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Volumn 11, Issue 3, 2006, Pages 124-132

Chewing the fat: β-oxidation in signalling and development

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID BETA OXIDATION MULTIENZYME COMPLEX; FATTY ACID BETA-OXIDATION MULTIENZYME COMPLEX; MULTIENZYME COMPLEX;

EID: 31844443844     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2006.01.005     Document Type: Review
Times cited : (221)

References (71)
  • 1
    • 0014670256 scopus 로고
    • β-oxidation in glyoxysomes from castor bean endosperm
    • T.G. Cooper, and H. Beevers β-oxidation in glyoxysomes from castor bean endosperm J. Biol. Chem. 244 1969 3515 3520
    • (1969) J. Biol. Chem. , vol.244 , pp. 3515-3520
    • Cooper, T.G.1    Beevers, H.2
  • 2
    • 0001592899 scopus 로고
    • Metabolic production of sucrose from fat
    • H. Beevers Metabolic production of sucrose from fat Nature 191 1961 433 436
    • (1961) Nature , vol.191 , pp. 433-436
    • Beevers, H.1
  • 3
    • 0036138649 scopus 로고    scopus 로고
    • Pathways of straight and branched chain fatty acid catabolism in higher plants
    • I.A. Graham, and P.J. Eastmond Pathways of straight and branched chain fatty acid catabolism in higher plants Prog. Lipid Res. 41 2002 156 181
    • (2002) Prog. Lipid Res. , vol.41 , pp. 156-181
    • Graham, I.A.1    Eastmond, P.J.2
  • 4
    • 0037124376 scopus 로고    scopus 로고
    • Control of germination and lipid mobilization by COMATOSE, the Arabidopsis homologue of human ALDP
    • S. Footitt Control of germination and lipid mobilization by COMATOSE, the Arabidopsis homologue of human ALDP EMBO J. 21 2002 2912 2922
    • (2002) EMBO J. , vol.21 , pp. 2912-2922
    • Footitt, S.1
  • 5
    • 0036008342 scopus 로고    scopus 로고
    • Ped3p is a peroxisomal ATP-binding cassette transporter that might supply substrates for fatty acid beta-oxidation
    • M. Hayashi Ped3p is a peroxisomal ATP-binding cassette transporter that might supply substrates for fatty acid beta-oxidation Plant Cell Physiol. 43 2002 1 11
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1-11
    • Hayashi, M.1
  • 6
    • 0035201037 scopus 로고    scopus 로고
    • The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid beta-oxidation
    • B.K. Zolman The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid beta-oxidation Plant Physiol. 127 2001 1266 1278
    • (2001) Plant Physiol. , vol.127 , pp. 1266-1278
    • Zolman, B.K.1
  • 7
    • 1042279122 scopus 로고    scopus 로고
    • Peroxisomal acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana
    • M. Fulda Peroxisomal acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana Plant Cell 16 2004 394 405
    • (2004) Plant Cell , vol.16 , pp. 394-405
    • Fulda, M.1
  • 8
    • 0034602157 scopus 로고    scopus 로고
    • Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination
    • P.J. Eastmond Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination J. Biol. Chem. 275 2000 34375 34381
    • (2000) J. Biol. Chem. , vol.275 , pp. 34375-34381
    • Eastmond, P.J.1
  • 9
    • 0034126739 scopus 로고    scopus 로고
    • ACX3, a novel medium-chain acyl-coenzyme a oxidase from Arabidopsis
    • B.E. Froman ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis Plant Physiol. 123 2000 733 742
    • (2000) Plant Physiol. , vol.123 , pp. 733-742
    • Froman, B.E.1
  • 10
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • H. Hayashi A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes J. Biol. Chem. 274 1999 12715 12721
    • (1999) J. Biol. Chem. , vol.274 , pp. 12715-12721
    • Hayashi, H.1
  • 11
    • 0033213084 scopus 로고    scopus 로고
    • Long-chain acyl-CoA oxidases of Arabidopsis
    • M.A. Hooks Long-chain acyl-CoA oxidases of Arabidopsis Plant J. 20 1999 1 13
    • (1999) Plant J. , vol.20 , pp. 1-13
    • Hooks, M.A.1
  • 12
    • 0038691611 scopus 로고    scopus 로고
    • Arabidopsis mutants in short and medium chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid β-oxidation is essential for embryo development
    • E.L. Rylott Arabidopsis mutants in short and medium chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid β-oxidation is essential for embryo development J. Biol. Chem. 278 2003 21370 21377
    • (2003) J. Biol. Chem. , vol.278 , pp. 21370-21377
    • Rylott, E.L.1
  • 13
    • 15544374294 scopus 로고    scopus 로고
    • Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation
    • A.R. Adham Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation Plant J. 41 2005 859 874
    • (2005) Plant J. , vol.41 , pp. 859-874
    • Adham, A.R.1
  • 14
    • 32944459159 scopus 로고    scopus 로고
    • Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism
    • H. Pinfield-Wells Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism Plant J. 43 2005 861 872
    • (2005) Plant J. , vol.43 , pp. 861-872
    • Pinfield-Wells, H.1
  • 15
    • 0033977040 scopus 로고    scopus 로고
    • The multifunctional protein AtMFP2 is co-ordinately expressed with other genes of fatty acid β-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh
    • P.J. Eastmond, and I.A. Graham The multifunctional protein AtMFP2 is co-ordinately expressed with other genes of fatty acid β-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh Biochem. Soc. Trans. 28 2000 95 99
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 95-99
    • Eastmond, P.J.1    Graham, I.A.2
  • 16
    • 0033212993 scopus 로고    scopus 로고
    • A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis
    • T.A. Richmond, and A.B. Bleecker A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis Plant Cell 11 1999 1911 1923
    • (1999) Plant Cell , vol.11 , pp. 1911-1923
    • Richmond, T.A.1    Bleecker, A.B.2
  • 17
    • 0034782175 scopus 로고    scopus 로고
    • Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
    • V. Germain Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings Plant J. 28 2001 1 12
    • (2001) Plant J. , vol.28 , pp. 1-12
    • Germain, V.1
  • 18
    • 0032004229 scopus 로고    scopus 로고
    • 2,4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid beta-oxidation
    • M. Hayashi 2,4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid beta-oxidation Plant Cell 10 1998 183 195
    • (1998) Plant Cell , vol.10 , pp. 183-195
    • Hayashi, M.1
  • 19
    • 30944458289 scopus 로고    scopus 로고
    • Molecular identification and characterization of the Arabidopsis Δ 3,5,Δ2,4-dienoyl-coenzyme a isomerase, a peroxisomal enzyme participating in the β-oxidation cycle of unsaturated fatty acids
    • S. Goepfert Molecular identification and characterization of the Arabidopsis Δ 3,5,Δ2,4-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the β-oxidation cycle of unsaturated fatty acids Plant Physiol. 138 2005 1947 1956
    • (2005) Plant Physiol. , vol.138 , pp. 1947-1956
    • Goepfert, S.1
  • 20
    • 0029783210 scopus 로고    scopus 로고
    • The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae
    • E. Hettema The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae EMBO J. 15 1996 3813 3822
    • (1996) EMBO J. , vol.15 , pp. 3813-3822
    • Hettema, E.1
  • 21
    • 0034820746 scopus 로고    scopus 로고
    • Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant
    • Y. Hayashi Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant Protoplasma 218 2001 83 94
    • (2001) Protoplasma , vol.218 , pp. 83-94
    • Hayashi, Y.1
  • 22
    • 33644858538 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana mutants in the multifunctional protein (MFP2) of β-oxidation during early post-germinative seedling growth
    • in press
    • Rylott, E.L. et al. Characterization of Arabidopsis thaliana mutants in the multifunctional protein (MFP2) of β-oxidation during early post-germinative seedling growth. Plant J. (in press)
    • Plant J.
    • Rylott, E.L.1
  • 23
    • 0036865360 scopus 로고    scopus 로고
    • Acyl-CoA measurements in plants suggest a role in regulating various cellular processes
    • I.A. Graham Acyl-CoA measurements in plants suggest a role in regulating various cellular processes Biochem. Soc. Trans. 30 2002 1095 1099
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1095-1099
    • Graham, I.A.1
  • 24
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells
    • F.J. Corpas Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells Trends Plant Sci. 6 2001 145 150
    • (2001) Trends Plant Sci. , vol.6 , pp. 145-150
    • Corpas, F.J.1
  • 25
    • 0034671619 scopus 로고    scopus 로고
    • Stress induces peroxisome biogenesis genes
    • E. Lopez-Huertas Stress induces peroxisome biogenesis genes EMBO J. 19 2000 6770 6777
    • (2000) EMBO J. , vol.19 , pp. 6770-6777
    • Lopez-Huertas, E.1
  • 26
    • 0347890291 scopus 로고    scopus 로고
    • Peroxisomes, reactive oxygen metabolism and stress-related enzyme activities
    • A. Baker I.A. Graham Kluwer Academic Publishers
    • L.A. Del Rio Peroxisomes, reactive oxygen metabolism and stress-related enzyme activities A. Baker I.A. Graham Plant Peroxisomes, Biochemistry, Cell Biology and Biotechnological Applications 2002 Kluwer Academic Publishers 221 258
    • (2002) Plant Peroxisomes, Biochemistry, Cell Biology and Biotechnological Applications , pp. 221-258
    • Del Rio, L.A.1
  • 27
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • A. Jimenez Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves Plant Physiol. 114 1997 275 284
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jimenez, A.1
  • 28
    • 0037832556 scopus 로고    scopus 로고
    • Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells
    • C.S. Lisenbee Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells Plant Physiol. 132 2003 870 882
    • (2003) Plant Physiol. , vol.132 , pp. 870-882
    • Lisenbee, C.S.1
  • 29
    • 31044444190 scopus 로고    scopus 로고
    • Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase
    • C.S. Lisenbee Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase Plant J. 43 2005 900 914
    • (2005) Plant J. , vol.43 , pp. 900-914
    • Lisenbee, C.S.1
  • 30
    • 11444263029 scopus 로고    scopus 로고
    • Ascorbate peroxidase, a scavenger of hydrogen peroxide in glyoxysomal membranes
    • K. Karyotou, and R.P. Donaldson Ascorbate peroxidase, a scavenger of hydrogen peroxide in glyoxysomal membranes Arch. Biochem. Biophys. 434 2005 248 257
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 248-257
    • Karyotou, K.1    Donaldson, R.P.2
  • 32
    • 0029064219 scopus 로고
    • The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions
    • C. van Roermund The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions EMBO J. 14 1995 3480 3486
    • (1995) EMBO J. , vol.14 , pp. 3480-3486
    • Van Roermund, C.1
  • 33
    • 0035208660 scopus 로고    scopus 로고
    • Re-examining the role of the glyoxylate cycle in oilseeds
    • P.J. Eastmond, and I.A. Graham Re-examining the role of the glyoxylate cycle in oilseeds Trends Plant Sci. 6 2001 72 77
    • (2001) Trends Plant Sci. , vol.6 , pp. 72-77
    • Eastmond, P.J.1    Graham, I.A.2
  • 34
    • 5644233748 scopus 로고    scopus 로고
    • Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase
    • J.E. Cornah Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase J. Biol. Chem. 279 2004 42916 42923
    • (2004) J. Biol. Chem. , vol.279 , pp. 42916-42923
    • Cornah, J.E.1
  • 35
    • 0034624977 scopus 로고    scopus 로고
    • Postgerminative growth and lipid catabolism in oilseeds lacking the glyoxylate cycle
    • P.J. Eastmond Postgerminative growth and lipid catabolism in oilseeds lacking the glyoxylate cycle Proc. Natl. Acad. Sci. U. S. A. 97 2000 5669 5674
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5669-5674
    • Eastmond, P.J.1
  • 36
    • 0033231013 scopus 로고    scopus 로고
    • Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p
    • C.W.T. van Roermund Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p EMBO J. 18 1999 5843 5852
    • (1999) EMBO J. , vol.18 , pp. 5843-5852
    • Van Roermund, C.W.T.1
  • 37
    • 0036741495 scopus 로고    scopus 로고
    • Arabidopsis a BOUT de SOUFFLE, which is homologous with mammalian carnitine acyl carrier, is required for postembryonic growth in the light
    • S. Lawand Arabidopsis A BOUT DE SOUFFLE, which is homologous with mammalian carnitine acyl carrier, is required for postembryonic growth in the light Plant Cell 14 2002 2161 2173
    • (2002) Plant Cell , vol.14 , pp. 2161-2173
    • Lawand, S.1
  • 38
    • 33644802667 scopus 로고    scopus 로고
    • Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination
    • I. Pracharoenwattana Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination Plant Cell 17 2005 2037 2048
    • (2005) Plant Cell , vol.17 , pp. 2037-2048
    • Pracharoenwattana, I.1
  • 39
    • 17744374145 scopus 로고    scopus 로고
    • The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana
    • J. Schuster, and S. Binder The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana Plant Mol. Biol. 57 2005 241 254
    • (2005) Plant Mol. Biol. , vol.57 , pp. 241-254
    • Schuster, J.1    Binder, S.2
  • 40
    • 1342287231 scopus 로고    scopus 로고
    • Lipoic acid-dependent oxidative catabolism of α-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis
    • N.L. Taylor Lipoic acid-dependent oxidative catabolism of α-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis Plant Physiol. 134 2004 838 848
    • (2004) Plant Physiol. , vol.134 , pp. 838-848
    • Taylor, N.L.1
  • 41
    • 0034979962 scopus 로고    scopus 로고
    • The mitochondrial isovaleryl-coenzyme a dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism
    • K. Daschner The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism Plant Physiol. 126 2001 601 612
    • (2001) Plant Physiol. , vol.126 , pp. 601-612
    • Daschner, K.1
  • 42
    • 0035903171 scopus 로고    scopus 로고
    • Chy1, an Arabidopsis mutant with impaired beta-oxidation, is defective in a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase
    • B.K. Zolman chy1, an Arabidopsis mutant with impaired beta-oxidation, is defective in a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase J. Biol. Chem. 276 2001 31037 31046
    • (2001) J. Biol. Chem. , vol.276 , pp. 31037-31046
    • Zolman, B.K.1
  • 43
    • 3342962408 scopus 로고    scopus 로고
    • An Arabidopsis mutant disrupted in valine catabolism is also compromised in peroxisomal fatty acid beta-oxidation
    • P.R. Lange An Arabidopsis mutant disrupted in valine catabolism is also compromised in peroxisomal fatty acid beta-oxidation FEBS Lett. 571 2004 147 153
    • (2004) FEBS Lett. , vol.571 , pp. 147-153
    • Lange, P.R.1
  • 44
    • 33644688603 scopus 로고    scopus 로고
    • The critical role of Arabidopsis electron-transfer flavoprotein: ubiquinone oxidoreductase during dark-induced starvation
    • K. Ishizaki The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone oxidoreductase during dark-induced starvation Plant Cell 17 2005 2587 2600
    • (2005) Plant Cell , vol.17 , pp. 2587-2600
    • Ishizaki, K.1
  • 45
    • 16544384619 scopus 로고    scopus 로고
    • AraPerox. a database of putative Arabidopsis proteins from plant peroxisomes
    • S. Reumann AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes Plant Physiol. 136 2004 2587 2608
    • (2004) Plant Physiol. , vol.136 , pp. 2587-2608
    • Reumann, S.1
  • 46
    • 0033762717 scopus 로고    scopus 로고
    • Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes
    • B.K. Zolman Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes Genetics 156 2000 1323 1337
    • (2000) Genetics , vol.156 , pp. 1323-1337
    • Zolman, B.K.1
  • 47
    • 0035696499 scopus 로고    scopus 로고
    • Inputs to the active indole-3-acetic acid pool: De novo synthesis, conjugate hydrolysis, and indole-3-butyric acid beta-oxidation
    • B. Bartel Inputs to the active indole-3-acetic acid pool: de novo synthesis, conjugate hydrolysis, and indole-3-butyric acid beta-oxidation J. Plant Growth Regul. 20 2001 198 216
    • (2001) J. Plant Growth Regul. , vol.20 , pp. 198-216
    • Bartel, B.1
  • 48
    • 0021105820 scopus 로고
    • The biosynthesis of jasmonic acid: A physiological role for plant lipoxygenase
    • B.A. Vick, and D. Zimmerman The biosynthesis of jasmonic acid: a physiological role for plant lipoxygenase Biochem. Biophys. Res. Commun. 111 1983 470 477
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 470-477
    • Vick, B.A.1    Zimmerman, D.2
  • 49
    • 0001699831 scopus 로고
    • Biosynthesis of jasmonic acid by several plant species
    • B.A. Vick, and D. Zimmerman Biosynthesis of jasmonic acid by several plant species Plant Physiol. 75 1984 458 461
    • (1984) Plant Physiol. , vol.75 , pp. 458-461
    • Vick, B.A.1    Zimmerman, D.2
  • 50
    • 20444470992 scopus 로고    scopus 로고
    • Biosynthesis and metabolism of jasmonates
    • F. Schaller Biosynthesis and metabolism of jasmonates J. Plant Growth Regul. 23 2005 179 199
    • (2005) J. Plant Growth Regul. , vol.23 , pp. 179-199
    • Schaller, F.1
  • 51
    • 20444476835 scopus 로고    scopus 로고
    • Jasmonic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes
    • F.L. Theodoulou Jasmonic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes Plant Physiol. 137 2005 835 840
    • (2005) Plant Physiol. , vol.137 , pp. 835-840
    • Theodoulou, F.L.1
  • 52
    • 0034031727 scopus 로고    scopus 로고
    • 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
    • F. Schaller 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis Planta 210 2000 979 984
    • (2000) Planta , vol.210 , pp. 979-984
    • Schaller, F.1
  • 53
    • 0010632418 scopus 로고    scopus 로고
    • Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
    • J. Strassner Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response Plant J. 32 2002 585 601
    • (2002) Plant J. , vol.32 , pp. 585-601
    • Strassner, J.1
  • 54
    • 0034641758 scopus 로고    scopus 로고
    • The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
    • A. Stintzi, and J. Browse The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis Proc. Natl. Acad. Sci. U. S. A. 97 2000 10625 10630
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10625-10630
    • Stintzi, A.1    Browse, J.2
  • 55
    • 0343962242 scopus 로고    scopus 로고
    • The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway
    • P.M. Sanders The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway Plant Cell 12 2000 1041 1061
    • (2000) Plant Cell , vol.12 , pp. 1041-1061
    • Sanders, P.M.1
  • 56
    • 0035940424 scopus 로고    scopus 로고
    • Plant defense in the absence of jasmonic acid: The role of cyclopentenones
    • A. Stintzi Plant defense in the absence of jasmonic acid: the role of cyclopentenones Proc. Natl. Acad. Sci. U. S. A. 98 2001 12837 12842
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12837-12842
    • Stintzi, A.1
  • 57
    • 17144416797 scopus 로고    scopus 로고
    • A new type of peroxisomal acyl-coenzyme a synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid
    • K. Schneider A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid J. Biol. Chem. 280 2005 13962 13972
    • (2005) J. Biol. Chem. , vol.280 , pp. 13962-13972
    • Schneider, K.1
  • 58
    • 1542350187 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana
    • G.B. Tilton Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana J. Biol. Chem. 279 2004 7487 7494
    • (2004) J. Biol. Chem. , vol.279 , pp. 7487-7494
    • Tilton, G.B.1
  • 59
    • 0038796765 scopus 로고    scopus 로고
    • Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases
    • J. Shockey Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme A synthetases Plant Physiol. 132 2003 1065 1076
    • (2003) Plant Physiol. , vol.132 , pp. 1065-1076
    • Shockey, J.1
  • 60
    • 2442648069 scopus 로고    scopus 로고
    • Gene-specific involvement of β-oxidation in wound-activated responses in Arabidopsis
    • M.C. Castillo Gene-specific involvement of β-oxidation in wound-activated responses in Arabidopsis Plant Physiol. 135 2004 85 94
    • (2004) Plant Physiol. , vol.135 , pp. 85-94
    • Castillo, M.C.1
  • 61
    • 20444481531 scopus 로고    scopus 로고
    • Role of beta-oxidation in jasmonate biosynthesis and systemic wound signaling in tomato
    • C. Li Role of beta-oxidation in jasmonate biosynthesis and systemic wound signaling in tomato Plant Cell 17 2005 971 986
    • (2005) Plant Cell , vol.17 , pp. 971-986
    • Li, C.1
  • 62
    • 22244440848 scopus 로고    scopus 로고
    • A defect in glyoxysomal fatty acid β-oxidation reduces jasmonic acid accumulation in Arabidopsis
    • M.M. Afitlhile A defect in glyoxysomal fatty acid β-oxidation reduces jasmonic acid accumulation in Arabidopsis Plant Physiol. Biochem. 43 2005 603 609
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 603-609
    • Afitlhile, M.M.1
  • 63
    • 0033824782 scopus 로고    scopus 로고
    • The Arabidopsis COMATOSE locus regulates germination potential
    • L. Russell The Arabidopsis COMATOSE locus regulates germination potential Development 127 2000 3759 3767
    • (2000) Development , vol.127 , pp. 3759-3767
    • Russell, L.1
  • 64
    • 13244295178 scopus 로고    scopus 로고
    • Reserve mobilization in the Arabidopsis endosperm fuels hypocotyl elongation in the dark, is independent of abscisic acid, and requires PHOSPHOENOLPYRUVATE CARBOXYKINASE1
    • S. Penfield Reserve mobilization in the Arabidopsis endosperm fuels hypocotyl elongation in the dark, is independent of abscisic acid, and requires PHOSPHOENOLPYRUVATE CARBOXYKINASE1 Plant Cell 16 2004 2705 2718
    • (2004) Plant Cell , vol.16 , pp. 2705-2718
    • Penfield, S.1
  • 65
    • 0036736285 scopus 로고    scopus 로고
    • Germination and storage reserve mobilization are regulated independently in Arabidopsis
    • S.L. Pritchard Germination and storage reserve mobilization are regulated independently in Arabidopsis Plant J. 31 2002 639 647
    • (2002) Plant J. , vol.31 , pp. 639-647
    • Pritchard, S.L.1
  • 66
    • 0036581314 scopus 로고    scopus 로고
    • Fatty acid-derived signals in plants
    • H. Weber Fatty acid-derived signals in plants Trends Plant Sci. 7 2002 217 224
    • (2002) Trends Plant Sci. , vol.7 , pp. 217-224
    • Weber, H.1
  • 67
    • 0034740304 scopus 로고    scopus 로고
    • The DEFECTIVE in ANTHER DEHISCENCE1 gene encodes a novel phospholipase A1 catalyzing the initial step of jasmonic acid biosynthesis, which synchronizes pollen maturation, anther dehiscence, and flower opening in Arabidopsis
    • S. Ishiguro The DEFECTIVE IN ANTHER DEHISCENCE1 gene encodes a novel phospholipase A1 catalyzing the initial step of jasmonic acid biosynthesis, which synchronizes pollen maturation, anther dehiscence, and flower opening in Arabidopsis Plant Cell 13 2001 2191 2209
    • (2001) Plant Cell , vol.13 , pp. 2191-2209
    • Ishiguro, S.1
  • 68
    • 0035918178 scopus 로고    scopus 로고
    • A novel class of oxylipins, sn1-O-(12-oxophytodienoyl)-sn2-O- (hexadecatrienoyl)-monogalactosyl diglyceride, from Arabidopsis thaliana
    • B. Stelmach A novel class of oxylipins, sn1-O-(12-oxophytodienoyl)-sn2-O- (hexadecatrienoyl)-monogalactosyl diglyceride, from Arabidopsis thaliana J. Biol. Chem. 276 2001 12832 12838
    • (2001) J. Biol. Chem. , vol.276 , pp. 12832-12838
    • Stelmach, B.1
  • 69
    • 0033835363 scopus 로고    scopus 로고
    • Octadecanoid and jasmonate signalling in tomato (Lycopersicon esculentum Mill.) leaves: Endogenous jasmonates do not induce jasmonate biosynthesis
    • O. Miersch, and C. Wasternack Octadecanoid and jasmonate signalling in tomato (Lycopersicon esculentum Mill.) leaves: endogenous jasmonates do not induce jasmonate biosynthesis Biol. Chem. 381 2000 715 722
    • (2000) Biol. Chem. , vol.381 , pp. 715-722
    • Miersch, O.1    Wasternack, C.2
  • 70
    • 0036794689 scopus 로고    scopus 로고
    • Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid β-oxidation
    • M. Fulda Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid β-oxidation Plant J. 32 2002 93 103
    • (2002) Plant J. , vol.32 , pp. 93-103
    • Fulda, M.1
  • 71
    • 0034951257 scopus 로고    scopus 로고
    • Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana
    • E.L. Rylott Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana Biochem. Soc. Trans. 29 2001 283 287
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 283-287
    • Rylott, E.L.1


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