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(en) Amit Dhingra, Archie R. Portis Jr. et Henry Daniell, « Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants », Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no 16, , p. 6315-6320 (PMID15067115, PMCID395966, DOI10.1073/pnas.0400981101, Bibcode2004PNAS..101.6315D, lire en ligne)
(en) Steven J. Crafts-Brandner et Michael E. Salvucci, « Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2 », Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no 24, , p. 13430-13435 (PMID11069297, PMCID27241, DOI10.1073/pnas.230451497, Bibcode2000PNAS...9713430C, lire en ligne)
(en) Ning Zhang, Russell P. Kallis, Robert G. Ewy et Archie R. Portis Jr, « Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform », Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no 5, , p. 3330-3334 (PMID11854454, PMCID122518, DOI10.1073/pnas.042529999, Bibcode2002PNAS...99.3330Z, lire en ligne)
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Christine H. Foyer, Arnold J. Bloom, Guillaume Queval et Graham Noctor, « Photorespiratory Metabolism: Genes, Mutants, Energetics, and Redox Signaling », Annual Review of Plant Biology, vol. 60, no 1, , p. 455–484 (ISSN1543-5008, DOI10.1146/annurev.arplant.043008.091948, lire en ligne, consulté le )
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(en) Samuel G. Wildman, « Along the trail from Fraction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase) », Photosynthesis Research, vol. 73, nos 1-3, , p. 243-250 (PMID16245127, DOI10.1023/A:1020467601966)
(en) Amit Dhingra, Archie R. Portis Jr. et Henry Daniell, « Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants », Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no 16, , p. 6315-6320 (PMID15067115, PMCID395966, DOI10.1073/pnas.0400981101, Bibcode2004PNAS..101.6315D, lire en ligne)
(en) Urs Feller, Iwona Anders et Tadahiko Mae, « Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated », Journal of Experimental Botany, vol. 59, no 7, , p. 1615-1624 (PMID17975207, DOI10.1093/jxb/erm242, lire en ligne)
(en) Le gène des sous-unités L fait partie du génome des chloroplastes chez les plantes (Entrez GeneID: )
(en) T. Lundqvist et G. Schneider, « Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate », Journal of Biological Chemistry, , p. 12604-12611 (PMID1905726, lire en ligne)
(en) Hadi Farazdaghi, « The single-process biochemical reaction of Rubisco: A unified theory and model with the effects of irradiance, CO2 and rate-limiting step on the kinetics of C3 and C4 photosynthesis from gas exchange », Biosystems, vol. 103, no 2, , p. 265-284 (PMID21093535, DOI10.1016/j.biosystems.2010.11.004, lire en ligne)
(en) JIN Song-heng, JIANG De-an, LI Xue-qin et SUN Jun-wei, « Characteristics of photosynthesis in rice plants transformed with an antisense Rubisco activase gene », Journal of Zhejiang University SCIENCE, vol. 5, no 8, , p. 897-899 (PMID15236471, DOI10.1631/jzus.2004.0897, lire en ligne)
(en) P. John Andralojc, Glenn W. Dawson, Martin A. J. Parry et Alfred J. Keys, « Incorporation of carbon from photosynthetic products into 2-carboxyarabinitol-1-phosphate and 2-carboxyarabinitol », Biochemical Journal, vol. 304, no Pt 3, , p. 781-786 (PMID7818481, PMCID1137402, lire en ligne)
(en) Shahnaz Khan, P. John Andralojc, Peter J. Lea et Martin A. J. Parry, « 2′-Carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown », European Journal of Biochemistry / FEBS, vol. 266, no 3, , p. 840-847 (PMID10583377, DOI10.1046/j.1432-1327.1999.00913.x, lire en ligne)
(en) Steven J. Crafts-Brandner et Michael E. Salvucci, « Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2 », Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no 24, , p. 13430-13435 (PMID11069297, PMCID27241, DOI10.1073/pnas.230451497, Bibcode2000PNAS...9713430C, lire en ligne)
(en) Michael E. Salvucci, Katherine W. Osteryoung, Steven J. Crafts-Brandner et Elizabeth Vierling, « Exceptional Sensitivity of Rubisco Activase to Thermal Denaturation in Vitro and in Vivo », Plant Physiology, vol. 127, no 3, , p. 1053-1064 (PMID11706186, PMCID129275, DOI10.1104/pp.010357, lire en ligne)
(en) Ning Zhang, Russell P. Kallis, Robert G. Ewy et Archie R. Portis Jr, « Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform », Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no 5, , p. 3330-3334 (PMID11854454, PMCID122518, DOI10.1073/pnas.042529999, Bibcode2002PNAS...99.3330Z, lire en ligne)
(en) Yehouda Marcus et Michael Gurevitz, « Activation of cyanobacterial RuBP-carboxylase/oxygenase is facilitated by inorganic phosphate via two independent mechanisms », European Journal of Biochemistry, vol. 267, no 19, , p. 5995-6003 (PMID10998060, DOI10.1046/j.1432-1327.2000.01674.x, lire en ligne)
oxfordjournals.org
jxb.oxfordjournals.org
(en) Urs Feller, Iwona Anders et Tadahiko Mae, « Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated », Journal of Experimental Botany, vol. 59, no 7, , p. 1615-1624 (PMID17975207, DOI10.1093/jxb/erm242, lire en ligne)
(en) Michael E. Salvucci, Katherine W. Osteryoung, Steven J. Crafts-Brandner et Elizabeth Vierling, « Exceptional Sensitivity of Rubisco Activase to Thermal Denaturation in Vitro and in Vivo », Plant Physiology, vol. 127, no 3, , p. 1053-1064 (PMID11706186, PMCID129275, DOI10.1104/pp.010357, lire en ligne)
pnas.org
(en) Amit Dhingra, Archie R. Portis Jr. et Henry Daniell, « Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants », Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no 16, , p. 6315-6320 (PMID15067115, PMCID395966, DOI10.1073/pnas.0400981101, Bibcode2004PNAS..101.6315D, lire en ligne)
(en) Steven J. Crafts-Brandner et Michael E. Salvucci, « Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2 », Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no 24, , p. 13430-13435 (PMID11069297, PMCID27241, DOI10.1073/pnas.230451497, Bibcode2000PNAS...9713430C, lire en ligne)
(en) Ning Zhang, Russell P. Kallis, Robert G. Ewy et Archie R. Portis Jr, « Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform », Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no 5, , p. 3330-3334 (PMID11854454, PMCID122518, DOI10.1073/pnas.042529999, Bibcode2002PNAS...99.3330Z, lire en ligne)
sciencedirect.com
(en) M. Yoon, J. J. Putterill, G. S. Ross, W. A. Laing, « Determination of the relative expression levels of rubisco small subunit genes in Arabidopsis by rapid amplification of cDNA ends », Anal. Biochem., vol. 291, no 2, , p. 237–244 (DOI10.1006/abio.2001.5042, lire en ligne)
(en) Hadi Farazdaghi, « The single-process biochemical reaction of Rubisco: A unified theory and model with the effects of irradiance, CO2 and rate-limiting step on the kinetics of C3 and C4 photosynthesis from gas exchange », Biosystems, vol. 103, no 2, , p. 265-284 (PMID21093535, DOI10.1016/j.biosystems.2010.11.004, lire en ligne)
(en) Shahnaz Khan, P. John Andralojc, Peter J. Lea et Martin A. J. Parry, « 2′-Carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown », European Journal of Biochemistry / FEBS, vol. 266, no 3, , p. 840-847 (PMID10583377, DOI10.1046/j.1432-1327.1999.00913.x, lire en ligne)
(en) Yehouda Marcus et Michael Gurevitz, « Activation of cyanobacterial RuBP-carboxylase/oxygenase is facilitated by inorganic phosphate via two independent mechanisms », European Journal of Biochemistry, vol. 267, no 19, , p. 5995-6003 (PMID10998060, DOI10.1046/j.1432-1327.2000.01674.x, lire en ligne)
zju.edu.cn
(en) JIN Song-heng, JIANG De-an, LI Xue-qin et SUN Jun-wei, « Characteristics of photosynthesis in rice plants transformed with an antisense Rubisco activase gene », Journal of Zhejiang University SCIENCE, vol. 5, no 8, , p. 897-899 (PMID15236471, DOI10.1631/jzus.2004.0897, lire en ligne)
