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Lipids, lipases, and lipid-modifying enzymes in plant disease resistance
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in press. [Published online.]
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Shah J: Lipids, lipases, and lipid-modifying enzymes in plant disease resistance. Annu Rev Phytopathol 2004, in press. [Published online.]
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(2004)
Annu Rev Phytopathol
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Shah, J.1
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42
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1042290708
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The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR of FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance
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A. Nandi, R. Welti, and J. Shah The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance Plant Cell 16 2004 465 477 The authors show that SFD1 contributes to the establishment of systemic resistance. SFD1 encodes a protein that is involved in glycerolipid metabolism, adding to a growing body of evidence for the involvement of lipid signaling in systemic resistance (see [41] for an up-to-date review). Like the dir1 mutant, which has a defective putative lipid-transfer protein [43], sfd1 plants exhibit normal local resistance responses to virulent and avirulent pathogens.
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(2004)
Plant Cell
, vol.16
, pp. 465-477
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Nandi, A.1
Welti, R.2
Shah, J.3
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43
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0037179714
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A putative lipid transfer protein involved in systemic resistance signaling in Arabidopsis
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A.M. Maldonado, P. Doerner, R.A. Dixon, C.J. Lamb, and R.K. Cameron A putative lipid transfer protein involved in systemic resistance signaling in Arabidopsis Nature 419 2002 399 403
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(2002)
Nature
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, pp. 399-403
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Maldonado, A.M.1
Doerner, P.2
Dixon, R.A.3
Lamb, C.J.4
Cameron, R.K.5
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44
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0347364622
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High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity
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D. Kumar, and D.F. Klessig High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity Proc Natl Acad Sci USA 100 2003 16101 16106 An impressive purification strategy for SABP2, a low-abundance high-affinity SA-binding protein, led to the identification of a lipase belonging to the α/β-fold hydrolase superfamily that also contains EDS1 and PAD4. Significantly, the authors show that SABP2 enzyme activity was stimulated by SA binding and that SABP2 is required for the full expression of both local and systemic resistance.
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(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 16101-16106
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Kumar, D.1
Klessig, D.F.2
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45
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13444263252
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Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity
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F. Forouhar, Y. Yang, D. Kumar, Y. Chen, E. Fridman, S.W. Park, Y. Chiang, T.B. Acton, G.T. Montelione, and E. Pichersky Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity Proc Natl Acad Sci USA 102 2005 1773 1778 The authors introduce an exciting new dimension to the study of plant defense regulators by analyzing the crystal structure of SABP2 alone and in complex with SA. They show that SABP2 uses methyl-salicylate as a substrate and that SA acts as a potent product inhibitor. The kinetics of SABP2 offer a potential mechanism for the fine-tuning of SA-dependent resistance responses.
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(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 1773-1778
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Forouhar, F.1
Yang, Y.2
Kumar, D.3
Chen, Y.4
Fridman, E.5
Park, S.W.6
Chiang, Y.7
Acton, T.B.8
Montelione, G.T.9
Pichersky, E.10
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