Статті в журналах з теми "Rubisco"
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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.
Whitney, Spencer M., Rosemary Birch, Celine Kelso, Jennifer L. Beck, and Maxim V. Kapralov. "Improving recombinant Rubisco biogenesis, plant photosynthesis and growth by coexpressing its ancillary RAF1 chaperone." Proceedings of the National Academy of Sciences 112, no. 11 (March 2, 2015): 3564–69. http://dx.doi.org/10.1073/pnas.1420536112.
Elsaied, Hosam, and Takeshi Naganuma. "Phylogenetic Diversity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Large-Subunit Genes from Deep-Sea Microorganisms." Applied and Environmental Microbiology 67, no. 4 (April 1, 2001): 1751–65. http://dx.doi.org/10.1128/aem.67.4.1751-1765.2001.
Morell, MK, K. Paul, HJ Kane, and TJ Andrews. "Rubisco: Maladapted or Misunderstood." Australian Journal of Botany 40, no. 5 (1992): 431. http://dx.doi.org/10.1071/bt9920431.
Rydzy, Małgorzata, Michał Tracz, Andrzej Szczepaniak, and Joanna Grzyb. "Insights into the Structure of Rubisco from Dinoflagellates-in Silico Studies." International Journal of Molecular Sciences 22, no. 16 (August 7, 2021): 8524. http://dx.doi.org/10.3390/ijms22168524.
Valegård, Karin, Dirk Hasse, Inger Andersson, and Laura H. Gunn. "Structure of Rubisco fromArabidopsis thalianain complex with 2-carboxyarabinitol-1,5-bisphosphate." Acta Crystallographica Section D Structural Biology 74, no. 1 (January 1, 2018): 1–9. http://dx.doi.org/10.1107/s2059798317017132.
Wei, Xueming, Luis A. Sayavedra-Soto, and Daniel J. Arp. "The transcription of the cbb operon in Nitrosomonas europaea." Microbiology 150, no. 6 (June 1, 2004): 1869–79. http://dx.doi.org/10.1099/mic.0.26785-0.
Poudel, Saroj, Douglas H. Pike, Hagai Raanan, Joshua A. Mancini, Vikas Nanda, Rosalind E. M. Rickaby, and Paul G. Falkowski. "Biophysical analysis of the structural evolution of substrate specificity in RuBisCO." Proceedings of the National Academy of Sciences 117, no. 48 (November 16, 2020): 30451–57. http://dx.doi.org/10.1073/pnas.2018939117.
Baker, Stefanie H., Songmu Jin, Henry C. Aldrich, Gary T. Howard, and Jessup M. Shively. "Insertion Mutation of the Form I cbbL Gene Encoding Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) in Thiobacillus neapolitanus Results in Expression of Form II RuBisCO, Loss of Carboxysomes, and an Increased CO2 Requirement for Growth." Journal of Bacteriology 180, no. 16 (August 15, 1998): 4133–39. http://dx.doi.org/10.1128/jb.180.16.4133-4139.1998.
Young, J. N., R. E. M. Rickaby, M. V. Kapralov, and D. A. Filatov. "Adaptive signals in algal Rubisco reveal a history of ancient atmospheric carbon dioxide." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1588 (February 19, 2012): 483–92. http://dx.doi.org/10.1098/rstb.2011.0145.
Raven, John A., Mario Giordano, John Beardall, and Stephen C. Maberly. "Algal evolution in relation to atmospheric CO 2 : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1588 (February 19, 2012): 493–507. http://dx.doi.org/10.1098/rstb.2011.0212.
Schulz, Luca, Zhijun Guo, Jan Zarzycki, Wieland Steinchen, Jan M. Schuller, Thomas Heimerl, Simone Prinz, Oliver Mueller-Cajar, Tobias J. Erb, and Georg K. A. Hochberg. "Evolution of increased complexity and specificity at the dawn of form I Rubiscos." Science 378, no. 6616 (October 14, 2022): 155–60. http://dx.doi.org/10.1126/science.abq1416.
Waheeda, Kazi, and Po-Lin Chiu. "Complex formation of rubisco and rubisco activase." Biophysical Journal 121, no. 3 (February 2022): 452a. http://dx.doi.org/10.1016/j.bpj.2021.11.520.
Sage, Rowan F., Danielle A. Way, and David S. Kubien. "Rubisco, Rubisco activase, and global climate change." Journal of Experimental Botany 59, no. 7 (April 23, 2008): 1581–95. http://dx.doi.org/10.1093/jxb/ern053.
Portis, A. R. "The regulation of Rubisco by Rubisco activase." Journal of Experimental Botany 46, special (September 1, 1995): 1285–91. http://dx.doi.org/10.1093/jxb/46.special_issue.1285.
Karthick, Palanivelu Vikram, Alagarswamy Senthil, Maduraimuthu Djanaguiraman, Kuppusamy Anitha, Ramalingam Kuttimani, Parasuraman Boominathan, Ramasamy Karthikeyan, and Muthurajan Raveendran. "Improving Crop Yield through Increasing Carbon Gain and Reducing Carbon Loss." Plants 13, no. 10 (May 10, 2024): 1317. http://dx.doi.org/10.3390/plants13101317.
Toyoda, Koichi, Yoichi Yoshizawa, Hiroyuki Arai, Masaharu Ishii, and Yasuo Igarashi. "The role of two CbbRs in the transcriptional regulation of three ribulose-1,5-bisphosphate carboxylase/oxygenase genes in Hydrogenovibrio marinus strain MH-110." Microbiology 151, no. 11 (November 1, 2005): 3615–25. http://dx.doi.org/10.1099/mic.0.28056-0.
Yoshizawa, Yoichi, Koichi Toyoda, Hiroyuki Arai, Masaharu Ishii, and Yasuo Igarashi. "CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and Carboxysomes in Hydrogenovibrio marinus Strain MH-110." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5685–91. http://dx.doi.org/10.1128/jb.186.17.5685-5691.2004.
Singh, Jaya, and F. Robert Tabita. "Roles of RubisCO and the RubisCO-Like Protein in 5-Methylthioadenosine Metabolism in the Nonsulfur Purple Bacterium Rhodospirillum rubrum." Journal of Bacteriology 192, no. 5 (December 28, 2009): 1324–31. http://dx.doi.org/10.1128/jb.01442-09.
Xiang, Fu, Yuanping Fang, and Jun Xiang. "Structural and evolutionary relationships among RuBisCOs inferred from their large and small subunits." Zeitschrift für Naturforschung C 71, no. 5-6 (May 1, 2016): 181–89. http://dx.doi.org/10.1515/znc-2016-0014.
Demirevska-Kepova, Klimentina, and Urs Feller. "Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants." Acta Physiologiae Plantarum 26, no. 1 (March 2004): 103–14. http://dx.doi.org/10.1007/s11738-004-0050-7.
Hotto, Amber M., Coralie Salesse-Smith, Myat Lin, Florian A. Busch, Isabelle Simpson, and David B. Stern. "Rubisco production in maize mesophyll cells through ectopic expression of subunits and chaperones." Journal of Experimental Botany 72, no. 13 (April 30, 2021): 4930–37. http://dx.doi.org/10.1093/jxb/erab189.
Madhavan, S., M. S. Miller-Goodman, and K. W. Lee. "Immunolocalization of Rubisco Activase and Rubisco in C3 and C4 Plant Tissues." Microscopy and Microanalysis 6, S2 (August 2000): 472–73. http://dx.doi.org/10.1017/s1431927600034851.
Yokota, Akiho. "Revisiting RuBisCO." Bioscience, Biotechnology, and Biochemistry 81, no. 11 (September 27, 2017): 2039–49. http://dx.doi.org/10.1080/09168451.2017.1379350.
Portis, Archie R. "Rubisco activase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1015, no. 1 (January 1990): 15–28. http://dx.doi.org/10.1016/0005-2728(90)90211-l.
Feng, Yujiao, Hao Wu, Huanhuan Liu, Yonghui He, and Zhitong Yin. "Effects of OsRCA Overexpression on Rubisco Activation State and Photosynthesis in Maize." Plants 12, no. 8 (April 11, 2023): 1614. http://dx.doi.org/10.3390/plants12081614.
Raunser, S., R. Magnani, Z. Huang, R. L. Houtz, R. C. Trievel, P. A. Penczek, and T. Walz. "Rubisco in complex with Rubisco large subunit methyltransferase." Proceedings of the National Academy of Sciences 106, no. 9 (February 10, 2009): 3160–65. http://dx.doi.org/10.1073/pnas.0810563106.
SEVİNDİK, Emre. "Amino Acids Sequence Based in Silico Analysis of RuBisCO (Ribulose-1,5 Bisphosphate Carboxylase Oxygenase) Proteins in Some Carthamus L. ssp." Notulae Scientia Biologicae 9, no. 2 (June 30, 2017): 204–8. http://dx.doi.org/10.15835/nsb9210053.
Witte, Brian, David John, Boris Wawrik, John H. Paul, David Dayan, and F. Robert Tabita. "Functional Prokaryotic RubisCO from an Oceanic Metagenomic Library." Applied and Environmental Microbiology 76, no. 9 (March 12, 2010): 2997–3003. http://dx.doi.org/10.1128/aem.02661-09.
Suganami, Mao, Yuji Suzuki, Eri Kondo, Shinji Nishida, So Konno, and Amane Makino. "Effects of Overproduction of Rubisco Activase on Rubisco Content in Transgenic Rice Grown at Different N Levels." International Journal of Molecular Sciences 21, no. 5 (February 27, 2020): 1626. http://dx.doi.org/10.3390/ijms21051626.
Warren, Charles R., Mark A. Adams, and ZuLiang Chen. "Is photosynthesis related to concentrations of nitrogen and Rubisco in leaves of Australian native plants?" Functional Plant Biology 27, no. 5 (2000): 407. http://dx.doi.org/10.1071/pp98162.
Roh, Kwang-Soo. "Influence of Nitrate on Growth, Chlorophyll Content, Content and Activity of Rubisco and Rubisco Activase of Tobacco Plant Treated with Cadmium in vitro." Journal of Life Science 20, no. 11 (November 30, 2010): 1667–74. http://dx.doi.org/10.5352/jls.2010.20.11.1667.
Cheng, Lailiang, and Leslie H. Fuchigami. "Photometric Measurements of Rubisco Activity in Leaves of Deciduous Fruit Crops." HortScience 32, no. 3 (June 1997): 531A—531. http://dx.doi.org/10.21273/hortsci.32.3.531a.
Watson, Gregory M. F., Jae-Pil Yu, and F. Robert Tabita. "Unusual Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase of Anoxic Archaea." Journal of Bacteriology 181, no. 5 (March 1, 1999): 1569–75. http://dx.doi.org/10.1128/jb.181.5.1569-1575.1999.
MARTÍNEZ-BARAJAS, E., J. MOLINA-GALÁN, and E. SÁNCHEZ de JIMÉNEZ. "Regulation of Rubisco activity during grain-fill in maize: possible role of Rubisco activase." Journal of Agricultural Science 128, no. 2 (March 1997): 155–61. http://dx.doi.org/10.1017/s002185969600408x.
Cheng, Lailiang, and Leslie H. Fuchigami. "The Relationship between Rubisco Activity and Photosynthesis in Apple Leaves with Different Nitrogen Content." HortScience 32, no. 3 (June 1997): 530E—531. http://dx.doi.org/10.21273/hortsci.32.3.530e.
O'Leary, Brendan M., Andrew P. Scafaro, Ricarda Fenske, Owen Duncan, Elke Ströher, Jakob Petereit, and A. Harvey Millar. "Rubisco lysine acetylation occurs at very low stoichiometry in mature Arabidopsis leaves: implications for regulation of enzyme function." Biochemical Journal 477, no. 19 (October 12, 2020): 3885–96. http://dx.doi.org/10.1042/bcj20200413.
Tabita, F. Robert, Thomas E. Hanson, Sriram Satagopan, Brian H. Witte, and Nathan E. Kreel. "Phylogenetic and evolutionary relationships of RubisCO and the RubisCO-like proteins and the functional lessons provided by diverse molecular forms." Philosophical Transactions of the Royal Society B: Biological Sciences 363, no. 1504 (May 16, 2008): 2629–40. http://dx.doi.org/10.1098/rstb.2008.0023.
Guo, Xue, Huaqun Yin, Jing Cong, Zhimin Dai, Yili Liang, and Xueduan Liu. "RubisCO Gene Clusters Found in a Metagenome Microarray from Acid Mine Drainage." Applied and Environmental Microbiology 79, no. 6 (January 18, 2013): 2019–26. http://dx.doi.org/10.1128/aem.03400-12.
Khaembah, Edith N., François Gastal, Serge Carre, Louis J. Irving, Philippe Barre, and Cory Matthew. "Morphology and Rubisco turnover characteristics of perennial ryegrass breeding populations after two and four cycles of divergent selection for long or short leaf length." Crop and Pasture Science 64, no. 7 (2013): 687. http://dx.doi.org/10.1071/cp13066.
Woodrow, IE, ME Kelly, and KA Mott. "Limitation of the Rate of Ribulosebisphosphate Carboxylase Activation by Carbamylation and Ribulosebisphosphate Carboxylase Activase Activity: Development and Tests of a Mechanistic Model." Functional Plant Biology 23, no. 2 (1996): 141. http://dx.doi.org/10.1071/pp9960141.