Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Autor Nach Häufigkeit alphabetisch sortiert: Monostori, T
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C
Autor Nach Häufigkeit alphabetisch sortiert: Sharma, V.K
Autor Nach Häufigkeit alphabetisch sortiert: Maucher, H
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C.
Autor Nach Häufigkeit alphabetisch sortiert: Drost, H.-G.
Autor Nach Häufigkeit alphabetisch sortiert: Carbonell, A.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Plant Signal Behav
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: FEBS Letters
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Bot. Acta
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: ACS Chem Biol
Autor Nach Häufigkeit alphabetisch sortiert: Molina, D.
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (2)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- Phytochemistry (12)
- 0 (10)
- Plant Physiol. (7)
- FEBS Lett. (5)
- Biol. Chem. (4)
- Planta (4)
- Trends Plant Sci. (4)
- New Phytol. (3)
- Plant Cell (3)
- Plant J. (3)
- Ann. Bot. (2)
- Annu. Rev. Plant Biol. (2)
- Bot. Acta (2)
- Fett/Lipid (2)
- J. Biol. Chem. (2)
- J. Exp. Bot. (2)
- Nat. Plants (2)
- New Biotechnol. (2)
- Plant Cell Physiol. (2)
- Plant Signal Behav. (2)
- ACS Chem. Biol. (1)
- Annu. Plant Rev. (1)
- BIOspektrum (1)
- BMC Genomics (1)
- Biochem. Soc. Trans. (1)
- Biochimie (1)
- Biologie in unserer Zeit (1)
- Biology of Plant-Microbe Interactions (1)
- Cereal Res. Commun. (1)
- ChemBioChem (1)
- ChemRxiv (1)
- Chromatographia (1)
- Curr. Opin. Plant Biol. (1)
- Eur. J. Plant Pathol. (1)
- Int. J. Mol. Sci. (1)
- J. Plant Growth Regul. (1)
- J. Plant Physiol. (1)
- Jap. Soc. Chem. Regul Plants, Abstr. (1)
- Mol. Biol. Evol. (1)
- Nucleic Acids Res. (1)
- PLOS ONE (1)
- Physiol. Plant. (1)
- Plant Biol. (1)
- Plant Cell Environ. (1)
- Plant Cell Rep. (1)
- Plant Growth Regul. (1)
- Plant Mol. Biol. (1)
- Proc. Natl. Acad. Sci. U.S.A. (1)
- Prog. Nucleic Acid Res. Mol. Biol. (1)
- Tetrahedron (1)
- Viruses (1)
- bioRxiv (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Hause, B. (2)
- Wasternack, C. (2)
- Feussner, K. (1)
- Lehmann, J. (1)
- Parthier, B. (1)
- zur Nieden, U. (1)
Zeige Ergebnisse 1 bis 2 von 2.
Hause, B.; Feussner, K.; Wasternack, C.; Nuclear Location of a Diadenosine 5′,5′”-P1,P4Tetraphosphate (Ap4A) Hydrolase in Tomato Cells Grown in Suspension Cultures Bot. Acta 110, 452-457, (1997) DOI: 10.1111/j.1438-8677.1997.tb00662.x
Diadenosine 5′,5′”‐P1,P4‐tetraphosphate (Ap4A) cleaving enzymes are assumed to regulate intracellular levels of Ap4A, a compound known to affect cell proliferation and stress responses. From plants an Ap4A hydrolase was recently purified using tomato cells grown in suspension. It was partially sequenced and a peptide antibody was prepared (Feussner et al., 1996). Using this polyclonal monospecific antibody, an abundant nuclear location of Ap4A hydrolase in 4‐day‐old cells of atomato cell suspension culture is demonstrated here by means of immunocytochemical techniques using FITC (fluorescein‐5‐isothiocyanate) labeled secondary antibodies. The microscopic analysis of the occurrence of Ap4A hydrolase performed for different stages of the cell cycle visualized by parallel DAPI (4,6‐diamidino‐2‐phenylindole) staining revealed that the protein accumulates within nuclei of cells in the interphase, but is absent in the nucleus as well as cytoplasm during all stages of mitosis. This first intracellular localization of an Ap4A degrading enzyme within the nucleus and its pattern of appearance during the cell cycle is discussed in relation to the suggested role of Ap4A in triggering DNA synthesis and cell proliferation.
Hause, B.; zur Nieden, U.; Lehmann, J.; Wasternack, C.; Parthier, B.; Intracellular Localization of Jasmonate-Induced Proteins in Barley Leaves Bot. Acta 107, 333-341, (1994) DOI: 10.1111/j.1438-8677.1994.tb00804.x
The plant growth substance jasmonic acid and its methyl ester (JA‐Me) induce a set of proteins (jasmonate‐induced proteins, JIPs) when applied to leaf segments of barley (Hordeum vulgare L. cv. Salome). Most of these JIPs could be localized within different cell compartments by using a combination of biochemical and histochemical methods. Isolation and purification of various cell organelles of barley mesophyll cells, the separation of their proteins by one‐dimensional polyacrylamide gel electrophoresis and the identification of the major abundant JIPs by Western blot analysis, as well as the immuno‐gold labelling of JIPs in ultrathin sections were performed to localize JIPs intracellularly. JIP‐23 was found to be in vacuoles, peroxisomes, and in the granular parts of the nucleus as well as within the cytoplasm; JIP‐37 was detected in vacuoles and in the nucleoplasm; JIP‐66 is a cytosolic protein. Some less abundant JIPs were also localized within different cell compartments: JIP‐100 was found within the stromal fraction of chloroplasts; JIP‐70 is present in the peroxisome and the nucleus; JIP‐50 and JIP‐6 accumulate in vacuoles. The location of JIP‐66 and JIP‐6 confirms their possible physiological role deduced from molecular analysis of their cDNA.