Ciclo di Krebs (Italian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Ciclo di Krebs" in Italian language version.

refsWebsite

Global rank Italian rank

23nih.gov

4^th place

9^th place

16doi.org

2^nd place

7^th place

9oadoi.org

799^th place

22^nd place

6archive.org

6^th place

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3web.archive.org

1^st place

2sciencemag.org

857^th place

540^th place

1google.it

215^th place

4^th place

1nobelprize.org

301^st place

270^th place

1treccani.it

182^nd place

6^th place

1atlasgeneticsoncology.org

low place

1jbc.org

4,455^th place

2,750^th place

1biology-direct.com

low place

1doai.io

low place

3,405^th place

archive.org

(EN) M. J. MacDonald, H. Al-Masri, M. Jumelle-Laclau e M. O. Cruz, Oscillations in activities of enzymes in pancreatic islet subcellular fractions induced by physiological concentrations of effectors, in Diabetes, vol. 46, n. 12, dicembre 1997, pp. 1996-2001, PMID 9392486.
(EN) H. Beinert e M. C. Kennedy, Aconitase, a two-faced protein: enzyme and iron regulatory factor, in The FASEB Journal, vol. 7, n. 15, dicembre 1993, pp. 1442-1449, PMID 8262329.
(EN) Michael Cox, David R. Nelson e Albert L. Lehninger, Lehninger Principles of Biochemistry, San Francisco, W.H. Freeman, 2005, pp. 609-611, ISBN 0-7167-4339-6.
(EN) B. H. Robinson, Cell culture studies on patients with mitochondrial diseases: molecular defects in pyruvate dehydrogenase, in Journal of Bioenergetics and Biomembranes, vol. 20, n. 3, giugno 1988, pp. 313-323, PMID 3136149.
(EN) J. P. Bonnefont, D. Chretien, P. Rustin e et al., Alpha-ketoglutarate dehydrogenase deficiency presenting as congenital lactic acidosis, in The Journal of Pediatrics, vol. 121, n. 2, agosto 1992, pp. 255-258, DOI:10.1016/S0022-3476(05)81199-0, PMID 1640293.
(EN) N. Guffon, C. Lopez-Mediavilla, R. Dumoulin e et al., 2-Ketoglutarate dehydrogenase deficiency, a rare cause of primary hyperlactataemia: report of a new case, in Journal of Inherited Metabolic Disease, vol. 16, n. 5, 1993, pp. 821-830, PMID 8295396.

atlasgeneticsoncology.org

(EN) Allison M. Lynch AM e Cynthia C. Morton, FH (fumarate hydratase), in Atlas of Genetics and Cytogenetics in Oncology and Haematology, vol. 10, n. 4, luglio 2006, pp. 247-250.

biology-direct.com

(EN) F. A. Kondrashov, E. V. Koonin, I. G. Morgunov, T. V. Finogenova e M. N. Kondrashova, Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation ^{[collegamento interrotto]}, in Biology Direct, vol. 1, n. 31, 2006, DOI:10.1186/1745-6150-1-31, PMC 1630690, PMID 17059607.

doai.io

(EN) R. E. Hall, K. G. Henriksson, S. F. Lewis, R. G. Haller e N. G. Kennaway, Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins, in Journal of Clinical Investigation, vol. 92, n. 6, dicembre 1993, pp. 2660-2666, DOI:10.1172/JCI116882, PMC 288463, PMID 8254022.

doi.org

dx.doi.org

(EN) Marion Stubbs e Geoff Gibbons, Hans Adolf Krebs (1900-1981)...His Life and Times, in IUBMB Life, vol. 50, n. 3, 2000, pp. 163-166, DOI:10.1080/152165400300001462.
(EN) E. D. Merkley, T. O. Metz, R. D. Smith, J. W. Baynes e N. Frizzell, The succinated proteome, in Mass Spectrometry Reviews, vol. 33, n. 2, 2014, pp. 98-109, DOI:10.1002/mas.21382, PMC 4038156, PMID 24115015.
(EN) G. Wiegand e S. J. Remington, Citrate synthase: structure, control, and mechanism, in Annual Review of Biophysics and Biophysical Chemistry, vol. 15, 1986, pp. 97-117, DOI:10.1146/annurev.bb.15.060186.000525, PMID 3013232.
(EN) Hanspeter Lauble e Charles David Stout, Steric and conformational features of the aconitase mechanism, in Proteins, vol. 22, n. 1, maggio 1995, pp. 1-11, DOI:10.1002/prot.340220102, PMID 7675781.
(EN) A. H. Robbins e C. D. Stout, The structure of aconitase, in Proteins, vol. 5, n. 4, 1989, pp. 289-312, DOI:10.1002/prot.340050406, PMID 2798408.
(EN) Y. Yasutake, S. Watanabe, M. Yao, Y. Takada, N. Fukunaga e I. Tanaka, Crystal Structure of the Monomeric Isocitrate Dehydrogenase in the Presence of NADP⁺, in Journal of Biological Chemistry, vol. 278, n. 38, 2003, pp. 36897-36904, DOI:10.1074/jbc.M304091200, PMID 12855708.
(EN) J. E. Knapp, D. Carroll, J. E. Lawson, S. R. Ernst, L. J. Reed e M. L. Hackert, Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase, in Protein Science, vol. 9, n. 1, gennaio 2000, pp. 37-48, DOI:10.1110/ps.9.1.37, PMC 2144448, PMID 10739245.
(EN) Marie E. Fraser, Michael N. G. James, William A. Bridger e William T. Wolodko, Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase, in Journal of Molecular Biology, vol. 299, n. 5, 23 giugno 2000, pp. 1325-1339, DOI:10.1006/jmbi.2000.3807, PMID 10873456.
(EN) V. Yankovskaya, R. Horsefield, S. Törnroth e et al., Architecture of succinate dehydrogenase and reactive oxygen species generation, in Science, vol. 299, n. 5607, 31 gennaio 2003, pp. 700-704, DOI:10.1126/science.1079605, PMID 12560550.
(EN) K. S. Oyedotun e B. D. Lemire, The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies, in Journal of Biological Chemistry, vol. 279, n. 10, 5 marzo 2004, pp. 9424-9431, DOI:10.1074/jbc.M311876200, PMID 14672929.
(EN) T. Weaver, M. Lees, V. Zaitsev e et al., Crystal structures of native and recombinant yeast fumarase, in Journal of Molecular Biology, vol. 280, n. 3, 17 luglio 1998, pp. 431-442, DOI:10.1006/jmbi.1998.1862, PMID 9665847.
(EN) M. Estévez, J. Skarda, J. Spencer, L. Banaszak e T. M. Weaver, X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation, in Protein Science, vol. 11, n. 6, giugno 2002, pp. 1552-1557, DOI:10.1110/ps.0201502, PMC 2373640, PMID 12021453.
(EN) F. A. Kondrashov, E. V. Koonin, I. G. Morgunov, T. V. Finogenova e M. N. Kondrashova, Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation ^{[collegamento interrotto]}, in Biology Direct, vol. 1, n. 31, 2006, DOI:10.1186/1745-6150-1-31, PMC 1630690, PMID 17059607.
(EN) P. Rustin, T. Bourgeron, B. Parfait, D. Chretien, A. Munnich e A. Rötig, Inborn errors of the Krebs cycle: a group of unusual mitochondrial diseases in human, in Biochimica et Biophysica Acta, vol. 1361, n. 2, 22 agosto 1997, pp. 185-197, DOI:10.1016/S0925-4439(97)00035-5, PMID 9300800.
(EN) R. E. Hall, K. G. Henriksson, S. F. Lewis, R. G. Haller e N. G. Kennaway, Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins, in Journal of Clinical Investigation, vol. 92, n. 6, dicembre 1993, pp. 2660-2666, DOI:10.1172/JCI116882, PMC 288463, PMID 8254022.
(EN) J. P. Bonnefont, D. Chretien, P. Rustin e et al., Alpha-ketoglutarate dehydrogenase deficiency presenting as congenital lactic acidosis, in The Journal of Pediatrics, vol. 121, n. 2, agosto 1992, pp. 255-258, DOI:10.1016/S0022-3476(05)81199-0, PMID 1640293.

google.it

books.google.it

Augusto Innocenti, Principi di Nutrizione Umana, Società Editrice Esculapio, 2013, p. 177, ISBN 978-88-7488-595-4.

jbc.org

(EN) M. Nishiyama, J. J. Birktoft e T. Beppu, Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis ^{[collegamento interrotto]}, in Journal of Biological Chemistry, vol. 268, n. 7, marzo 1993, pp. 4656-4660, PMID 8444839.

nih.gov

ncbi.nlm.nih.gov

(EN) E. D. Merkley, T. O. Metz, R. D. Smith, J. W. Baynes e N. Frizzell, The succinated proteome, in Mass Spectrometry Reviews, vol. 33, n. 2, 2014, pp. 98-109, DOI:10.1002/mas.21382, PMC 4038156, PMID 24115015.
(EN) K. C. Usher, S. J. Remington, D. P. Martin e D. G. Drueckhammer, A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase, in Biochemistry, vol. 33, n. 25, 28 giugno 1994, pp. 7753-7759, PMID 8011640.
(EN) G. Wiegand e S. J. Remington, Citrate synthase: structure, control, and mechanism, in Annual Review of Biophysics and Biophysical Chemistry, vol. 15, 1986, pp. 97-117, DOI:10.1146/annurev.bb.15.060186.000525, PMID 3013232.
(EN) M. J. MacDonald, H. Al-Masri, M. Jumelle-Laclau e M. O. Cruz, Oscillations in activities of enzymes in pancreatic islet subcellular fractions induced by physiological concentrations of effectors, in Diabetes, vol. 46, n. 12, dicembre 1997, pp. 1996-2001, PMID 9392486.
(EN) Hanspeter Lauble e Charles David Stout, Steric and conformational features of the aconitase mechanism, in Proteins, vol. 22, n. 1, maggio 1995, pp. 1-11, DOI:10.1002/prot.340220102, PMID 7675781.
(EN) A. H. Robbins e C. D. Stout, The structure of aconitase, in Proteins, vol. 5, n. 4, 1989, pp. 289-312, DOI:10.1002/prot.340050406, PMID 2798408.
(EN) H. Beinert e M. C. Kennedy, Aconitase, a two-faced protein: enzyme and iron regulatory factor, in The FASEB Journal, vol. 7, n. 15, dicembre 1993, pp. 1442-1449, PMID 8262329.
(EN) Andrew D. Mesecar, Barry L. Stoddard e Daniel E. Koshland Jr., Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences, in Science, vol. 277, n. 5323, 11 luglio 1997, pp. 202–206, PMID 9211842.
(EN) Y. Yasutake, S. Watanabe, M. Yao, Y. Takada, N. Fukunaga e I. Tanaka, Crystal Structure of the Monomeric Isocitrate Dehydrogenase in the Presence of NADP⁺, in Journal of Biological Chemistry, vol. 278, n. 38, 2003, pp. 36897-36904, DOI:10.1074/jbc.M304091200, PMID 12855708.
(EN) J. E. Knapp, D. Carroll, J. E. Lawson, S. R. Ernst, L. J. Reed e M. L. Hackert, Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase, in Protein Science, vol. 9, n. 1, gennaio 2000, pp. 37-48, DOI:10.1110/ps.9.1.37, PMC 2144448, PMID 10739245.
(EN) Marie E. Fraser, Michael N. G. James, William A. Bridger e William T. Wolodko, Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase, in Journal of Molecular Biology, vol. 299, n. 5, 23 giugno 2000, pp. 1325-1339, DOI:10.1006/jmbi.2000.3807, PMID 10873456.
(EN) V. Yankovskaya, R. Horsefield, S. Törnroth e et al., Architecture of succinate dehydrogenase and reactive oxygen species generation, in Science, vol. 299, n. 5607, 31 gennaio 2003, pp. 700-704, DOI:10.1126/science.1079605, PMID 12560550.
(EN) K. S. Oyedotun e B. D. Lemire, The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies, in Journal of Biological Chemistry, vol. 279, n. 10, 5 marzo 2004, pp. 9424-9431, DOI:10.1074/jbc.M311876200, PMID 14672929.
(EN) T. Weaver, M. Lees, V. Zaitsev e et al., Crystal structures of native and recombinant yeast fumarase, in Journal of Molecular Biology, vol. 280, n. 3, 17 luglio 1998, pp. 431-442, DOI:10.1006/jmbi.1998.1862, PMID 9665847.
(EN) M. Estévez, J. Skarda, J. Spencer, L. Banaszak e T. M. Weaver, X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation, in Protein Science, vol. 11, n. 6, giugno 2002, pp. 1552-1557, DOI:10.1110/ps.0201502, PMC 2373640, PMID 12021453.
(EN) M. Nishiyama, J. J. Birktoft e T. Beppu, Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis ^{[collegamento interrotto]}, in Journal of Biological Chemistry, vol. 268, n. 7, marzo 1993, pp. 4656-4660, PMID 8444839.
(EN) J. M. Berg, J. L. Tymoczko e L. Stryer, Section 17.2 Entry to the Citric Acid Cycle and Metabolism Through It Are Controlled, in Biochemistry, 5ª ed., New York, W. H. Freeman, 2002, ISBN 0-7167-3051-0.
(EN) F. A. Kondrashov, E. V. Koonin, I. G. Morgunov, T. V. Finogenova e M. N. Kondrashova, Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation ^{[collegamento interrotto]}, in Biology Direct, vol. 1, n. 31, 2006, DOI:10.1186/1745-6150-1-31, PMC 1630690, PMID 17059607.
(EN) P. Rustin, T. Bourgeron, B. Parfait, D. Chretien, A. Munnich e A. Rötig, Inborn errors of the Krebs cycle: a group of unusual mitochondrial diseases in human, in Biochimica et Biophysica Acta, vol. 1361, n. 2, 22 agosto 1997, pp. 185-197, DOI:10.1016/S0925-4439(97)00035-5, PMID 9300800.
(EN) B. H. Robinson, Cell culture studies on patients with mitochondrial diseases: molecular defects in pyruvate dehydrogenase, in Journal of Bioenergetics and Biomembranes, vol. 20, n. 3, giugno 1988, pp. 313-323, PMID 3136149.
(EN) R. E. Hall, K. G. Henriksson, S. F. Lewis, R. G. Haller e N. G. Kennaway, Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins, in Journal of Clinical Investigation, vol. 92, n. 6, dicembre 1993, pp. 2660-2666, DOI:10.1172/JCI116882, PMC 288463, PMID 8254022.
(EN) J. P. Bonnefont, D. Chretien, P. Rustin e et al., Alpha-ketoglutarate dehydrogenase deficiency presenting as congenital lactic acidosis, in The Journal of Pediatrics, vol. 121, n. 2, agosto 1992, pp. 255-258, DOI:10.1016/S0022-3476(05)81199-0, PMID 1640293.
(EN) N. Guffon, C. Lopez-Mediavilla, R. Dumoulin e et al., 2-Ketoglutarate dehydrogenase deficiency, a rare cause of primary hyperlactataemia: report of a new case, in Journal of Inherited Metabolic Disease, vol. 16, n. 5, 1993, pp. 821-830, PMID 8295396.

nobelprize.org

(EN) The Nobel Prize in Physiology or Medicine 1937, su nobelprize.org, The Nobel Foundation. URL consultato il 26 ottobre 2011.

oadoi.org

(EN) Marion Stubbs e Geoff Gibbons, Hans Adolf Krebs (1900-1981)...His Life and Times, in IUBMB Life, vol. 50, n. 3, 2000, pp. 163-166, DOI:10.1080/152165400300001462.
(EN) G. Wiegand e S. J. Remington, Citrate synthase: structure, control, and mechanism, in Annual Review of Biophysics and Biophysical Chemistry, vol. 15, 1986, pp. 97-117, DOI:10.1146/annurev.bb.15.060186.000525, PMID 3013232.
(EN) Hanspeter Lauble e Charles David Stout, Steric and conformational features of the aconitase mechanism, in Proteins, vol. 22, n. 1, maggio 1995, pp. 1-11, DOI:10.1002/prot.340220102, PMID 7675781.
(EN) A. H. Robbins e C. D. Stout, The structure of aconitase, in Proteins, vol. 5, n. 4, 1989, pp. 289-312, DOI:10.1002/prot.340050406, PMID 2798408.
(EN) Y. Yasutake, S. Watanabe, M. Yao, Y. Takada, N. Fukunaga e I. Tanaka, Crystal Structure of the Monomeric Isocitrate Dehydrogenase in the Presence of NADP⁺, in Journal of Biological Chemistry, vol. 278, n. 38, 2003, pp. 36897-36904, DOI:10.1074/jbc.M304091200, PMID 12855708.
(EN) Marie E. Fraser, Michael N. G. James, William A. Bridger e William T. Wolodko, Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase, in Journal of Molecular Biology, vol. 299, n. 5, 23 giugno 2000, pp. 1325-1339, DOI:10.1006/jmbi.2000.3807, PMID 10873456.
(EN) K. S. Oyedotun e B. D. Lemire, The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies, in Journal of Biological Chemistry, vol. 279, n. 10, 5 marzo 2004, pp. 9424-9431, DOI:10.1074/jbc.M311876200, PMID 14672929.
(EN) T. Weaver, M. Lees, V. Zaitsev e et al., Crystal structures of native and recombinant yeast fumarase, in Journal of Molecular Biology, vol. 280, n. 3, 17 luglio 1998, pp. 431-442, DOI:10.1006/jmbi.1998.1862, PMID 9665847.
(EN) P. Rustin, T. Bourgeron, B. Parfait, D. Chretien, A. Munnich e A. Rötig, Inborn errors of the Krebs cycle: a group of unusual mitochondrial diseases in human, in Biochimica et Biophysica Acta, vol. 1361, n. 2, 22 agosto 1997, pp. 185-197, DOI:10.1016/S0925-4439(97)00035-5, PMID 9300800.

sciencemag.org

(EN) Andrew D. Mesecar, Barry L. Stoddard e Daniel E. Koshland Jr., Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences, in Science, vol. 277, n. 5323, 11 luglio 1997, pp. 202–206, PMID 9211842.
(EN) V. Yankovskaya, R. Horsefield, S. Törnroth e et al., Architecture of succinate dehydrogenase and reactive oxygen species generation, in Science, vol. 299, n. 5607, 31 gennaio 2003, pp. 700-704, DOI:10.1126/science.1079605, PMID 12560550.

treccani.it

Anna Atlante, Ciclo di Krebs, su treccani.it, Enciclopedia Treccani. URL consultato il 26 ottobre 2014.

web.archive.org

(EN) Takusagawa F., Chapter 16: Citric Acid Cycle (PDF), su crystal.res.ku.edu, Department of Molecular Biosciences - University of Kansas. URL consultato il 31 gennaio 2015 (archiviato dall'url originale il 12 aprile 2015).
(EN) University of London, IUBMB Enzyme Nomenclature - EC 4.2.1.3, su chem.qmul.ac.uk. URL consultato il 31 gennaio 2015 (archiviato dall'url originale il 14 luglio 2007).
(EN) Interconnessioni del ciclo di Krebs con altri pathways cellulari, su genome.jp, KEGG PATHWAY Database. URL consultato il 10 ottobre 2014 (archiviato dall'url originale il 20 ottobre 2014).