Добірка наукової літератури з теми "Rubisco"
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Статті в журналах з теми "Rubisco":
Valente, Ana I., Ana M. Ferreira, Mafalda R. Almeida, Aminou Mohamadou, Mara G. Freire, and Ana P. M. Tavares. "Efficient Extraction of the RuBisCO Enzyme from Spinach Leaves Using Aqueous Solutions of Biocompatible Ionic Liquids." Sustainable Chemistry 3, no. 1 (December 24, 2021): 1–18. http://dx.doi.org/10.3390/suschem3010001.
McNevin, Dennis B., Murray R. Badger, Spencer M. Whitney, Susanne von Caemmerer, Guillaume G. B. Tcherkez, and Graham D. Farquhar. "Differences in Carbon Isotope Discrimination of Three Variants of D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Reflect Differences in Their Catalytic Mechanisms." Journal of Biological Chemistry 282, no. 49 (October 9, 2007): 36068–76. http://dx.doi.org/10.1074/jbc.m706274200.
Whitney, Spencer M., and T. John Andrews. "The CO2/O2 specificity of single-subunit ribulose-bisphosphate carboxylase from the dinoflagellate, Amphidinium carterae." Functional Plant Biology 25, no. 2 (1998): 131. http://dx.doi.org/10.1071/pp97131.
Mueller-Cajar, Oliver, and Spencer M. Whitney. "Evolving improved Synechococcus Rubisco functional expression in Escherichia coli." Biochemical Journal 414, no. 2 (August 12, 2008): 205–14. http://dx.doi.org/10.1042/bj20080668.
Iqbal, Wasim A., Isabel G. Miller, Rebecca L. Moore, Iain J. Hope, Daniel Cowan-Turner, and Maxim V. Kapralov. "Rubisco substitutions predicted to enhance crop performance through carbon uptake modelling." Journal of Experimental Botany 72, no. 17 (June 11, 2021): 6066–75. http://dx.doi.org/10.1093/jxb/erab278.
Utåker, Janne B., Kjell Andersen, Ågot Aakra, Birgitte Moen, and Ingolf F. Nes. "Phylogeny and Functional Expression of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from the Autotrophic Ammonia-Oxidizing Bacterium Nitrosospira sp.Isolate 40KI." Journal of Bacteriology 184, no. 2 (January 15, 2002): 468–78. http://dx.doi.org/10.1128/jb.184.2.468-478.2002.
Ng, Jediael, Zhijun Guo, and Oliver Mueller-Cajar. "Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco." Journal of Biological Chemistry 295, no. 48 (September 18, 2020): 16427–35. http://dx.doi.org/10.1074/jbc.ra120.015759.
Wang, Renée Z., Albert K. Liu, Douglas M. Banda, Woodward W. Fischer, and Patrick M. Shih. "A Bacterial Form I’ Rubisco Has a Smaller Carbon Isotope Fractionation than Its Form I Counterpart." Biomolecules 13, no. 4 (March 26, 2023): 596. http://dx.doi.org/10.3390/biom13040596.
Loganathan, Nitin, Yi-Chin Candace Tsai, and Oliver Mueller-Cajar. "Characterization of the heterooligomeric red-type rubisco activase from red algae." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): 14019–24. http://dx.doi.org/10.1073/pnas.1610758113.
Tabita, F. Robert, Thomas E. Hanson, Huiying Li, Sriram Satagopan, Jaya Singh, and Sum Chan. "Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs." Microbiology and Molecular Biology Reviews 71, no. 4 (December 2007): 576–99. http://dx.doi.org/10.1128/mmbr.00015-07.
Дисертації з теми "Rubisco":
Milward, Sara Eve. "Interrogating plant Rubisco-Rubisco activase interactions." Phd thesis, Canberra, ACT : The Australian National University, 2018. http://hdl.handle.net/1885/149565.
Keown, Jeremy Russell. "Rubisco's chiropractor: a study of higher plant Rubisco activase." Thesis, University of Canterbury. School of Biology, 2015. http://hdl.handle.net/10092/10398.
Saschenbrecker, Sandra. "Folding and assembly of RuBisCO." Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-75775.
Girnus, Jan. "Regulation of Rubisco in CAM plants." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.616010.
Singh, Jaya. "Functional Relationships Among Rubisco Family Members." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1220413240.
Bošková, Martina. "Vliv stáří jehlic na obsah a aktivitu enzymu Rubisco u smrku ztepilého v podmínkách normální a zvýšené koncentrace CO2." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2009. http://www.nusl.cz/ntk/nusl-216513.
Butt, Mohammed Salman. "Technologies and methods to characterise Rubisco function." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/39375.
Wietrzynski, Wojciech. "Rubisco biogenesis and assembly in Chlamydomonas reinhardtii." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066336/document.
The necessity to coordinate the expression of genes originating from different genomes within the plant cell resulted in the appearance of mechanisms imposing nuclear control over organelle gene expression. Anterograde signaling through sequence-specific trans-acting proteins (OTAFs) coexists in the chloroplast with an assembly dependent control of chloroplast synthesis (CES process) that coordinates the stoichiometric formation of photosynthetic complexes.Ribulose bisphosphate carboxylase/oxygenase (Rubisco) is a chloroplast-located carbon fixing enzyme constituted of two subunits. Large subunit (LSU) and small subunit (SSU) are encoded in the chloroplast and nuclear genomes respectively. In the stroma they assemble to form a hexadecameric holoenzyme (LSU8SSU8). In this study I tried to highlight major regulatory points of its synthesis in Chlamydomonas reinhardtii focusing on the posttranscriptional regulation of LSU.I showed that the MRL1 PPR protein is a limiting factor for rbcL mRNA accumulation. Whereas it has been previously designated as a stabilization factor for the abovementioned transcript, MRL1 appeared also to have a function in rbcL translation.Most notably, I have demonstrated that in Chlamydomonas reinhardtii Rubisco expression is controlled by the small subunit (SSU) presence. In its absence rbcL undergoes an inhibition of translation through its own product – the unassembled Rubisco large subunit. This process depends on LSU-oligomerization state as I was able to show that the presence of a high order LSU assembly intermediate bound to the RAF1 assembly chaperone is essential for the regulation to occur. In parallel I shed light on the fate of unassembled LSU in a deregulated CES context, thereby improving our understanding of the process of its folding and assembly
Wietrzynski, Wojciech. "Rubisco biogenesis and assembly in Chlamydomonas reinhardtii." Electronic Thesis or Diss., Paris 6, 2017. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2017PA066336.pdf.
The necessity to coordinate the expression of genes originating from different genomes within the plant cell resulted in the appearance of mechanisms imposing nuclear control over organelle gene expression. Anterograde signaling through sequence-specific trans-acting proteins (OTAFs) coexists in the chloroplast with an assembly dependent control of chloroplast synthesis (CES process) that coordinates the stoichiometric formation of photosynthetic complexes.Ribulose bisphosphate carboxylase/oxygenase (Rubisco) is a chloroplast-located carbon fixing enzyme constituted of two subunits. Large subunit (LSU) and small subunit (SSU) are encoded in the chloroplast and nuclear genomes respectively. In the stroma they assemble to form a hexadecameric holoenzyme (LSU8SSU8). In this study I tried to highlight major regulatory points of its synthesis in Chlamydomonas reinhardtii focusing on the posttranscriptional regulation of LSU.I showed that the MRL1 PPR protein is a limiting factor for rbcL mRNA accumulation. Whereas it has been previously designated as a stabilization factor for the abovementioned transcript, MRL1 appeared also to have a function in rbcL translation.Most notably, I have demonstrated that in Chlamydomonas reinhardtii Rubisco expression is controlled by the small subunit (SSU) presence. In its absence rbcL undergoes an inhibition of translation through its own product – the unassembled Rubisco large subunit. This process depends on LSU-oligomerization state as I was able to show that the presence of a high order LSU assembly intermediate bound to the RAF1 assembly chaperone is essential for the regulation to occur. In parallel I shed light on the fate of unassembled LSU in a deregulated CES context, thereby improving our understanding of the process of its folding and assembly
Zítková, Jana. "Vliv zvýšené koncentrace oxidu uhličitého na denní chod obsahu a aktivity enzymu Rubisco." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2011. http://www.nusl.cz/ntk/nusl-216688.
Книги з теми "Rubisco":
Martin, Gillian Clare. The use of Rubisco in the study of orchid hybridization. Birmingham: Universityof Birmingham, 1987.
Galmés, Jeroni. La Rubisco, el punt d'inici de la vida: Significat ecològic i una possible clau per a la millora genètica de la productivitat vegetal. Palma: Hiperdimensional, 2006.
Kopf, Gail. Rubicon. Nashville: T. Nelson Publishers, 1993.
John, Hooker. Rubicon. Ringwood, Vic., Australia: Penguin Books, 1991.
Alexander, Lawrence. Rubicon. New York: William Morrow, 2008.
Saylor, Steven. Rubicon. New York: St. Martin's Press, 1999.
Garamvölgyi, László. Rubicon. Budapest: BTR Kft., 2000.
Erickson, Steve. Rubicon Beach. New York: Vintage Books, 1987.
Dennis, Jones. Rubicon one. London: Arrow, 1985.
Erickson, Steve. Rubicon Beach. New York: Poseidon Press, 1986.
Частини книг з теми "Rubisco":
Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 1485. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1395.
Liu, Cuimin, Kaiyao Huang, and Jianrong Xia. "Rubisco." In Research Methods of Environmental Physiology in Aquatic Sciences, 65–74. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-5354-7_7.
Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 2224. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1395.
Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1395-2.
Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 2702. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1395.
Andrews, T. John, Susanne von Caemmerer, Colleen J. Mate, Graham S. Hudson, and John R. Evans. "The Regulation of Rubisco Catalysis by Rubisco Activase." In Photosynthesis: from Light to Biosphere, 3909–14. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_920.
Portis, Archie R., Brian Esau, Eric M. Larson, Genhai Zhu, Chris J. Chastain, Carolyn M. O’Brien, and Robert J. Spreitzer. "Characteristics of the Interaction between Rubisco and Rubisco Activase." In Photosynthesis: from Light to Biosphere, 3933–38. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_924.
Haslam, Richard P., Alfred J. Keys, P. John Andralojc, Pippa J. Madgwick, Andersson Inger, Anette Grimsrud, Hans C. Eilertsen, and Martin A. J. Parry. "Specificity of diatom Rubisco." In Plant Responses to Air Pollution and Global Change, 157–64. Tokyo: Springer Japan, 2005. http://dx.doi.org/10.1007/4-431-31014-2_18.
Andrews, T. John, Murray R. Badger, Daryl L. Edmondson, Heather J. Kane, Matthew K. Morell, and Kalanethee Paul. "Rubisco: Subunits and Mechanism." In Current Research in Photosynthesis, 2237–44. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_511.
Wu, Xiang-yu, Wei Gu, and Guang-yao Wu. "Rubisco from Amaranthus Hypochondriacus." In Current Research in Photosynthesis, 2245–48. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_512.
Тези доповідей конференцій з теми "Rubisco":
Zhou, Hualu, Giang Vu, and David J. McClements. "Rubisco Proteins as Plant-based Alternatives to Egg White Proteins: Characterization of Thermal Gelation Properties." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/vamx3998.
Callaghan, Jake. "NOVEL ARCHAEAL LINEAGES UTILIZING RUBISCO IN LAKE SUPERIOR SEDIMENTS." In 54th Annual GSA North-Central Section Meeting - 2020. Geological Society of America, 2020. http://dx.doi.org/10.1130/abs/2020nc-348067.
Gao, Lan. "Structure of a Novel Rubisco Activase in Gardenia jasminoides." In 2018 2nd International Conference on Advances in Energy, Environment and Chemical Science (AEECS 2018). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/aeecs-18.2018.8.
Kacar, Betul, Zachary R. Adam, Victor Hanson-Smith, and Nicholas Boekelheide. "CONSTRAINING THE GREAT OXIDATION EVENT WITHIN THE RUBISCO PHYLOGENETIC TREE." In GSA Annual Meeting in Denver, Colorado, USA - 2016. Geological Society of America, 2016. http://dx.doi.org/10.1130/abs/2016am-287360.
Holden, Todd, S. Dehipawala, E. Cheung, R. Bienaime, J. Ye, G. Tremberger, Jr., P. Schneider, D. Lieberman, and T. Cheung. "Diverse nucleotide compositions and sequence fluctuation in Rubisco protein genes." In SPIE Optical Engineering + Applications, edited by Richard B. Hoover, Paul C. W. Davies, Gilbert V. Levin, and Alexei Y. Rozanov. SPIE, 2011. http://dx.doi.org/10.1117/12.893434.
Babani, Salma I., Chukwuma C. Ogbaga, Dominic Okolo, and George Mangse. "Bioactive Compound and Rubisco Analyses of Leaf and Seed Extracts of Sesamum indicum." In 2019 15th International Conference on Electronics, Computer and Computation (ICECCO). IEEE, 2019. http://dx.doi.org/10.1109/icecco48375.2019.9043249.
Yesiltas, Betül, Pedro J. García-Moreno, Egon B. Hansen, Paolo Marcatili, Tobias H. Olsen, Simon Gregersen, and Charlotte Jacobsen. "Antioxidant Activity of Peptides Embedded in Potato, Seaweed, Rubisco and Single Cell Proteins." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists’ Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.25.
Subramani, Boopathi, and Kuo-Yuan Hwa. "In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family." In 2010 2nd International Conference on Information Technology Convergence and Services (ITCS). IEEE, 2010. http://dx.doi.org/10.1109/itcs.2010.5581267.
Ogbaga, Chukwuma C., Rashida A. Maishanu, and Dominic Okolo. "Characterisation of the Rubisco Content and Bioactive Compound Analysis of Leaf and Seed Extracts of Tamarindus indica." In 2019 15th International Conference on Electronics, Computer and Computation (ICECCO). IEEE, 2019. http://dx.doi.org/10.1109/icecco48375.2019.9043238.
Biswas, Ishita, and Debanjan Mitra. "Comparative Analysis of RuBisCO Evolution and Intrinsic Differences: Insights from In Silico Assessment in Cyanobacteria, Monocot, and Dicot Plants." In The 3rd International Electronic Conference on Agronomy. Basel Switzerland: MDPI, 2024. http://dx.doi.org/10.3390/iecag2023-15820.
Звіти організацій з теми "Rubisco":
Salvucci, Michael. Consequences of altering rubisco regulation. Office of Scientific and Technical Information (OSTI), December 2013. http://dx.doi.org/10.2172/1164812.
Spreitzer, Robert Joseph. Role of the Rubisco Small Subunit. Office of Scientific and Technical Information (OSTI), November 2016. http://dx.doi.org/10.2172/1330984.
Zielinski, R. (Structure and expression of nuclear genes encoding rubisco activase). Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/6993018.
Hartman, F. C. Rubisco Mechanism: Dissection of the Enolization Partial Reaction. Final Report. Office of Scientific and Technical Information (OSTI), June 2003. http://dx.doi.org/10.2172/824531.
Zielinski, R. E. Structure and expression of nuclear genes encoding rubisco activase. Final technical report. Office of Scientific and Technical Information (OSTI), June 1994. http://dx.doi.org/10.2172/10154999.
Spreitzer, Robert J. Role of the Rubisco small subunit. Final report for period May 1, 1997--April 30,2000. Office of Scientific and Technical Information (OSTI), October 2000. http://dx.doi.org/10.2172/809467.
Azem, Abdussalam, George Lorimer, and Adina Breiman. Molecular and in vivo Functions of the Chloroplast Chaperonins. United States Department of Agriculture, June 2011. http://dx.doi.org/10.32747/2011.7697111.bard.
Miller, John. Japan Crosses the Rubicon? Fort Belvoir, VA: Defense Technical Information Center, January 2002. http://dx.doi.org/10.21236/ada417346.
Rubiano, Kristian, and Dalia C. Barragán Barrera. ¿Las áreas protegidas sí están protegiendo nuestra biodiversidad? Universidad del Rosario, November 2022. http://dx.doi.org/10.12804/dvcn_10336.36920_num6.
Tabita, F. Robert. Biochemistry and control of the reductive tricarboxylic acid pathway of CO2 fixation and physiological role of the Rubis CO-like protein. Office of Scientific and Technical Information (OSTI), December 2008. http://dx.doi.org/10.2172/943343.