Sign In

Login

Password

Forgot Password ? Sign Up

Rubisco (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "Rubisco" in French language version.

Last modified:

Ref.Un. Ref.Website
Global rank French rank
1916doi.org
2nd place
3rd place
1715nih.gov
5th place
11th place
43adsabs.harvard.edu
14th place
54th place
43pnas.org
1,411th place
525th place
22sciencedirect.com
137th place
99th place
22wiley.com
150th place
129th place
21oxfordjournals.org
1,550th place
649th place
21phys.org
1,595th place
2,523rd place
11jbc.org
6,339th place
2,667th place
11nature.com
207th place
147th place
11springer.com
182nd place
214th place
11zju.edu.cn
low place
low place
11biochemj.org
low place
9,960th place
11plantphysiol.org
low place
low place
11issn.org
33rd place
4th place
11annualreviews.org
2,959th place
1,791st place
11courrierinternational.com
2,667th place
184th place

adsabs.harvard.edu (Global: 14th place; French: 54th place)

ui.adsabs.harvard.edu

annualreviews.org (Global: 2,959th place; French: 1,791st place)

  • 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 (ISSN 1543-5008, DOI 10.1146/annurev.arplant.043008.091948, lire en ligne, consulté le )

biochemj.org (Global: low place; French: 9,960th place)

  • (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 (PMID 7818481, PMCID 1137402, lire en ligne)

courrierinternational.com (Global: 2,667th place; French: 184th place)

  • René Didde, « Nutrition. Vous reprendrez bien un peu de steak d’herbe ? », Courrier International,‎ (lire en ligne)

doi.org (Global: 2nd place; French: 3rd place)

dx.doi.org

  • (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 (PMID 16245127, DOI 10.1023/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 (PMID 15067115, PMCID 395966, DOI 10.1073/pnas.0400981101, Bibcode 2004PNAS..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 (PMID 17975207, DOI 10.1093/jxb/erm242, lire en ligne)
  • (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 (DOI 10.1006/abio.2001.5042, lire en ligne)
  • (en) R. John Ellis, « Biochemistry: Tackling unintelligent design », Nature, vol. 463, no 7278,‎ , p. 164-165 (PMID 20075906, DOI 10.1038/463164a, 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 (PMID 21093535, DOI 10.1016/j.biosystems.2010.11.004, lire en ligne)
  • (en) Archie R. Portis Jr., « Rubisco activase – Rubisco's catalytic chaperone », Photosynthesis Research, vol. 75, no 1,‎ , p. 11-27 (PMID 16245090, DOI 10.1023/A:1022458108678, 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 (PMID 15236471, DOI 10.1631/jzus.2004.0897, 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 (PMID 10583377, DOI 10.1046/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 (PMID 11069297, PMCID 27241, DOI 10.1073/pnas.230451497, Bibcode 2000PNAS...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 (PMID 11706186, PMCID 129275, DOI 10.1104/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 (PMID 11854454, PMCID 122518, DOI 10.1073/pnas.042529999, Bibcode 2002PNAS...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 (PMID 10998060, DOI 10.1046/j.1432-1327.2000.01674.x, lire en ligne)
  • (en) Robert E. Sharwood, « Reconstructing CO2 fixation from the past », Science, vol. 378, no 6616,‎ , p. 137-138 (DOI 10.1126/science.ade6522).
  • (en) Luca Schulz, Zhijun Guo, Jan Zarzycki, Wieland Steinchen, Jan M. Schuller et al., « Evolution of increased complexity and specificity at the dawn of form I Rubiscos », Science, vol. 378, no 6616,‎ , p. 155-160 (DOI 10.1126/science.abq1416).
  • 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 (ISSN 1543-5008, DOI 10.1146/annurev.arplant.043008.091948, lire en ligne, consulté le )

issn.org (Global: 33rd place; French: 4th place)

portal.issn.org

  • 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 (ISSN 1543-5008, DOI 10.1146/annurev.arplant.043008.091948, lire en ligne, consulté le )

jbc.org (Global: 6,339th place; French: 2,667th place)

  • (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 (PMID 1905726, lire en ligne)

nature.com (Global: 207th place; French: 147th place)

nih.gov (Global: 5th place; French: 11th place)

ncbi.nlm.nih.gov

  • (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 (PMID 16245127, DOI 10.1023/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 (PMID 15067115, PMCID 395966, DOI 10.1073/pnas.0400981101, Bibcode 2004PNAS..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 (PMID 17975207, DOI 10.1093/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 (PMID 1905726, lire en ligne)
  • (en) R. John Ellis, « Biochemistry: Tackling unintelligent design », Nature, vol. 463, no 7278,‎ , p. 164-165 (PMID 20075906, DOI 10.1038/463164a, 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 (PMID 21093535, DOI 10.1016/j.biosystems.2010.11.004, lire en ligne)
  • (en) Archie R. Portis Jr., « Rubisco activase – Rubisco's catalytic chaperone », Photosynthesis Research, vol. 75, no 1,‎ , p. 11-27 (PMID 16245090, DOI 10.1023/A:1022458108678, 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 (PMID 15236471, DOI 10.1631/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 (PMID 7818481, PMCID 1137402, 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 (PMID 10583377, DOI 10.1046/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 (PMID 11069297, PMCID 27241, DOI 10.1073/pnas.230451497, Bibcode 2000PNAS...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 (PMID 11706186, PMCID 129275, DOI 10.1104/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 (PMID 11854454, PMCID 122518, DOI 10.1073/pnas.042529999, Bibcode 2002PNAS...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 (PMID 10998060, DOI 10.1046/j.1432-1327.2000.01674.x, lire en ligne)

oxfordjournals.org (Global: 1,550th place; French: 649th place)

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 (PMID 17975207, DOI 10.1093/jxb/erm242, lire en ligne)

phys.org (Global: 1,595th place; French: 2,523rd place)

plantphysiol.org (Global: low place; French: low place)

  • (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 (PMID 11706186, PMCID 129275, DOI 10.1104/pp.010357, lire en ligne)

pnas.org (Global: 1,411th place; French: 525th place)

sciencedirect.com (Global: 137th place; French: 99th place)

  • (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 (DOI 10.1006/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 (PMID 21093535, DOI 10.1016/j.biosystems.2010.11.004, lire en ligne)

springer.com (Global: 182nd place; French: 214th place)

link.springer.com

wiley.com (Global: 150th place; French: 129th place)

onlinelibrary.wiley.com

  • (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 (PMID 10583377, DOI 10.1046/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 (PMID 10998060, DOI 10.1046/j.1432-1327.2000.01674.x, lire en ligne)

zju.edu.cn (Global: low place; French: low place)

  • (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 (PMID 15236471, DOI 10.1631/jzus.2004.0897, lire en ligne)