    • Schaeffer, A.1    Bronner, R.2    Benveniste, P.3    Schaller, H.4
  • 58
    • 0030725702 scopus 로고    scopus 로고
    • Design of fluorescent substrates and potent inhibitors of CYP73As, P450s that catalyze 4-hydroxylation of cinnamic acid in higher plants
    • Schalk, M., Batard, Y., Seyer, A., Nedelkina, S., Durst, F., and Werck-Reichhart, D. (1997). Design of fluorescent substrates and potent inhibitors of CYP73As, P450s that catalyze 4-hydroxylation of cinnamic acid in higher plants. Biochemistry 36: 15253-15261.
    • (1997) Biochemistry , vol.36 , pp. 15253-15261
    • Schalk, M.1    Batard, Y.2    Seyer, A.3    Nedelkina, S.4    Durst, F.5    Werck-Reichhart, D.6
  • 59
    • 0037306331 scopus 로고    scopus 로고
    • The many roles of cyto-chrome b5
    • Schenkman, J.B., and Jansson, I. (2003). The many roles of cyto-chrome b5. Pharmacol. Ther. 97: 139-152.
    • (2003) Pharmacol. Ther , vol.97 , pp. 139-152
    • Schenkman, J.B.1    Jansson, I.2
  • 60
    • 0035965253 scopus 로고    scopus 로고
    • CYP98A3 from Arabidopsis thaliana is a 39-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway
    • Schoch, G., Goepfert, S., Morant, M., Hehn, A., Meyer, D., Ullmann, P., and Werck-Reichhart, D. (2001). CYP98A3 from Arabidopsis thaliana is a 39-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276: 36566-36574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3    Hehn, A.4    Meyer, D.5    Ullmann, P.6    Werck-Reichhart, D.7
  • 62
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cyto-chrome P450 2C8. Evidence for a peripheral fatty acid binding site
    • Schoch, G.A., Yano, J.K., Wester, M.R., Griffin, K.J., Stout, C.D., and Johnson, E.F. (2004). Structure of human microsomal cyto-chrome P450 2C8. Evidence for a peripheral fatty acid binding site. J. Biol. Chem. 279: 9497-9503.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 66
    • 83055181408 scopus 로고    scopus 로고
    • FrontiERs: Movers and shapers of the higher plant cortical endoplasmic reticulum
    • Sparkes, I., Hawes, C., and Frigerio, L. (2011). FrontiERs: Movers and shapers of the higher plant cortical endoplasmic reticulum. Curr. Opin. Plant Biol. 14: 658-665.
    • (2011) Curr. Opin. Plant Biol. , vol.14 , pp. 658-665
    • Sparkes, I.1    Hawes, C.2    Frigerio, L.3
  • 67
    • 77953177103 scopus 로고    scopus 로고
    • Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties
    • Sparkes, I., Tolley, N., Aller, I., Svozil, J., Osterrieder, A., Botchway, S., Mueller, C., Frigerio, L., and Hawes, C. (2010). Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 22: 1333-1343.
    • (2010) Plant Cell , vol.22 , pp. 1333-1343
    • Sparkes, I.1    Tolley, N.2    Aller, I.3    Svozil, J.4    Osterrieder, A.5    Botchway, S.6    Mueller, C.7    Frigerio, L.8    Hawes, C.9
  • 69
  • 70
    • 0016736883 scopus 로고
    • Chemical synthesis and properties of hydroxycinnamoyl coenzyme A derivatives
    • Stöckigt, J., and Zenk, M.H. (1975). Chemical synthesis and properties of hydroxycinnamoyl coenzyme A derivatives. Z. Naturforsch. C 30c: 352-358.
    • (1975) Z. Naturforsch. C , vol.30 c , pp. 352-358
    • Stöckigt, J.1    Zenk, M.H.2
  • 71
    • 77952304154 scopus 로고    scopus 로고
    • CYP2C9-CYP3A4 protein-protein interactions: Role of the hydro-phobic N terminus
    • Subramanian, M., Tam, H., Zheng, H., and Tracy, T.S. (2010). CYP2C9-CYP3A4 protein-protein interactions: Role of the hydro-phobic N terminus. Drug Metab. Dispos. 38: 1003-1009.
    • (2010) Drug Metab. Dispos , vol.38 , pp. 1003-1009
    • Subramanian, M.1    Tam, H.2    Zheng, H.3    Tracy, T.S.4
  • 72
    • 0032437596 scopus 로고    scopus 로고
    • Mobility of cytochrome P450 in the endoplasmic reticulum membrane
    • Szczesna-Skorupa, E., Chen, C.D., Rogers, S., and Kemper, B. (1998). Mobility of cytochrome P450 in the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA 95: 14793-14798.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 14793-14798
    • Szczesna-Skorupa, E.1    Chen, C.D.2    Rogers, S.3    Kemper, B.4
  • 73
    • 33645219173 scopus 로고    scopus 로고
    • BAP31 is involved in the retention of cytochrome P450 2C2 in the endoplasmic re-ticulum
    • Szczesna-Skorupa, E., and Kemper, B. (2006). BAP31 is involved in the retention of cytochrome P450 2C2 in the endoplasmic re-ticulum. J. Biol. Chem. 281: 4142-4148.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4142-4148
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 74
    • 0043234255 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cytochromes P450 2C2 and 2E1 molecular interactions in living cells
    • Szczesna-Skorupa, E., Mallah, B., and Kemper, B. (2003). Fluorescence resonance energy transfer analysis of cytochromes P450 2C2 and 2E1 molecular interactions in living cells. J. Biol. Chem. 278: 31269-31276.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31269-31276
    • Szczesna-Skorupa, E.1    Mallah, B.2    Kemper, B.3
  • 75
    • 78149447878 scopus 로고    scopus 로고
    • Transmembrane domain length is responsible for the ability of a plant reticulon to shape endoplasmic reticulum tubules in vivo
    • Tolley, N., Sparkes, I., Craddock, C.P., Eastmond, P.J., Runions, J., Hawes, C., and Frigerio, L. (2010). Transmembrane domain length is responsible for the ability of a plant reticulon to shape endoplasmic reticulum tubules in vivo. Plant J. 64: 411-418.
    • (2010) Plant J , vol.64 , pp. 411-418
    • Tolley, N.1    Sparkes, I.2    Craddock, C.P.3    Eastmond, P.J.4    Runions, J.5    Hawes, C.6    Frigerio, L.7
  • 76
    • 77955608634 scopus 로고    scopus 로고
    • Targeted interactomics reveals a complex core cell cycle machinery in Arabidopsis thaliana
    • Van Leene, J., et al. (2010). Targeted interactomics reveals a complex core cell cycle machinery in Arabidopsis thaliana. Mol. Syst. Biol. 6: 397.
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 397
    • van Leene, J.1
  • 77
    • 34547137389 scopus 로고    scopus 로고
    • A tandem affinity purification-based technology platform to study the cell cycle interactome in Arabi-dopsis thaliana
    • Van Leene, J., et al. (2007). A tandem affinity purification-based technology platform to study the cell cycle interactome in Arabi-dopsis thaliana. Mol. Cell. Proteomics 6: 1226-1238.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1226-1238
    • van Leene, J.1
  • 78
    • 53149142072 scopus 로고    scopus 로고
    • Boosting tandem affinity purification of plant protein complexes
    • Van Leene, J., Witters, E., Inzé, D., and De Jaeger, G. (2008). Boosting tandem affinity purification of plant protein complexes. Trends Plant Sci. 13: 517-520.
    • (2008) Trends Plant Sci. , vol.13 , pp. 517-520
    • van Leene, J.1    Witters, E.2    Inzé, D.3    de Jaeger, G.4
  • 79
    • 76549093442 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis
    • Vogt, T. (2010). Phenylpropanoid biosynthesis. Mol. Plant 3: 2-20.
    • (2010) Mol. Plant , vol.3 , pp. 2-20
    • Vogt, T.1
  • 80
    • 3242655621 scopus 로고    scopus 로고
    • Metabolic channeling in plants
    • Winkel, B.S. (2004). Metabolic channeling in plants. Annu. Rev. Plant Biol. 55: 85-107.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 85-107
    • Winkel, B.S.1
  • 81
    • 26944463131 scopus 로고    scopus 로고
    • Arabidopsis membrane steroid binding protein 1 is involved in inhibition of cell elongation
    • Yang, X.H., Xu, Z.H., and Xue, H.W. (2005). Arabidopsis membrane steroid binding protein 1 is involved in inhibition of cell elongation. Plant Cell 17: 116-131.
    • (2005) Plant Cell , vol.17 , pp. 116-131
    • Yang, X.H.1    Xu, Z.H.2    Xue, H.W.3


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