Grupy prostetyczne (Polish Wikipedia)

Analysis of information sources in references of the Wikipedia article "Grupy prostetyczne" in Polish language version.

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10doi.org

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9nih.gov

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1iupac.org

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635^th place

1silverchair.com

low place

doi.org

M.W.G. de Bolster (ed.). Glossary of terms used in Bioinorganic Chemistry. „Pure & App. Chem”. 69 (6), s. 1251-1303, 1997. International Union of Pure and Applied Chemistry. DOI: 10.1351/pac199769061251. (ang.).
FMN i FAD są zwykle koenzymami, jedynie w niektórych flawoenzymach ich pierścień izoalloksazynowy reszty flawiny jest związany kowalencyjnie z resztami aminokwasowymi His, Cys lub Tyr flawoenzymu, zob.: Joosten V, van Berkel WJ. Flavoenzymes. „Curr Opin Chem Biol”. 11 (2), s. 195–202, 2007. DOI: 10.1016/j.cbpa.2007.01.010. PMID: 17275397.
Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. „Annu. Rev. Biochem.”. 73, s. 383–415, 2004. DOI: 10.1146/annurev.biochem.73.011303.074021. PMID: 15189147.
Jitrapakdee S, Wallace JC. The biotin enzyme family: conserved structural motifs and domain rearrangements. „Curr. Protein Pept. Sci.”. 4 (3), s. 217–229, 2003. DOI: 10.2174/1389203033487199. PMID: 12769720.
Banerjee R, Ragsdale SW. The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. „Annu. Rev. Biochem.”. 72, s. 209–247, 2003. DOI: 10.1146/annurev.biochem.72.121801.161828. PMID: 14527323.
Frank RA, Leeper FJ, Luisi BF. Structure, mechanism and catalytic duality of thiamine-dependent enzymes. „Cell. Mol. Life Sci.”. 64 (7-8), s. 892–905, 2007. DOI: 10.1007/s00018-007-6423-5. PMID: 17429582.
Wijayanti N, Katz N, Immenschuh S. Biology of heme in health and disease. „Curr. Med. Chem.”. 11 (8), s. 981–986, 2004. DOI: 10.2174/0929867043455521. PMID: 15078160.
Mendel RR, Hänsch R. Molybdoenzymes and molybdenum cofactor in plants. „J. Exp. Bot.”. 53 (375), s. 1689–1698, 2002. DOI: 10.1093/jxb/erf038. PMID: 12147719.
Mendel RR, Bittner F. Cell biology of molybdenum. „Biochim. Biophys. Acta”. 1763 (7), s. 621–635, 2006. DOI: 10.1016/j.bbamcr.2006.03.013. PMID: 16784786.
Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH. α-Lipoic acid in liver metabolism and disease. „Free Radic. Biol. Med.”. 24 (6), s. 1023–1039, 1998. DOI: 10.1016/S0891-5849(97)00371-7. PMID: 9607614.

iupac.org

M.W.G. de Bolster (ed.). Glossary of terms used in Bioinorganic Chemistry. „Pure & App. Chem”. 69 (6), s. 1251-1303, 1997. International Union of Pure and Applied Chemistry. DOI: 10.1351/pac199769061251. (ang.).

nih.gov

ncbi.nlm.nih.gov

FMN i FAD są zwykle koenzymami, jedynie w niektórych flawoenzymach ich pierścień izoalloksazynowy reszty flawiny jest związany kowalencyjnie z resztami aminokwasowymi His, Cys lub Tyr flawoenzymu, zob.: Joosten V, van Berkel WJ. Flavoenzymes. „Curr Opin Chem Biol”. 11 (2), s. 195–202, 2007. DOI: 10.1016/j.cbpa.2007.01.010. PMID: 17275397.
Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. „Annu. Rev. Biochem.”. 73, s. 383–415, 2004. DOI: 10.1146/annurev.biochem.73.011303.074021. PMID: 15189147.
Jitrapakdee S, Wallace JC. The biotin enzyme family: conserved structural motifs and domain rearrangements. „Curr. Protein Pept. Sci.”. 4 (3), s. 217–229, 2003. DOI: 10.2174/1389203033487199. PMID: 12769720.
Banerjee R, Ragsdale SW. The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. „Annu. Rev. Biochem.”. 72, s. 209–247, 2003. DOI: 10.1146/annurev.biochem.72.121801.161828. PMID: 14527323.
Frank RA, Leeper FJ, Luisi BF. Structure, mechanism and catalytic duality of thiamine-dependent enzymes. „Cell. Mol. Life Sci.”. 64 (7-8), s. 892–905, 2007. DOI: 10.1007/s00018-007-6423-5. PMID: 17429582.
Wijayanti N, Katz N, Immenschuh S. Biology of heme in health and disease. „Curr. Med. Chem.”. 11 (8), s. 981–986, 2004. DOI: 10.2174/0929867043455521. PMID: 15078160.
Mendel RR, Hänsch R. Molybdoenzymes and molybdenum cofactor in plants. „J. Exp. Bot.”. 53 (375), s. 1689–1698, 2002. DOI: 10.1093/jxb/erf038. PMID: 12147719.
Mendel RR, Bittner F. Cell biology of molybdenum. „Biochim. Biophys. Acta”. 1763 (7), s. 621–635, 2006. DOI: 10.1016/j.bbamcr.2006.03.013. PMID: 16784786.
Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH. α-Lipoic acid in liver metabolism and disease. „Free Radic. Biol. Med.”. 24 (6), s. 1023–1039, 1998. DOI: 10.1016/S0891-5849(97)00371-7. PMID: 9607614.

silverchair.com

watermark.silverchair.com

Mendel RR, Hänsch R. Molybdoenzymes and molybdenum cofactor in plants. „J. Exp. Bot.”. 53 (375), s. 1689–1698, 2002. DOI: 10.1093/jxb/erf038. PMID: 12147719.