Ριβουλόζη-1,5-διφωσφορική καρβοξυλάση/οξυγενάση (Greek Wikipedia)

Analysis of information sources in references of the Wikipedia article "Ριβουλόζη-1,5-διφωσφορική καρβοξυλάση/οξυγενάση" in Greek language version.

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10nih.gov

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7doi.org

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5archive.org

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1ekt.gr

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1tovima.gr

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1harvard.edu

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archive.org

Nivison, Helen; Stocking, C. (1983). «Ribulose Bisphosphate Carboxylase Synthesis in Barley Leaves». Plant Physiology 73 (4): 906–911. doi:10.1104/pp.73.4.906. PMID 16663341. PMC 1066578. https://archive.org/details/sim_plant-physiology_1983-12_73_4/page/n43.
Mächler, Felix; Nösberger, Josef (1988). «Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase». Plant Physiology 88 (2): 462–465. doi:10.1104/pp.88.2.462. PMID 16666327. PMC 1055600. https://archive.org/details/sim_plant-physiology_1988-10_88_2/page/462.
«10.The Chloroplast Genome». The Cell: A Molecular Approach (2nd έκδοση). Washington, D.C: ASM Press. 2000. ISBN 978-0-87893-106-4. , one of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme that catalyzes the addition of CO₂ to ribulose-1,5-bisphosphate during the Calvin cycle. It is also thought to be the single most abundant protein on Earth, so it is noteworthy that one of its subunits is encoded by the chloroplast genome.
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615.
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615. Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.

doi.org

dx.doi.org

«Discovery of the canonical Calvin-Benson cycle». Photosynthesis Research 140 (2): 235–252. May 2019. doi:10.1007/s11120-018-0600-2. PMID 30374727.
Nivison, Helen; Stocking, C. (1983). «Ribulose Bisphosphate Carboxylase Synthesis in Barley Leaves». Plant Physiology 73 (4): 906–911. doi:10.1104/pp.73.4.906. PMID 16663341. PMC 1066578. https://archive.org/details/sim_plant-physiology_1983-12_73_4/page/n43.
Mächler, Felix; Nösberger, Josef (1988). «Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase». Plant Physiology 88 (2): 462–465. doi:10.1104/pp.88.2.462. PMID 16666327. PMC 1055600. https://archive.org/details/sim_plant-physiology_1988-10_88_2/page/462.
«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 101 (16): 6315–6320. April 2004. doi:10.1073/pnas.0400981101. PMID 15067115. Bibcode: 2004PNAS..101.6315D. «(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast;».
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615.
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615. Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.

doi.org

«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615. Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.

ekt.gr

thesis.ekt.gr

https://thesis.ekt.gr/thesisBookReader/id/1461#page/1/mode/2up ΡΟΥΜΠΙΣΚΟ

harvard.edu

adsabs.harvard.edu

«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 101 (16): 6315–6320. April 2004. doi:10.1073/pnas.0400981101. PMID 15067115. Bibcode: 2004PNAS..101.6315D. «(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast;».

nih.gov

ncbi.nlm.nih.gov

«Discovery of the canonical Calvin-Benson cycle». Photosynthesis Research 140 (2): 235–252. May 2019. doi:10.1007/s11120-018-0600-2. PMID 30374727.
Nivison, Helen; Stocking, C. (1983). «Ribulose Bisphosphate Carboxylase Synthesis in Barley Leaves». Plant Physiology 73 (4): 906–911. doi:10.1104/pp.73.4.906. PMID 16663341. PMC 1066578. https://archive.org/details/sim_plant-physiology_1983-12_73_4/page/n43.
Mächler, Felix; Nösberger, Josef (1988). «Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase». Plant Physiology 88 (2): 462–465. doi:10.1104/pp.88.2.462. PMID 16666327. PMC 1055600. https://archive.org/details/sim_plant-physiology_1988-10_88_2/page/462.
«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 101 (16): 6315–6320. April 2004. doi:10.1073/pnas.0400981101. PMID 15067115. Bibcode: 2004PNAS..101.6315D. «(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast;».
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615.
«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615. Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.

pubmedcentral.nih.gov

Nivison, Helen; Stocking, C. (1983). «Ribulose Bisphosphate Carboxylase Synthesis in Barley Leaves». Plant Physiology 73 (4): 906–911. doi:10.1104/pp.73.4.906. PMID 16663341. PMC 1066578. https://archive.org/details/sim_plant-physiology_1983-12_73_4/page/n43.
Mächler, Felix; Nösberger, Josef (1988). «Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase». Plant Physiology 88 (2): 462–465. doi:10.1104/pp.88.2.462. PMID 16666327. PMC 1055600. https://archive.org/details/sim_plant-physiology_1988-10_88_2/page/462.
«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 101 (16): 6315–6320. April 2004. doi:10.1073/pnas.0400981101. PMID 15067115. Bibcode: 2004PNAS..101.6315D. «(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast;».

pubmed.ncbi.nlm.nih.gov

«Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated». Journal of Experimental Botany 59 (7): 1615–1624. 2008. doi:10.1093/jxb/erm242. PMID 17975207. https://archive.org/details/sim_journal-of-experimental-botany_2008_59_7/page/1615. Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.

tovima.gr

Πρατικάκης, Βαγγέλης (18 Σεπτεμβρίου 2014). «Αύξηση της αγροτικής παραγωγής με επιτάχυνση της φωτοσύνθεσης;». ΤΟ ΒΗΜΑ. Ανακτήθηκε στις 18 Μαρτίου 2023.