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Publikationen - Molekulare Signalverarbeitung

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Publikation

Weichert, H.; Kohlmann, M.; Wasternack, C.; Feussner, I. Lipids and signalling: oxylipins 3 - functional aspects Biochem. Soc. Trans. 28, 861-862, (2001)

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Publikation

Feussner, I.; Kühn, H.; Wasternack, C. The lipoxygenase dependent degradation of storage lipids Trends Plant Sci. 6, 268-273, (2001)

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Publikation

Berger, S.; Weichert, H.; Porzel, A.; Wasternack, C.; Kühn, H.; Feussner, I. Enzymatic and non-enzymatic lipid peroxidation in leaf development Biochim. Biophys. Acta 1533, 266-276, (2001)

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Publikation

Weichert, H.; Kolbe, A.; Wasternack, C.; Feussner, I. Formation of 4-hydroxy-1-alkenals in barley leaves Biochem. Soc. Trans. 28, 850-851, (2001)

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Publikation

Kenton, P.; Mur, L.A.J.; Atzorn, R.; Wasternack, C.; Draper, J. (—)-Jasmonic Acid Accumulation in Tobacco Hypersensitive Response Lesions Mol. Plant Microbiol. Interactions 12, 74-78, (1999) DOI: 10.1094/MPMI.1999.12.1.74

Tobacco infected with Pseudomonas syringae pv. phaseolicola undergoes a hypersensitive response (HR). Jasmonic acid (JA) accumulated within the developing lesion 3 to 9 h after infection and this accumulation preceded protein loss, cell death, and malondialdehyde accumulation. Accumulating JA consisted largely of the (—)-JA stereoisomer and was essentially restricted to the HR lesion
Publikation

Kramell, R.; Miersch, O.; Schneider, G.; Wasternack, C. Liquid chromatography of jasmonic acid amine conjugates Chromatographia 49, 42-46, (1999)

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Publikation

Miersch, O.; Bohlmann, H.; Wasternack, C. Jasmonates and related compounds form Fusarium oxysporum Phytochemistry 50, 517-523, (1999)

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Publikation

Miersch, O.; Kramell, R.; Parthier, B.; Wasternack, C. Structure-activity relations of substituted, deleted or stereospecifically altered jasmonic acid in gene expression of barley leaves Phytochemistry 50, 353-361, (1999)

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Publikation

Herde, O.; Peña-Cortés, H.; Wasternack, C.; Willmitzer, L.; Fisahn, J. Electric signaling and PIN2 gene expression on different abiotic stimuli depend on a distinct threshold level of endogenous ABA in several ABA-deficient tomato mutants Plant Physiol. 119, 213-218, (1999)

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Publikation

Feussner, I.; Hause, B.; Nellen, A.; Wasternack, C.; Kindl, H. Lipid-body lipoxygenase is expressed in cotyledons during germination prior to other lipoxygenase forms Planta 198, 288-293, (1996) DOI: 10.1007/BF00206255

Lipid bodies are degraded during germination. Whereas some proteins, e.g. oleosins, are synthesized during the formation of lipid bodies of maturating seeds, a new set of proteins, including a specific form of lipoxygenase (LOX; EC 1.13.11.12), is detectable in lipid bodies during the stage of fat degradation in seed germination. In cotyledons of cucumber (Cucumis sativus L.) seedlings at day 4 of germination, the most conspicuous staining with anti-LOX antibodies was observed in the cytosol. At very early stages of germination, however, the LOX form present in large amounts and synthesized preferentially was the lipid-body LOX. This was demonstrated by immunocytochemical staining of cotyledons from 1-h and 24-h-old seedlings: the immunodecoration of sections of 24-h-old seedlings with anti-LOX antiserum showed label exclusively correlated with lipid bodies of around 3 μm in diameter. In accordance, the profile of LOX protein isolated from lipid bodies during various stages of germination showed a maximum at day 1. By measuring biosynthesis of the protein in vivo we demonstrated that the highest rates of synthesis of lipid-body LOX occurred at day 1 of germination. The early and selective appearance of a LOX form associated with lipid bodies at this stage of development is discussed.
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