Συμπαράγοντας (βιοχημεία) (Greek Wikipedia)

Analysis of information sources in references of the Wikipedia article "Συμπαράγοντας (βιοχημεία)" in Greek language version.

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archive.org

Nelson, David L.· Cox, Michael M. (2008). Lehninger Principles of Biochemistry (Fifth έκδοση). New York: W.H. Freeman and Company. σελ. 184. ISBN 978-1429224161. Unknown parameter |name-list-style= ignored (βοήθεια)
Sauke, David J.· Metzler, David E.· Metzler, Carol M. (2001). Biochemistry: the chemical reactions of living cells (2nd έκδοση). San Diego: Harcourt/Academic Press. ISBN 978-0-12-492540-3. Unknown parameter |name-list-style= ignored (βοήθεια)
Jordan, Frank· Patel, Mulchand S. (2004). Thiamine: catalytic mechanisms in normal and disease states. New York, N.Y: Marcel Dekker. σελ. 588. ISBN 978-0-8247-4062-7. Unknown parameter |name-list-style= ignored (βοήθεια)
«The biochemistry of chromium». The Journal of Nutrition 130 (4): 715–8. April 2000. doi:10.1093/jn/130.4.715. PMID 10736319. https://archive.org/details/sim_journal-of-nutrition_2000-04_130_4/page/715.
Palmer, Trevor (1981). Understanding enzymes. New York: Horwood. ISBN 978-0-85312-307-1. Unknown parameter |name-list-style= ignored (βοήθεια)
Cox, Michael· Lehninger, Albert L· Nelson, David R. (2000). Lehninger principles of biochemistry (3rd έκδοση). New York: Worth Publishers. ISBN 978-1-57259-153-0. Unknown parameter |name-list-style= ignored (βοήθεια)
Bugg, Tim (1997). An introduction to enzyme and coenzyme chemistry. Oxford: Blackwell Science. σελίδες 95. ISBN 978-0-86542-793-8. Unknown parameter |name-list-style= ignored (βοήθεια)
«S-Adenosylmethionine and methylation». FASEB Journal 10 (4): 471–80. March 1996. doi:10.1096/fasebj.10.4.8647346. PMID 8647346. https://archive.org/details/sim_faseb-journal_1996-03_10_4/page/471.
«Structure and methylation of coenzyme M(HSCH2CH2SO3)». The Journal of Biological Chemistry 249 (15): 4879–85. August 1974. doi:10.1016/S0021-9258(19)42403-4. PMID 4367810. https://archive.org/details/sim_journal-of-biological-chemistry_1974-08-10_249_15/page/n218.
«Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid)». Journal of Bacteriology 137 (1): 256–63. January 1979. doi:10.1128/JB.137.1.256-263.1979. PMID 104960. PMC 218444. https://archive.org/details/sim_journal-of-bacteriology_1979-01_137_1/page/256.
Buchanan, Bob B.· Gruissem, Wilhelm· Jones, Russell L. (2000). Biochemistry & molecular biology of plants (1st έκδοση). American society of plant physiology. ISBN 978-0-943088-39-6. Unknown parameter |name-list-style= ignored (βοήθεια)
«Glutathione». Annual Review of Biochemistry 52: 711–60. 1983. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189. https://archive.org/details/sim_annual-review-of-biochemistry_1983_52_annual/page/711.
«Molybdoenzymes and molybdenum cofactor in plants». Journal of Experimental Botany 53 (375): 1689–98. August 2002. doi:10.1093/jxb/erf038. PMID 12147719. https://archive.org/details/sim_journal-of-experimental-botany_2002-08_53_375/page/1689.
«Unusual coenzymes of methanogenesis». Annual Review of Biochemistry 59: 355–94. 1990. doi:10.1146/annurev.bi.59.070190.002035. PMID 2115763. https://archive.org/details/sim_annual-review-of-biochemistry_1990_59/page/355.
«Mechanisms of enzyme-catalyzed group transfer reactions». Annual Review of Biochemistry 47: 1031–78. 1978. doi:10.1146/annurev.bi.47.070178.005123. PMID 354490. https://archive.org/details/sim_annual-review-of-biochemistry_1978_47/page/1031.
Lipmann F (1 September 1945). «Acetylation of sulfanilamide by liver homogenates and extracts». J. Biol. Chem. 160 (1): 173–90. doi:10.1016/S0021-9258(18)43110-9. https://archive.org/details/sim_journal-of-biological-chemistry_1945-09_160_1/page/173.

books.google.com

Grill D, Tausz T, De Kok LJ (2001). Significance of glutathione in plant adaptation to the environment. Springer. ISBN 978-1-4020-0178-9.

cuny.edu

academic.brooklyn.cuny.edu

«coenzymes and cofactors». Αρχειοθετήθηκε από το πρωτότυπο στις 26 Αυγούστου 1999. Ανακτήθηκε στις 17 Νοεμβρίου 2007.

doi.org

dx.doi.org

Hasim, Onn H.; Adnan, Nor Azila (2010). «Coenzyme, Cofactor and Prosthetic Group — Ambiguous Biochemical Jargon». Biochemical Education 22 (2): 93–94. doi:10.1016/0307-4412(94)90088-4. http://eprints.um.edu.my/3450/1/Coenzyme%2C_cofactor_and_prosthetic_group%C3%A2%E2%82%AC%E2%80%9Dambiguous_biochemical_jargon.pdf.
«Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins». Proteins 44 (3): 282–91. August 2001. doi:10.1002/prot.1093. PMID 11455601.
Bryce (March 1979). «SAM – semantics and misunderstandings». Trends Biochem. Sci. 4 (3): N62–N63. doi:10.1016/0968-0004(79)90255-X.
«Physiology and metabolism of essential trace elements: an outline». Clinics in Endocrinology and Metabolism 14 (3): 513–43. August 1985. doi:10.1016/S0300-595X(85)80005-0. PMID 3905079.
«Is chromium a trace essential metal?». BioFactors 11 (3): 149–62. 2000. doi:10.1002/biof.5520110301. PMID 10875302.
«The biochemistry of chromium». The Journal of Nutrition 130 (4): 715–8. April 2000. doi:10.1093/jn/130.4.715. PMID 10736319. https://archive.org/details/sim_journal-of-nutrition_2000-04_130_4/page/715.
«Iodine metabolism and thyroid physiology: current concepts». Thyroid 7 (2): 177–81. April 1997. doi:10.1089/thy.1997.7.177. PMID 9133680.
«Calcium signaling». Cell 131 (6): 1047–58. 2007. doi:10.1016/j.cell.2007.11.028. PMID 18083096.
«Ca2+ signaling and intracellular Ca2+ binding proteins». Journal of Biochemistry 120 (4): 685–98. October 1996. doi:10.1093/oxfordjournals.jbchem.a021466. PMID 8947828.
«Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase». Science 267 (5203): 1463–9. March 1995. doi:10.1126/science.7878465. PMID 7878465. Bibcode: 1995Sci...267.1463C.
«A biological function for cadmium in marine diatoms». Proceedings of the National Academy of Sciences of the United States of America 97 (9): 4627–31. April 2000. doi:10.1073/pnas.090091397. PMID 10781068. Bibcode: 2000PNAS...97.4627L.
«Biochemistry: a cadmium enzyme from a marine diatom». Nature 435 (7038): 42. 2005. doi:10.1038/435042a. PMID 15875011. Bibcode: 2005Natur.435...42L.
«Structural analysis of heme proteins: implications for design and prediction». BMC Structural Biology 11: 13. March 2011. doi:10.1186/1472-6807-11-13. PMID 21371326.
«Iron-sulfur protein folds, iron-sulfur chemistry, and evolution». J. Biol. Inorg. Chem. 13 (2): 157–70. February 2008. doi:10.1007/s00775-007-0318-7. PMID 17992543.
«Studies on the nature of the binding of thiamine pyrophosphate to enzymes». The Journal of Biological Chemistry 243 (11): 3009–19. June 1968. doi:10.1016/S0021-9258(18)93372-7. PMID 4968184. http://www.jbc.org/content/243/11/3009.
«Conservation of the Enzyme–Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme». Journal of Molecular Evolution 85 (5–6): 205–218. December 2017. doi:10.1007/s00239-017-9821-9. PMID 29177972. Bibcode: 2017JMolE..85..205H.
«Novel biochemistry of methanogenesis». The Journal of Biological Chemistry 263 (17): 7913–6. June 1988. doi:10.1016/S0021-9258(18)68417-0. PMID 3131330.
«Structure, mechanism and catalytic duality of thiamine-dependent enzymes». Cell. Mol. Life Sci. 64 (7–8): 892–905. 2007. doi:10.1007/s00018-007-6423-5. PMID 17429582.
«The power to reduce: pyridine nucleotides—small molecules with a multitude of functions». Biochem. J. 402 (2): 205–18. 2007. doi:10.1042/BJ20061638. PMID 17295611.
«Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations». Annu. Rev. Biochem. 73: 383–415. 2004. doi:10.1146/annurev.biochem.73.011303.074021. PMID 15189147.
«The many faces of vitamin B₁₂: catalysis by cobalamin-dependent enzymes». Annu. Rev. Biochem. 72: 209–47. 2003. doi:10.1146/annurev.biochem.72.121801.161828. PMID 14527323. https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1458&context=biochemfacpub.
«The biotin enzyme family: conserved structural motifs and domain rearrangements». Curr. Protein Pept. Sci. 4 (3): 217–29. 2003. doi:10.2174/1389203033487199. PMID 12769720.
«Coenzyme A: back in action». Prog. Lipid Res. 44 (2–3): 125–53. 2005. doi:10.1016/j.plipres.2005.04.001. PMID 15893380.
«Folic acid». Critical Reviews in Clinical Laboratory Sciences 38 (3): 183–223. June 2001. doi:10.1080/20014091084209. PMID 11451208.
«Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management». Microbiology 145 (8): 1817–30. August 1999. doi:10.1099/13500872-145-8-1817. PMID 10463148. Αρχειοθετήθηκε από το πρωτότυπο στις 2008-05-29. https://web.archive.org/web/20080529070520/http://mic.sgmjournals.org/cgi/reprint/145/8/1817.pdf. Ανακτήθηκε στις 2024-04-11.
«Vitamin C. Biosynthesis, recycling and degradation in mammals». FEBS J. 274 (1): 1–22. 2007. doi:10.1111/j.1742-4658.2006.05607.x. PMID 17222174.
«Flavoenzymes». Curr Opin Chem Biol 11 (2): 195–202. 2007. doi:10.1016/j.cbpa.2007.01.010. PMID 17275397.
«Riboflavin analogs and inhibitors of riboflavin biosynthesis». Appl. Microbiol. Biotechnol. 71 (3): 265–75. 2006. doi:10.1007/s00253-006-0421-7. PMID 16607521.
«S-Adenosylmethionine and methylation». FASEB Journal 10 (4): 471–80. March 1996. doi:10.1096/fasebj.10.4.8647346. PMID 8647346. https://archive.org/details/sim_faseb-journal_1996-03_10_4/page/471.
«Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum». Proceedings of the National Academy of Sciences of the United States of America 83 (12): 4238–42. June 1986. doi:10.1073/pnas.83.12.4238. PMID 3086878. Bibcode: 1986PNAS...83.4238N.
«Structure and methylation of coenzyme M(HSCH2CH2SO3)». The Journal of Biological Chemistry 249 (15): 4879–85. August 1974. doi:10.1016/S0021-9258(19)42403-4. PMID 4367810. https://archive.org/details/sim_journal-of-biological-chemistry_1974-08-10_249_15/page/n218.
«Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid)». Journal of Bacteriology 137 (1): 256–63. January 1979. doi:10.1128/JB.137.1.256-263.1979. PMID 104960. PMC 218444. https://archive.org/details/sim_journal-of-bacteriology_1979-01_137_1/page/256.
«Biochemical functions of coenzyme Q10». Journal of the American College of Nutrition 20 (6): 591–8. December 2001. doi:10.1080/07315724.2001.10719063. PMID 11771674. http://www.jacn.org/cgi/content/full/20/6/591.
«Glutathione». Annual Review of Biochemistry 52: 711–60. 1983. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189. https://archive.org/details/sim_annual-review-of-biochemistry_1983_52_annual/page/711.
«Biology of heme in health and disease». Curr. Med. Chem. 11 (8): 981–6. 2004. doi:10.2174/0929867043455521. PMID 15078160.
«The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea». European Journal of Biochemistry 248 (3): 919–24. September 1997. doi:10.1111/j.1432-1033.1997.00919.x. PMID 9342247.
«Molybdoenzymes and molybdenum cofactor in plants». Journal of Experimental Botany 53 (375): 1689–98. August 2002. doi:10.1093/jxb/erf038. PMID 12147719. https://archive.org/details/sim_journal-of-experimental-botany_2002-08_53_375/page/1689.
«Cell biology of molybdenum». Biochim. Biophys. Acta 1763 (7): 621–35. 2006. doi:10.1016/j.bbamcr.2006.03.013. PMID 16784786.
«Structure and function of sulfotransferases». Archives of Biochemistry and Biophysics 390 (2): 149–57. June 2001. doi:10.1006/abbi.2001.2368. PMID 11396917. https://zenodo.org/record/1229406.
«A novel coenzyme from bacterial primary alcohol dehydrogenases». Nature 280 (5725): 843–4. August 1979. doi:10.1038/280843a0. PMID 471057. Bibcode: 1979Natur.280..843S.
«Tetrahydrobiopterin biosynthesis, regeneration and functions». The Biochemical Journal 347 (1): 1–16. April 2000. doi:10.1042/0264-6021:3470001. PMID 10727395.
«Unusual coenzymes of methanogenesis». Annual Review of Biochemistry 59: 355–94. 1990. doi:10.1146/annurev.bi.59.070190.002035. PMID 2115763. https://archive.org/details/sim_annual-review-of-biochemistry_1990_59/page/355.
«The Ninth Sir Hans Krebs Lecture. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems». European Journal of Biochemistry 95 (1): 1–20. March 1979. doi:10.1111/j.1432-1033.1979.tb12934.x. PMID 378655.
«Mechanisms of enzyme-catalyzed group transfer reactions». Annual Review of Biochemistry 47: 1031–78. 1978. doi:10.1146/annurev.bi.47.070178.005123. PMID 354490. https://archive.org/details/sim_annual-review-of-biochemistry_1978_47/page/1031.
«Ribozyme catalysis of metabolism in the RNA world». Chemistry & Biodiversity 4 (4): 633–55. 2007. doi:10.1002/cbdv.200790055. PMID 17443876.
«The emergence of major cellular processes in evolution». FEBS Letters 390 (2): 119–23. July 1996. doi:10.1016/0014-5793(96)00631-X. PMID 8706840.
«Coenzymes as fossils of an earlier metabolic state». Journal of Molecular Evolution 7 (2): 101–4. March 1976. doi:10.1007/BF01732468. PMID 1263263. Bibcode: 1976JMolE...7..101W.
«The tyranny of adenosine recognition among RNA aptamers to coenzyme A». BMC Evol. Biol. 3: 26. 2003. doi:10.1186/1471-2148-3-26. PMID 14687414.
«Coenzymes as coribozymes». Biochimie 84 (9): 877–88. 2002. doi:10.1016/S0300-9084(02)01404-9. PMID 12458080.
«Computational design of Candida boidinii xylose reductase for altered cofactor specificity». Protein Science 18 (10): 2125–38. October 2009. doi:10.1002/pro.227. PMID 19693930.
«The Alcoholic Ferment of Yeast-Juice». Proceedings of the Royal Society B: Biological Sciences 78 (526): 369–75. 24 October 1906. doi:10.1098/rspb.1906.0070.
Lohmann K (August 1929). «Über die Pyrophosphatfraktion im Muskel». Naturwissenschaften 17 (31): 624–5. doi:10.1007/BF01506215. Bibcode: 1929NW.....17..624..
Lipmann F (1 September 1945). «Acetylation of sulfanilamide by liver homogenates and extracts». J. Biol. Chem. 160 (1): 173–90. doi:10.1016/S0021-9258(18)43110-9. https://archive.org/details/sim_journal-of-biological-chemistry_1945-09_160_1/page/173.
«Pyridin, the hydrogen-transferring component of the fermentation enzymes (pyridine nucleotide)». Biochemische Zeitschrift 287: E79–E88. 1936. doi:10.1002/hlca.193601901199.
«Origins of the concept oxidative phosphorylation». Molecular and Cellular Biochemistry 5 (1–2): 55–63. November 1974. doi:10.1007/BF01874172. PMID 4279328.
«Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen». J. Biol. Chem. 178 (2): 611–23. 1949. doi:10.1016/S0021-9258(18)56879-4. PMID 18116985. http://www.jbc.org/cgi/reprint/178/2/611.
«Protein-Derived Cofactors. Expanding the Scope of Post-Translational Modifications†». Biochemistry 46 (18): 5283–5292. 2007. doi:10.1021/bi700468t. PMID 17439161.
«Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone». Annual Review of Biochemistry 82: 531–50. 2013. doi:10.1146/annurev-biochem-051110-133601. PMID 23746262.
«A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway». Proceedings of the National Academy of Sciences of the United States of America 110 (20): 8069–74. May 2013. doi:10.1073/pnas.1304733110. PMID 23633564. Bibcode: 2013PNAS..110.8069H.
«Coactivators and corepressors: what's in a name?». Molecular Endocrinology 22 (10): 2213–4. October 2008. doi:10.1210/me.2008-0201. PMID 18701638.

doi.org

Koch AL (1998). How did bacteria come to be?. Advances in Microbial Physiology. 40. σελίδες 353–99. doi:10.1016/S0065-2911(08)60135-6. ISBN 9780120277407. PMID 9889982.
Lipmann F (1941). «Metabolic generation and utilization of phosphate bond energy». A Source Book in Chemistry, 1900-1950. Adv Enzymol. 1. σελίδες 99–162. doi:10.4159/harvard.9780674366701.c141. ISBN 9780674366701.

du.ac.in

vle.du.ac.in

«Biochemistry: Enzymes: Classification and catalysis (Cofactors)». vle.du.ac.in. Ανακτήθηκε στις 7 Φεβρουαρίου 2018. ^{[νεκρός σύνδεσμος]}

elmhurst.edu

«Enzyme Cofactors». Αρχειοθετήθηκε από το πρωτότυπο στις 5 Μαΐου 2003. Ανακτήθηκε στις 17 Νοεμβρίου 2007.

harvard.edu

adsabs.harvard.edu

«Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase». Science 267 (5203): 1463–9. March 1995. doi:10.1126/science.7878465. PMID 7878465. Bibcode: 1995Sci...267.1463C.
«A biological function for cadmium in marine diatoms». Proceedings of the National Academy of Sciences of the United States of America 97 (9): 4627–31. April 2000. doi:10.1073/pnas.090091397. PMID 10781068. Bibcode: 2000PNAS...97.4627L.
«Biochemistry: a cadmium enzyme from a marine diatom». Nature 435 (7038): 42. 2005. doi:10.1038/435042a. PMID 15875011. Bibcode: 2005Natur.435...42L.
«Conservation of the Enzyme–Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme». Journal of Molecular Evolution 85 (5–6): 205–218. December 2017. doi:10.1007/s00239-017-9821-9. PMID 29177972. Bibcode: 2017JMolE..85..205H.
«Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum». Proceedings of the National Academy of Sciences of the United States of America 83 (12): 4238–42. June 1986. doi:10.1073/pnas.83.12.4238. PMID 3086878. Bibcode: 1986PNAS...83.4238N.
«A novel coenzyme from bacterial primary alcohol dehydrogenases». Nature 280 (5725): 843–4. August 1979. doi:10.1038/280843a0. PMID 471057. Bibcode: 1979Natur.280..843S.
«Coenzymes as fossils of an earlier metabolic state». Journal of Molecular Evolution 7 (2): 101–4. March 1976. doi:10.1007/BF01732468. PMID 1263263. Bibcode: 1976JMolE...7..101W.
Lohmann K (August 1929). «Über die Pyrophosphatfraktion im Muskel». Naturwissenschaften 17 (31): 624–5. doi:10.1007/BF01506215. Bibcode: 1929NW.....17..624..
«A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway». Proceedings of the National Academy of Sciences of the United States of America 110 (20): 8069–74. May 2013. doi:10.1073/pnas.1304733110. PMID 23633564. Bibcode: 2013PNAS..110.8069H.

iupac.org

publications.iupac.org

de Bolster, M. W. G. (1997). GLOSSARY OF TERMS USED IN BIOINORGANIC CHEMISTRY (PDF). Pure & Appl. Chem.

jacn.org

«Biochemical functions of coenzyme Q10». Journal of the American College of Nutrition 20 (6): 591–8. December 2001. doi:10.1080/07315724.2001.10719063. PMID 11771674. http://www.jacn.org/cgi/content/full/20/6/591.

jbc.org

«Studies on the nature of the binding of thiamine pyrophosphate to enzymes». The Journal of Biological Chemistry 243 (11): 3009–19. June 1968. doi:10.1016/S0021-9258(18)93372-7. PMID 4968184. http://www.jbc.org/content/243/11/3009.
«Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen». J. Biol. Chem. 178 (2): 611–23. 1949. doi:10.1016/S0021-9258(18)56879-4. PMID 18116985. http://www.jbc.org/cgi/reprint/178/2/611.

libretexts.org

chem.libretexts.org

«Pyruvate Dehydrogenase Complex». Chemistry LibreTexts. 2013-10-02. https://chem.libretexts.org/Core/Biological_Chemistry/Metabolism/Catabolism/Pyruvate_Dehydrogenase_Complex. Ανακτήθηκε στις 2017-05-10.

nih.gov

ncbi.nlm.nih.gov

«Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins». Proteins 44 (3): 282–91. August 2001. doi:10.1002/prot.1093. PMID 11455601.
«Physiology and metabolism of essential trace elements: an outline». Clinics in Endocrinology and Metabolism 14 (3): 513–43. August 1985. doi:10.1016/S0300-595X(85)80005-0. PMID 3905079.
«Is chromium a trace essential metal?». BioFactors 11 (3): 149–62. 2000. doi:10.1002/biof.5520110301. PMID 10875302.
«The biochemistry of chromium». The Journal of Nutrition 130 (4): 715–8. April 2000. doi:10.1093/jn/130.4.715. PMID 10736319. https://archive.org/details/sim_journal-of-nutrition_2000-04_130_4/page/715.
«Iodine metabolism and thyroid physiology: current concepts». Thyroid 7 (2): 177–81. April 1997. doi:10.1089/thy.1997.7.177. PMID 9133680.
«Calcium signaling». Cell 131 (6): 1047–58. 2007. doi:10.1016/j.cell.2007.11.028. PMID 18083096.
«Ca2+ signaling and intracellular Ca2+ binding proteins». Journal of Biochemistry 120 (4): 685–98. October 1996. doi:10.1093/oxfordjournals.jbchem.a021466. PMID 8947828.
«The vanadium-containing nitrogenase of Azotobacter». BioFactors 1 (2): 111–6. July 1988. PMID 3076437.
«Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase». Science 267 (5203): 1463–9. March 1995. doi:10.1126/science.7878465. PMID 7878465. Bibcode: 1995Sci...267.1463C.
«A biological function for cadmium in marine diatoms». Proceedings of the National Academy of Sciences of the United States of America 97 (9): 4627–31. April 2000. doi:10.1073/pnas.090091397. PMID 10781068. Bibcode: 2000PNAS...97.4627L.
«Biochemistry: a cadmium enzyme from a marine diatom». Nature 435 (7038): 42. 2005. doi:10.1038/435042a. PMID 15875011. Bibcode: 2005Natur.435...42L.
«Structural analysis of heme proteins: implications for design and prediction». BMC Structural Biology 11: 13. March 2011. doi:10.1186/1472-6807-11-13. PMID 21371326.
«Iron-sulfur protein folds, iron-sulfur chemistry, and evolution». J. Biol. Inorg. Chem. 13 (2): 157–70. February 2008. doi:10.1007/s00775-007-0318-7. PMID 17992543.
«Studies on the nature of the binding of thiamine pyrophosphate to enzymes». The Journal of Biological Chemistry 243 (11): 3009–19. June 1968. doi:10.1016/S0021-9258(18)93372-7. PMID 4968184. http://www.jbc.org/content/243/11/3009.
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