Relevant bibliographies by topics / Nuclear activation analysis

Academic literature on the topic 'Nuclear activation analysis'

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Published: 4 June 2021
Last updated: 1 August 2024

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Journal articles on the topic "Nuclear activation analysis"

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Heydorn, K. "Recent Developments in Nuclear Activation Analysis." Isotopenpraxis Isotopes in Environmental and Health Studies 24, no. 2 (January 1988): 45–48. http://dx.doi.org/10.1080/10256018808623895.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry 223, no. 1-2 (September 1997): 251–61. http://dx.doi.org/10.1007/bf02223397.

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Bujdosó, B. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 178, no. 1 (February 1994): 207–36. http://dx.doi.org/10.1007/bf02068672.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 89, no. 1 (March 1985): 289–304. http://dx.doi.org/10.1007/bf02070218.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 102, no. 2 (December 1986): 551–78. http://dx.doi.org/10.1007/bf02047929.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 131, no. 1 (May 1989): 235–52. http://dx.doi.org/10.1007/bf02046626.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry 231, no. 1-2 (May 1998): 207–15. http://dx.doi.org/10.1007/bf02388036.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry 220, no. 2 (June 1997): 275–85. http://dx.doi.org/10.1007/bf02034873.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 116, no. 2 (December 1987): 471–88. http://dx.doi.org/10.1007/bf02035790.

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Bujdosó, E. "Analysis by nuclear reactions and activation." Journal of Radioanalytical and Nuclear Chemistry Articles 141, no. 2 (August 1990): 443–53. http://dx.doi.org/10.1007/bf02035811.

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Dissertations / Theses on the topic "Nuclear activation analysis"

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Al-Mugrabi, M. A. "Optimisation of instrumental neutron activation analysis." Thesis, University of Surrey, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.377262.

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Farooqi, Asad Saeed. "Nuclear activation techniques and methods of elemental concentration determination in bioenvironmental studies." Thesis, University of Surrey, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.280334.

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Zhang, Li 1969. "Coded aperture imaging for fast neautron activation analysis." Thesis, Massachusetts Institute of Technology, 1996. http://hdl.handle.net/1721.1/41018.

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Thesis (M.S.)--Massachusetts Institute of Technology, Dept. of Nuclear Engineering, 1996, and Thesis (M.S.)--Massachusetts Institute of Technology, Dept. of Electrical Engineering and Computer Science, 1996.
Includes bibliographical references (leaves 107-111).
by Li Zhang.
M.S.
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Kipler-Koch, Debra Ann. "Provenance determination of Bronze Age pottery using neutron activation analysis /." Online version of thesis, 1989. http://hdl.handle.net/1850/11432.

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Blaylock, Dwayne Patrick. "Activation products in the biological shield of the Georgia Tech Research Reactor." Thesis, Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/19431.

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Liddy, D. J. "A study of Roman amphoras from North Africa by neutron activation analysis." Thesis, University of Manchester, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355911.

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Ames, Michael Richard. "Development and application of a methodology for measuring atmospheric mercury by instrumental neutron activation analysis." Thesis, Massachusetts Institute of Technology, 1995. http://hdl.handle.net/1721.1/36020.

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Inyang, Otu Effiong. "Development of a prompt-gamma, neutron-activation analysis facility at the Texas A&M University Nuclear Science Center." Thesis, [College Station, Tex. : Texas A&M University, 2008. http://hdl.handle.net/1969.1/ETD-TAMU-2980.

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De, Chiara Alessia. "Molecular analysis of the prosurvival effect of cytosolic Proliferating Cell Nuclear Antigen (PCNA) in neutrophils." Thesis, Paris 5, 2014. http://www.theses.fr/2014PA05S002.

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Le polynucléaire neutrophile (PMN), cellule clé de l’immunité innée, est la première cellule à être recrutée sur le site inflammatoire. Après avoir détruit l’agent pathogène, il entre en apoptose puis est éliminé par les macrophages pour éviter le déversement de son contenu lytique, dangereux pour l’environnement. La régulation de la balance survie/apoptose du neutrophile est donc une étape cruciale de la résolution de l’inflammation. Notre laboratoire a mis en évidence la présence du Proliferating Cell Nuclear Antigen (PCNA) dans le neutrophile mature. PCNA est exprimé dans le noyau des cellules proliférantes, où il est impliqué dans la réplication/réparation de l’ADN et dans le contrôle du cycle cellulaire. PCNA est une protéine trimérique conservée au cours de l’évolution dépourvue d’activité enzymatique. En effet, PCNA constitue une “plateforme” qui interagit avec différents partenaires protéiques et orchestre leurs fonctions. De plus, pour assurer sa fonction, PCNA doit être obligatoirement sous forme trimérique. Dans le neutrophile mature, il a été démontré que PCNA avait une localisation exclusivement cytosolique et qu’il contrôlait spécifiquement la survie du neutrophile. La translocation de PCNA du noyau au cytosol a lieu pendant la différenciation granulocytaire. Elle est dépendante d'une séquence d'export nucléaire (NES) accessible et fonctionnelle que lorsque PCNA est monomérique. Le but de ma thèse a été d’étudier la plateforme de PCNA dans le cytosol du neutrophile afin d'identifier les protéines associées à PCNA afin de comprendre sa fonction dans les neutrophiles. Nous avons montré la présence de la forme monomérique et de la forme trimérique de PCNA dans le cytosol du neutrophile mature. Nous avons démontré une activité anti-apoptotique de la forme monomérique dans des cellules PLB985 différenciées en neutrophiles. De plus, nous avons identifié des peptides exposés sur la surface monomérique de PCNA qui sont utilisé comme des compétiteurs pour déplacer les interactions entre PCNA et ses partenaires dans le cytosol des neutrophiles. Ces peptides modulent la survie des neutrophiles. Grâce à des analyses de Spectrométrie de Masse, nous avons identifié des nouveaux partenaires de PCNA dans le cytosol du neutrophile impliqués dans plusieurs voies métaboliques. Cela suggère que PCNA régule la survie du neutrophile en interagissant avec différents protéines cytosoliques. Parmi les partenaires identifiés, nous avons trouvé les sous-unités cytosoliques de la NADPH oxydase, enzyme responsable de la production de formes réactives de l’oxygène, à la base de l’activité microbicide du neutrophile. Nous avons montré en particulier l’interaction entre p47phox et PCNA. Nous avons enfin étudié l’implication fonctionnelle de l’interaction de PCNA avec la NADPH oxydase dans des cellules PLB985 et également dans des neutrophiles humains. L’ensemble des résultats suggère que PCNA cytoplasmique maintient le neutrophile dans un état de repos, et aide l’assemblage de la NADPH oxydase lors de son activation. Le réseau protéique associé à PCNA régule l’activité et la survie du neutrophile en modulant différentes voies de signalisation
Polymorphonuclear neutrophils (PMN), key cells of innate immunity are the first cell recruited to the inflammatory site. After destroying the pathogen, neutrophils undergo apoptosis and are cleared by macrophages to prevent the spillage of their lytic content that is dangerous for the environment. The regulation of the survival/apoptosis balance of neutrophil is a crucial step in the inflammation resolution. Our laboratory has shown the presence of Proliferating Cell Nuclear Antigen (PCNA) in mature neutrophils. PCNA is expressed in the nucleus of proliferating cells, where it is involved in DNA replication/repair and in cell cycle control. PCNA is a trimeric protein conserved during evolution and deprived of enzymatic activity. Indeed, PCNA is a “platform” that interacts with different partner proteins and orchestrates their functions. Furthermore, PCNA must be in trimeric form to play its role. In mature neutrophils, PCNA has an exclusively cytosolic localization where it specifically controls their survival. The PCNA translocation from nucleus to the cytosol happened during the granulocytic differentiation. This nuclear-to-cytosol relocalisation is dependent on a nuclear export sequence (NES), which is accessible and functional when PCNA is monomeric. The aim of my thesis was to study the PCNA platform in the neutrophil cytosol to identify the proteins associated with PCNA in order to understand its function in neutrophils. We have shown the expression of monomeric and trimeric forms of PCNA in the cytosol of mature neutrophils. We have demonstrated the anti-apoptotic activity of the monomeric form in PLB985 cells differentiated in neutrophils. Moreover, we have identified the surface-exposed peptides from the monomeric PCNA which are used as competitors of interactions between PCNA and its partner in the cytosol of neutrophils. These peptides modulate neutrophils survival. Thanks to the analysis of Mass Spectrometry, we have identified new partners of PCNA in the neutrophil cytosol involved in several metabolic pathways. This suggests that PCNA regulates neutrophil survival by interacting with different cytosolic proteins. Among the identified partners, we have found the cytosolic subunits of the NADPH oxidase, the enzyme responsible of the reactive oxygen species production, at the base of the neutrophil microbicidal activity. We have shown especially the interaction between p47phox and PCNA. Finally, we have investigated the functional implication of the interaction of PCNA with the NADPH oxidase in PLB985 cells and also in human neutrophils. Taken altogether, results suggest that the cytosolic PCNA maintains the resting state of neutrophils, and it helps the assembly of the NADPH oxidase when activated. The protein network associated with PCNA regulates the activity and the survival of neutrophil by modulating several pathways
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Miller, Dean Allan. "Monte Carlo dosimetry and activation calculation for a proposed fusion device : MCNP analysis of aAlcator C-MOD." Thesis, Massachusetts Institute of Technology, 1985. http://hdl.handle.net/1721.1/15123.

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Thesis (M.S.)--Massachusetts Institute of Technology, Dept. of Nuclear Engineering, 1985.
MICROFICHE COPY AVAILABLE IN ARCHIVES AND SCIENCE.
Bibliography: leaf 109.
by Dean Allan Miller.
M.S.
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Books on the topic "Nuclear activation analysis"

1

Segebade, Christian. Photon activation analysis. Berlin: W. de Gruyter, 1987.

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Roberto, Cesareo, ed. Nuclear analytical techniques in medicine. Amsterdam: Elsevier, 1988.

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Parry, Susan J. Activation spectrometry in chemical analysis. New York: Wiley, 1991.

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Parry, Susan J. Handbook of neutron activation analysis. Woking: Viridian Publishing, 2003.

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Agency, International Atomic Energy, ed. Handbook on nuclear activation data. Vienna: International Atomic Energy Agency, 1987.

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Agency, International Atomic Energy, ed. Handbook on nuclear activation data. Vienna: International Atomic Energy Agency, 1987.

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B, Alfassi Zeev, and Peisach Max, eds. Elemental analysis by particle accelerators. Boca Raton: CRC Press, 1992.

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Gordadze, G. P. Optimizat͡s︡ii͡a︡ aktivat͡s︡ionnogo analiza. Moskva: Ėnergoatomizdat, 1985.

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A, Mikhaĭlov V., and Stepin B. D, eds. Komparatornyĭ neĭtronno-aktivat͡s︡ionnyĭ analiz: Izuchenie atmosfernykh aėrozoleĭ. Novosibirsk: "Nauka," Sibirskoe otd-nie, 1989.

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Starchik, L. P. I͡A︡derno-fizicheskie metody kontroli͡a︡ kachestva tverdogo topliva. Moskva: Nedra, 1985.

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Book chapters on the topic "Nuclear activation analysis"

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Zeisler, R., N. Vajda, G. Kennedy, G. Lamaze, and G. L. Molnár. "Activation Analysis." In Handbook of Nuclear Chemistry, 1553–617. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-0720-2_30.

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Balla, M., G. KeÖmley, and Zs Molnár. "Neutron Activation Analysis." In Nuclear Methods in Mineralogy and Geology, 115–44. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5363-2_2.

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Révay, Z., R. M. Lindstrom, E. A. Mackey, and T. Belgya. "Neutron-Induced Prompt Gamma Activation Analysis (PGAA)." In Handbook of Nuclear Chemistry, 1619–72. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-0720-2_31.

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Gwozdz, R., F. Grass, G. Polikarpov, and Yu Kutlakhmedov. "Activation Analysis of Large Volume Soil Extract Samples." In Nuclear Physical Methods in Radioecological Investigations of Nuclear Test Sites, 245–52. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-4116-1_23.

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Guinn, Vincent P. "A Short History of Nuclear Activation Analysis." In Nuclear Analytical Methods in the Life Sciences, 1–7. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0473-2_1.

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Hoste, J., and C. Vandecasteele. "Charged-Particle Activation Analysis of Biological Material." In Nuclear Analytical Methods in the Life Sciences, 119–31. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0473-2_14.

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Guinn, Vincent P., and Maria Gavrilas. "Instrumental Neutron Activation Analysis of Biological Samples." In Nuclear Analytical Methods in the Life Sciences, 9–16. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0473-2_2.

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Sarmani, S., L. L. Kuan, and M. A. A. Bakar. "Instrumental Neutron Activation Analysis of Kidney Stones." In Nuclear Analytical Methods in the Life Sciences, 497–502. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0473-2_54.

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Anderson, D. L., W. C. Cunningham, and E. A. Mackey. "Neutron Capture Prompt-γ Activation Analysis of Foods." In Nuclear Analytical Methods in the Life Sciences, 613–22. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0473-2_66.

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Cosmi, F., V. F. Romano, and L. F. Bellido. "An Automatic Sample Changer for Nuclear Activation Analysis." In Advanced Manufacturing Systems and Technology, 609–16. Vienna: Springer Vienna, 1996. http://dx.doi.org/10.1007/978-3-7091-2678-3_73.

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Conference papers on the topic "Nuclear activation analysis"

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Menapace, Enzio. "Nuclear data for fast-neutron activation analysis." In 4th International Conference on Applications of Nuclear Techniques: Neutrons and their Applications, edited by George Vourvopoulos and Themis Paradellis. SPIE, 1995. http://dx.doi.org/10.1117/12.204191.

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Arter, Wayne, and Guy Morgan. "Sensitivity Analysis for Activation Problems." In SNA + MC 2013 - Joint International Conference on Supercomputing in Nuclear Applications + Monte Carlo, edited by D. Caruge, C. Calvin, C. M. Diop, F. Malvagi, and J. C. Trama. Les Ulis, France: EDP Sciences, 2014. http://dx.doi.org/10.1051/snamc/201402404.

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Greaves, E. D., L. Sajo-Bohus, M. Manrique, and C. DeArriba. "Cryolite-Alumina Solutions Analysis by Neutron Activation." In VI LATIN AMERICAN SYMPOSIUM ON NUCLEAR PHYSICS AND APPLICATIONS. AIP, 2007. http://dx.doi.org/10.1063/1.2710636.

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Wells, Douglas P., Christian R. Segebade, Philip L. Cole, Ricardo Alarcon, Phil Cole, Andres J. Kreiner, and Hugo F. Arellano. "Photon Activation Analysis at the Idaho Accelerator Center." In VIII LATIN AMERICAN SYMPOSIUM ON NUCLEAR PHYSICS AND APPLICATIONS. AIP, 2010. http://dx.doi.org/10.1063/1.3480205.

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Bentley, R., G. Santistevan, D. Wells, A. Hutton, A. Stavola, S. Benson, K. Jordan, J. Gubeli, P. Degiarenko, and L. Dabill. "Photon Activation Analysis in Gallium, Nickel, and Vanadium." In 14th International Topical Meeting on Nuclear Applications of Accelerators. Illinois: American Nuclear Society, 2021. http://dx.doi.org/10.13182/t125-37162.

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Vartsky, David, and Mark B. Goldberg. "Body composition studies: neutron activation analysis vs nuclear resonance absorption." In Fifth International Conference on Applications of Nuclear Techniques: Neutrons in Research and Industry, edited by George Vourvopoulos. SPIE, 1997. http://dx.doi.org/10.1117/12.267938.

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Cabellos, O., N. Garc, J. Sanz, S. Reyes, P. Fernández, and B. Fernández. "Effect of activation cross section uncertainties in transmutation analysis of realistic low-activation steels for IFMIF." In International Conference on Nuclear Data for Science and Technology. Les Ulis, France: EDP Sciences, 2007. http://dx.doi.org/10.1051/ndata:07337.

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Ruddy, Frank H., John G. Seidel, and Robert W. Flammang. "Prompt Pulsed Neutron Activation Analysis for Detection of Fission Neutrons." In 2006 IEEE Nuclear Science Symposium Conference Record. IEEE, 2006. http://dx.doi.org/10.1109/nssmic.2006.356112.

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Dallimore, M., G. Crossingham, and D. Ramsden. "High-resolution scintillation spectrometers for neutron-activation analysis." In 2003 IEEE Nuclear Science Symposium. Conference Record (IEEE Cat. No.03CH37515). IEEE, 2003. http://dx.doi.org/10.1109/nssmic.2003.1351797.

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Baljinnyam, N., B. Jugder, N. Norov, M. V. Frontasyeva, T. M. Ostrovnaya, S. S. Pavlov, Dugersuren Dashdorj, and Gary E. Mitchell. "Epithermal Neutron Activation Analysis of the Asian Herbal Plants." In SECOND INTERNATIONAL ULAANBAATAR CONFERENCE ON NUCLEAR PHYSICS AND APPLICATIONS. AIP, 2011. http://dx.doi.org/10.1063/1.3583172.

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Reports on the topic "Nuclear activation analysis"

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Trkov, Andrej. Summary Report from the Technical Meeting on Nuclear Data for Neutron Activation Analysis and Dosimetry. IAEA Nuclear Data Section, August 2019. http://dx.doi.org/10.61092/iaea.pcrs-xry3.

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Shaw, D. M., and P. L. C. Smith. Prompt gamma neutron activation analysis of SRMS at the McMaster Nuclear Reactor in 1990 and the future prospects. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 1993. http://dx.doi.org/10.4095/193293.

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Schwantes, Jon M., Christopher R. Orton, and Richard A. Clark. Analysis of a Nuclear Accident: Fission and Activation Product Releases from the Fukushima Daiichi Nuclear Facility as Remote Indicators of Source Identification, Extent of Release, and State of Damaged Spent Nuclear Fuel. Office of Scientific and Technical Information (OSTI), December 2011. http://dx.doi.org/10.2172/1076730.

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Barkan, Alice, and Zach Adam. The Role of Proteases in Regulating Gene Expression and Assembly Processes in the Chloroplast. United States Department of Agriculture, January 2003. http://dx.doi.org/10.32747/2003.7695852.bard.

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Chloroplasts house many biochemical processes that are essential for plant viability. Foremost, among these is photosynthesis, which requires the protein-rich thylakoid membrane system. The activation of chloroplast genes encoding thylakoid membrane proteins and the targeting and assembly of these proteins together with their nuclear-encoded partners are essential for the elaboration of the thylakoid membrane. Several nuclear-encoded proteins that regulate chloroplast gene expression and that mediate the targeting of proteins to the thylakoid membrane have been identified in recent years, and many more remain to be discovered. The abundance of such proteins is critical and is likely to be determined to a significant extent by their stability, which in turn, is influenced by chloroplast protease activities. The primary goal of this project was to link specific proteases to specific substrates, and in particular, to specific regulatory and assembly proteins. We proposed a two-pronged approach, involving genetic analysis of the consequences of the mutational loss of chloroplast proteases, and biochemical analysis of the degradation pathways of specific proteins that have been shown to control chloroplast gene expression. Our initial bioinformatic analysis of chloroplast proteases allowed us to identify the set of pro teases that is targeted to the chloroplast. We used that information to recover three Arabidopsis mutants with T - DNA insertions in specific chloroplast protease genes. We carried out the first analysis of the stability of a regulator of chloroplast gene expression (CRS2), and found that the protein is much less stable than are typical components of the photosynthetic apparatus. Genetic reagents and analytical methods were developed that have set the stage for a rapid advancement of our understanding of chloroplast proteolysis. The results obtained may be useful for manipulating the expression of transgenes in the chloroplast and for engineering plants whose photosynthetic activity is optimized under harsh environmental conditions.
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Sessa, Guido, and Gregory Martin. Role of GRAS Transcription Factors in Tomato Disease Resistance and Basal Defense. United States Department of Agriculture, 2005. http://dx.doi.org/10.32747/2005.7696520.bard.

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The research problem: Bacterial spot and bacterial speck diseases of tomato are causedby strains of Xanthomonas campestris pv. vesicatoria (Xcv) and Pseudomonas syringae pv.tomato (Pst), respectively. These bacteria colonize aerial parts of the plant and causesignificant losses in tomato production worldwide. Protection against Xcv and Pst bycultural practices or chemical control has been unsuccessful and there are only limitedsources of genetic resistance to these pathogens. In previous research supported in part byBARD IS-3237-01, we extensively characterized changes in tomato gene expression uponthe onset of spot and speck disease resistance. A remarkable finding of these studies wasthe inducibility in tomato leaves by both Xcv and Pst strains of genes encodingtranscriptional activator of the GRAS family, which has not been previously linked todisease resistance. Goals: Central goals of this research were to investigate the role of GRAS genes in tomatoinnate immunity and to assess their potential use for disease control.Specific objectives were to: 1. Identify GRAS genes that are induced in tomato during thedefense response and analyze their role in disease resistance by loss-of-function experiments.2. Overexpress GRAS genes in tomato and characterize plants for possible broad-spectrumresistance. 3. Identify genes whose transcription is regulated by GRAS family. Our main achievements during this research program are in three major areas:1. Identification of tomato GRAS family members induced in defense responses andanalysis of their role in disease resistance. Genes encoding tomato GRAS family memberswere retrieved from databases and analyzed for their inducibility by Pst avirulent bacteria.Real-time RT-PCR analysis revealed that six SlGRAS transcripts are induced during theonset of disease resistance to Pst. Further expression analysis of two selected GRAS genesshowed that they accumulate in tomato plants in response to different avirulent bacteria orto the fungal elicitor EIX. In addition, eight SlGRAS genes, including the Pst-induciblefamily members, were induced by mechanical stress in part in a jasmonic acid-dependentmanner. Remarkably, SlGRAS6 gene was found to be required for tomato resistance to Pstin virus-induced gene silencing (VIGS) experiments.2. Molecular analysis of pathogen-induced GRAS transcriptional activators. In aheterologous yeast system, Pst-inducible GRAS genes were shown to have the ability toactivate transcription in agreement with their putative function of transcription factors. Inaddition, deletion analysis demonstrated that short sequences at the amino-terminus ofSlGRAS2, SlGRAS4 and SlGRAS6 are sufficient for transcriptional activation. Finally,defense-related SlGRAS proteins were found to localize to the cell nucleus. 3. Disease resistance and expression profiles of transgenic plants overexpressing SlGRASgenes. Transgenic plants overexpressing SlGRAS3 or SlGRAS6 were generated. Diseasesusceptibility tests revealed that these plants are not more resistant to Pst than wild-typeplants. Gene expression profiles of the overexpressing plants identified putative direct orindirect target genes regulated by SlGRAS3 and SlGRAS6. Scientific and agricultural significance: Our research activities established a novel linkbetween the GRAS family of transcription factors, plant disease resistance and mechanicalstress response. SlGRAS6 was found to be required for disease resistance to Pstsuggesting that this and possibly other GRAS family members are involved in thetranscriptional reprogramming that takes place during the onset of disease resistance.Their nuclear localization and transcriptional activation ability support their proposed roleas transcription factors or co-activators. However, the potential of utilizing GRAS familymembers for the improvement of plant disease resistance in agriculture has yet to bedemonstrated.
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Lers, Amnon, and Pamela J. Green. LX Senescence-Induced Ribonuclease in Tomato: Function and Regulation. United States Department of Agriculture, September 2003. http://dx.doi.org/10.32747/2003.7586455.bard.

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Natural leaf senescence, which occurs even when growth conditions are near optimal, has a negative influence on yield. Postharvest induced senescence contributes to the losses of quality in flowers, foliage, and vegetables. Strategies designed to control the senescence process in crop plants could therefore have great applied significance. However, the successful design of such strategies requires a better insight into the senescence machinery and control in higher plants. A main feature of senescence is the hydrolysis of macromolecules by hydrolases of various types such as ribonucleases (RNases) and proteases. Previously we had identified and characterized the tomato LX RNase gene demonstrating its transcript to be highly and specifically induced during senescence. This reported study was focused on LX but also had broadened our research to other senescence-associated nucleic acids degrading enzymes to learn about their function and the regulation of their encoding genes. Beside tomato we used parsley and Arabidopsis for the study of: the bi-functional nuclease which has a role in senescence. The study of different senescence- associated nucleases in few plant systems will allow a more general view on function and regulation of these enzymes in senescence. The specific original proposed objectives included: 1. Study the consequences of alterations in LX RNase level on tomato leaf senescence and general development; 2. Analyze stimuli which may participate in senescence-specific activation of the LX gene; 3. Clone the senescence-associated BFNI nuclease gene homologue from tomato. 4. Further characterize the sequences required for senescence-specific gene expression. Homozygous transgenic plants in which LX gene was either inhibited or over-expressed were generated. In both of these LX mutated plants no major phenotypic consequences were observed, which may suggests that LX is not essential for plant growth under optimal growth conditions. Lack of any abnormalities in the LX over-expressing lines suggests that special system exist to allow function of the RNase only when needed. Detailed analyses of growth under stress and consequences to RNA metabolism are underway. We have analyzed LX expression on the protein level demonstrating that it is involved also in petal senescing. Our results suggest that LX is responding to complex regulation involving developmental, organ dependent factors and responds differently to hormonal or environmental stimuli in the different plant organs. The cloned 1.4 kb promoter was cloned and its analysis revealed that probably not all required elements for senescence induction are included. Biochemical analysis of senescence-associated be-functional nucleases in the different plants, tomato, parsley and Arabidopsis, suggests they belong to a sub-class within the type I plant nucleases. The parsley PcNUC1/2 nuclease protein was purified from senescing leaves its and activity was studied in vitro revealing endo-, double strand, nucleolytic activity and exo-nucleolytic activity. Its encoding gene was cloned and found to be induced on the mRNA level. The promoter of the related Arabidopsis BFNI nuclease was shown in both tomato and Arabidopsis to be able and direct senescence-specific expression suggesting that, at least part, the gene is regulated on the transcriptional level and that the mechanism for this senescence-specific regulation is conserved between different plants. Few plants in which the BFNI gene is mutated were identified which are subjected now to detailed analysis. Our results suggest that the senescence-related nucleic acid degrading enzymes share similarities in both function and regulation between different plants and possibly have important functions in processes un-related to senescence. Still, the function of these enzymes, at least in some cases is not essential to plant development under optimal growth conditions. We are now at the stage which permits in depth investigation of the specific functions and mode of molecular regulation of senescence-associated nucleases with the aid of the research tools developed. The isolated senescence-specific promoter, shown to be active in heterologous plant system, could be utilized in agricultural-related biotechnological applications for retardation of senescence.
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