Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Autor Nach Häufigkeit alphabetisch sortiert: Monostori, T
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C
Autor Nach Häufigkeit alphabetisch sortiert: Maucher, H
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C.
Autor Nach Häufigkeit alphabetisch sortiert: Zheng, N.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Ann. Plant Reviews, Blackwell, Oxford, UK
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Eur. J. Biochem.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: University Press, Oxford, UK
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Plant Mol Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Trends Plant Sci.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: J. Plant Physiol
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (3)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- Phytochemistry (12)
- Plant Physiol. (10)
- FEBS Lett. (8)
- Planta (8)
- J. Plant Physiol. (6)
- Plant Cell (6)
- Biol. Chem. (5)
- J. Biol. Chem. (5)
- Plant Cell Physiol. (5)
- Plant J. (5)
- J. Exp. Bot. (4)
- Bot. Acta (3)
- New Phytol. (3)
- Ann. Bot. (2)
- Biochem. Soc. Trans. (2)
- Biologie in unserer Zeit (2)
- Fett/Lipid (2)
- J. Plant Growth Regul. (2)
- Nat. Chem. Biol. (2)
- Plant Biol. (2)
- Plant Mol. Biol. (2)
- Plant Signal Behav. (2)
- Trends Plant Sci. (2)
- 0 (1)
- ACS Chem. Biol. (1)
- Acta Biol. Szeged. (1)
- Acta Physiol. Plant. (1)
- Anal. Biochem. (1)
- Annu. Rev. Plant Biol. (1)
- BBA-Mol. Cell Biol. Lipids (1)
- BIOspektrum (1)
- Biochemistry (1)
- Biochimie (1)
- Biotechnol. Adv. (1)
- Cereal Res. Commun. (1)
- ChemBioChem (1)
- ChemRxiv (1)
- Chromatographia (1)
- Cold Spring Harb. Perspect. Biol. (1)
- Curr. Opin. Plant Biol. (1)
- Eur. J. Biochem. (1)
- Eur. J. Plant Pathol. (1)
- J. Chromatogr. A (1)
- Jap. Soc. Chem. Regul Plants, Abstr. (1)
- Mol. Plant Microbe Interact. (1)
- Nature (1)
- Physiol. Plant. (1)
- Phytomedicine (1)
- Plant Cell Environ. (1)
- Plant Cell Rep. (1)
- Plant Growth Regul. (1)
- Proc. Natl. Acad. Sci. U.S.A. (1)
- Science (1)
- Tetrahedron (1)
- Z. Naturforsch. C (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Wasternack, C. (3)
- Abel, S. (2)
- Feussner, I. (2)
- Kühn, H. (2)
- Parthier, B. (2)
- Delker, C. (1)
- Graner, A. (1)
- Grubb, C. D. (1)
- Lee, J. (1)
- Löbler, M. (1)
- Quint, M. (1)
- Ticconi, C. A. (1)
- Vörös, K. (1)
Zeige Ergebnisse 1 bis 3 von 3.
Feussner, I.; Kühn, H.; Wasternack, C.; Lipoxygenase-dependent degradation of storage lipids Trends Plant Sci. 6, 268-273, (2001) DOI: 10.1016/S1360-1385(01)01950-1
Oilseed germination is characterized by the mobilization of storage lipids as a carbon source for the germinating seedling. In spite of the importance of lipid mobilization, its mechanism is only partially understood. Recent data suggest that a novel degradation mechanism is initiated by a 13-lipoxygenase during germination, using esterified fatty acids specifically as substrates. This 13-lipoxygenase reaction leads to a transient accumulation of ester lipid hydroperoxides in the storage lipids, and the corresponding oxygenated fatty acid moieties are preferentially removed by specific lipases. The free hydroperoxy fatty acids are subsequently reduced to their hydroxy derivatives, which might in turn undergo β-oxidation.
Vörös, K.; Feussner, I.; Kühn, H.; Lee, J.; Graner, A.; Löbler, M.; Parthier, B.; Wasternack, C.; Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves Eur. J. Biochem. 251, 36-44, (1998) DOI: 10.1046/j.1432-1327.1998.2510036.x
We found three methyl jasmonate−induced lipoxygenases with molecular masses of 92 kDa, 98 kDa, and 100 kDa (LOX‐92, ‐98 and ‐100) [Feussner, I., Hause, B., Vörös, K., Parthier, B. & Wasternack, C. (1995) Plant J. 7 , 949−957]. At least two of them (LOX‐92 and LOX‐100), were shown to be localized within chloroplasts of barley leaves. Here, we describe the isolation of a cDNA (3073 bp) coding for LOX‐100, a protein of 936 amino acid residues and a molecular mass of 106 kDa. By sequence comparison this lipoxygenase could be identified as LOX2‐type lipoxygenase and was therefore designated LOX2 : Hv : 1 . The recombinant lipoxygenase was expressed in Escherichia coli and characterized as linoleate 13‐LOX and arachidonate 15‐LOX, respectively. The enzyme exhibited a pH optimum around pH 7.0 and a moderate substrate preference for linoleic acid. The gene was transiently expressed after exogenous application of jasmonic acid methyl ester with a maximum between 12 h and 18 h. Its expression was not affected by exogenous application of abscisic acid. Also a rise of endogenous jasmonic acid resulting from sorbitol stress did not induce LOX2 : Hv : 1 , suggesting a separate signalling pathway compared with other jasmonate‐induced proteins of barley. The properties of LOX2 : Hv : 1 are discussed in relation to its possible involvement in jasmonic acid biosynthesis and other LOX forms of barley identified so far.
Wasternack, C.; Parthier, B.; Jasmonate-signalled plant gene expression Trends Plant Sci. 2, 302-307, (1997) DOI: 10.1016/S1360-1385(97)89952-9
Jasmonic acid is distributed throughout higher plants, synthesized from linolenic acid via the octadecanoic pathway. An important and probably essential role seems to be its operation as a ‘master switch’, responsible for the activation of signal transduction pathways in response to predation and pathogen attack. Proteins encoded by jasmonate-induced genes include enzymes of alkaloid and phytoalexin synthesis, storage proteins, cell wall constituents and stress protectants. The wound-induced formation of proteinase inhibitors is a well-studied example, in which jasmonic acid combines with abscisic acid and ethylene to protect the plant from predation.