Flavínadeníndinukleotid (Slovak Wikipedia)

Analysis of information sources in references of the Wikipedia article "Flavínadeníndinukleotid" in Slovak language version.

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23nih.gov

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22doi.org

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5worldcat.org

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2archive.org

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1books.google.com

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1themedicalbiochemistrypage.org

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1science.co.il

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1jbc.org

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archive.org

METZLER, David E.; METZLER, Carol M.; SAUKE, David J.. Biochemistry. 2nd. vyd. San Diego : Harcourt, Academic Press, 2003. Dostupné online. ISBN 978-0-12-492541-0.
STRYER, Lubert; BERG, Jeremy M.; TYMOCZKO, John L.. Biochemistry. 6th. vyd. New York : Freeman, 2007. Dostupné online. ISBN 978-0-7167-8724-2.

books.google.com

LIU, Shijie. Bioprocess Engineering: Kinetics, Sustainability, and Reactor Design. [s.l.] : Newnes, 2012. Dostupné online. ISBN 978-0-444-63783-3.

doi.org

dx.doi.org

Unusual flavoenzyme catalysis in marine bacteria. Current Opinion in Chemical Biology, 2016-04-01, s. 31–39. ISSN 1879-0402. DOI: 10.1016/j.cbpa.2016.01.001. PMID 26803009.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement.. Nature, 28 November 2013, s. 552–6. DOI: 10.1038/nature12643. PMID 24162851.
Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor. Journal of the American Chemical Society, 2015-07-01, s. 8078–8085. ISSN 1520-5126. DOI: 10.1021/jacs.5b03983. PMID 26067765.
Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers. Microbiology and Molecular Biology Reviews, Jun 2011, s. 321–60. DOI: 10.1128/mmbr.00030-10. PMID 21646432.
Biosynthesis of flavin cofactors in man: implications in health and disease. Current Pharmaceutical Design, 2013, s. 2649–75. DOI: 10.2174/1381612811319140014. PMID 23116402.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature, 2013-11-28, s. 552–556. ISSN 1476-4687. DOI: 10.1038/nature12643. PMID 24162851.
Emerging concepts in the flavinylation of succinate dehydrogenase. Biochimica et Biophysica Acta (BBA) - Bioenergetics, May 2013, s. 627–36. DOI: 10.1016/j.bbabio.2013.01.012. PMID 23380393.
The FAD-dependent tricarballylate dehydrogenase (TcuA) enzyme of Salmonella enterica converts tricarballylate into cis-aconitate. Journal of Bacteriology, Aug 2006, s. 5479–86. DOI: 10.1128/jb.00514-06. PMID 16855237.
Conformational behavior of flavin adenine dinucleotide: conserved stereochemistry in bound and free states. The Journal of Physical Chemistry B, Nov 2014, s. 13486–97. DOI: 10.1021/jp507629n. PMID 25389798.
Flavogenomics--a genomic and structural view of flavin-dependent proteins. The FEBS Journal, Aug 2011, s. 2625–34. DOI: 10.1111/j.1742-4658.2011.08202.x. PMID 21635694.
The human flavoproteome. Archives of Biochemistry and Biophysics, Jul 2013, s. 150–62. DOI: 10.1016/j.abb.2013.02.015. PMID 23500531.
Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis, Feb 2015, s. 518–25. DOI: 10.1002/elps.201400451. PMID 25488801.
The diverse roles of flavin coenzymes--nature's most versatile thespians. The Journal of Organic Chemistry, Aug 2007, s. 6329–42. DOI: 10.1021/jo0703092. PMID 17580897.
Structure-based classification of FAD binding sites: A comparative study of structural alignment tools. Proteins: Structure, Function, and Bioinformatics, 2016-11-01, s. 1728–1747. ISSN 1097-0134. DOI: 10.1002/prot.25158. PMID 27580869. (po anglicky)
Hanukoglu I. Electron transfer proteins of cytochrome P450 systems. Adv. Mol. Cell Biol., 1996, s. 29–55. Dostupné online. DOI: 10.1016/S1569-2558(08)60339-2.
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. Journal of Molecular Biology, Jun 1999, s. 981–90. DOI: 10.1006/jmbi.1999.2807. PMID 10369776.
Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme. Journal of Molecular Evolution, 2017, s. 205–218. DOI: 10.1007/s00239-017-9821-9. PMID 29177972.
Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin. The Journal of Biological Chemistry, Apr 1980, s. 3057–61. Dostupné online. DOI: 10.1016/S0021-9258(19)85851-9. PMID 6766943.
Prokaryotic assembly factors for the attachment of flavin to complex II. Biochimica et Biophysica Acta (BBA) - Bioenergetics, May 2013, s. 637–47. DOI: 10.1016/j.bbabio.2012.09.003. PMID 22985599.
The prokaryotic FAD synthetase family: a potential drug target. Current Pharmaceutical Design, 2013, s. 2637–48. DOI: 10.2174/1381612811319140013. PMID 23116401.
LOV to BLUF: flavoprotein contributions to the optogenetic toolkit. Molecular Plant, May 2012, s. 533–44. DOI: 10.1093/mp/sss020. PMID 22431563.
In vivo native fluorescence spectroscopy and nicotinamide adinine dinucleotide/flavin adenine dinucleotide reduction and oxidation states of oral submucous fibrosis for chemopreventive drug monitoring. Journal of Biomedical Optics, 2010, s. 017010–017010–11. DOI: 10.1117/1.3324771. PMID 20210484.

jbc.org

Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin. The Journal of Biological Chemistry, Apr 1980, s. 3057–61. Dostupné online. DOI: 10.1016/S0021-9258(19)85851-9. PMID 6766943.

nih.gov

ncbi.nlm.nih.gov

Unusual flavoenzyme catalysis in marine bacteria. Current Opinion in Chemical Biology, 2016-04-01, s. 31–39. ISSN 1879-0402. DOI: 10.1016/j.cbpa.2016.01.001. PMID 26803009.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement.. Nature, 28 November 2013, s. 552–6. DOI: 10.1038/nature12643. PMID 24162851.
Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor. Journal of the American Chemical Society, 2015-07-01, s. 8078–8085. ISSN 1520-5126. DOI: 10.1021/jacs.5b03983. PMID 26067765.
Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers. Microbiology and Molecular Biology Reviews, Jun 2011, s. 321–60. DOI: 10.1128/mmbr.00030-10. PMID 21646432.
Biosynthesis of flavin cofactors in man: implications in health and disease. Current Pharmaceutical Design, 2013, s. 2649–75. DOI: 10.2174/1381612811319140014. PMID 23116402.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature, 2013-11-28, s. 552–556. ISSN 1476-4687. DOI: 10.1038/nature12643. PMID 24162851.
Emerging concepts in the flavinylation of succinate dehydrogenase. Biochimica et Biophysica Acta (BBA) - Bioenergetics, May 2013, s. 627–36. DOI: 10.1016/j.bbabio.2013.01.012. PMID 23380393.
The FAD-dependent tricarballylate dehydrogenase (TcuA) enzyme of Salmonella enterica converts tricarballylate into cis-aconitate. Journal of Bacteriology, Aug 2006, s. 5479–86. DOI: 10.1128/jb.00514-06. PMID 16855237.
Conformational behavior of flavin adenine dinucleotide: conserved stereochemistry in bound and free states. The Journal of Physical Chemistry B, Nov 2014, s. 13486–97. DOI: 10.1021/jp507629n. PMID 25389798.
Flavogenomics--a genomic and structural view of flavin-dependent proteins. The FEBS Journal, Aug 2011, s. 2625–34. DOI: 10.1111/j.1742-4658.2011.08202.x. PMID 21635694.
The human flavoproteome. Archives of Biochemistry and Biophysics, Jul 2013, s. 150–62. DOI: 10.1016/j.abb.2013.02.015. PMID 23500531.
Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis, Feb 2015, s. 518–25. DOI: 10.1002/elps.201400451. PMID 25488801.
The diverse roles of flavin coenzymes--nature's most versatile thespians. The Journal of Organic Chemistry, Aug 2007, s. 6329–42. DOI: 10.1021/jo0703092. PMID 17580897.
Structure-based classification of FAD binding sites: A comparative study of structural alignment tools. Proteins: Structure, Function, and Bioinformatics, 2016-11-01, s. 1728–1747. ISSN 1097-0134. DOI: 10.1002/prot.25158. PMID 27580869. (po anglicky)
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. Journal of Molecular Biology, Jun 1999, s. 981–90. DOI: 10.1006/jmbi.1999.2807. PMID 10369776.
Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme. Journal of Molecular Evolution, 2017, s. 205–218. DOI: 10.1007/s00239-017-9821-9. PMID 29177972.
Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin. The Journal of Biological Chemistry, Apr 1980, s. 3057–61. Dostupné online. DOI: 10.1016/S0021-9258(19)85851-9. PMID 6766943.
HASAN, N.; NESTER, E. W.. Purification and properties of chorismate synthase from Bacillus subtilis. The Journal of Biological Chemistry, 1978-07-25, roč. 253, čís. 14, s. 4993–4998. PMID 97285. Dostupné online [cit. 2022-12-28]. ISSN 0021-9258.
Prokaryotic assembly factors for the attachment of flavin to complex II. Biochimica et Biophysica Acta (BBA) - Bioenergetics, May 2013, s. 637–47. DOI: 10.1016/j.bbabio.2012.09.003. PMID 22985599.
The prokaryotic FAD synthetase family: a potential drug target. Current Pharmaceutical Design, 2013, s. 2637–48. DOI: 10.2174/1381612811319140013. PMID 23116401.
LOV to BLUF: flavoprotein contributions to the optogenetic toolkit. Molecular Plant, May 2012, s. 533–44. DOI: 10.1093/mp/sss020. PMID 22431563.
In vivo native fluorescence spectroscopy and nicotinamide adinine dinucleotide/flavin adenine dinucleotide reduction and oxidation states of oral submucous fibrosis for chemopreventive drug monitoring. Journal of Biomedical Optics, 2010, s. 017010–017010–11. DOI: 10.1117/1.3324771. PMID 20210484.

pubmed.ncbi.nlm.nih.gov

HASAN, N.; NESTER, E. W.. Purification and properties of chorismate synthase from Bacillus subtilis. The Journal of Biological Chemistry, 1978-07-25, roč. 253, čís. 14, s. 4993–4998. PMID 97285. Dostupné online [cit. 2022-12-28]. ISSN 0021-9258.

science.co.il

Hanukoglu I. Electron transfer proteins of cytochrome P450 systems. Adv. Mol. Cell Biol., 1996, s. 29–55. Dostupné online. DOI: 10.1016/S1569-2558(08)60339-2.

themedicalbiochemistrypage.org

Vitamins, Minerals, Supplements [online]. 18 May 2020. Dostupné online.

worldcat.org

Unusual flavoenzyme catalysis in marine bacteria. Current Opinion in Chemical Biology, 2016-04-01, s. 31–39. ISSN 1879-0402. DOI: 10.1016/j.cbpa.2016.01.001. PMID 26803009.
Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor. Journal of the American Chemical Society, 2015-07-01, s. 8078–8085. ISSN 1520-5126. DOI: 10.1021/jacs.5b03983. PMID 26067765.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature, 2013-11-28, s. 552–556. ISSN 1476-4687. DOI: 10.1038/nature12643. PMID 24162851.
Structure-based classification of FAD binding sites: A comparative study of structural alignment tools. Proteins: Structure, Function, and Bioinformatics, 2016-11-01, s. 1728–1747. ISSN 1097-0134. DOI: 10.1002/prot.25158. PMID 27580869. (po anglicky)
HASAN, N.; NESTER, E. W.. Purification and properties of chorismate synthase from Bacillus subtilis. The Journal of Biological Chemistry, 1978-07-25, roč. 253, čís. 14, s. 4993–4998. PMID 97285. Dostupné online [cit. 2022-12-28]. ISSN 0021-9258.