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Luciferina (molécula) (Spanish Wikipedia)

Analysis of information sources in references of the Wikipedia article "Luciferina (molécula)" in Spanish language version.

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49nih.gov
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25doi.org
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4jbc.org
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3sciencedirect.com
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2web.archive.org
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1pnas.org
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1nature.com
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1jst.go.jp
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1archive.today
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1promega.de
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1jove.com
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1aip.org
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aip.org

spiedl.aip.org

  • O’Connell-Rodwell, CE. et al. (2008): In vivo analysis of heat-shock-protein-70 induction following pulsed laser irradiation in a transgenic reporter mouse. In: J Biomed Opt. 13(3); 030501; PMID 18601518; PDF (freier Volltextzugriff, engl.).

archive.today

doi.org

dx.doi.org

  • Waldemar Adam (1973), «Biologisches Licht», Chemie in unserer Zeit 7 (6): 182-192, doi:10.1002/ciuz.19730070605 .
  • E. H. White et al.: The chemi- and bioluminescence of firefly luciferin: an efficient chemical production of electronically excited states. In: Bioorg. Chem. Bd. 1, Nr. 1–2, 1971, S. 92–122, doi 10.1016/0045-2068(71)90009-5.
  • Fraga, H. (2008): Firefly luminescence: a historical perspective and recent developments. In: Photochem Photobiol Sci. 7(2); 146–158; PMID 18264582; doi 10.1039/b719181b.
  • Day, JC. et al. (2004): Evolution of beetle bioluminescence: the origin of beetle luciferin. In: Luminescence, 19(1); 8–20; PMID 14981641; doi 10.1002/bio.749.
  • Hastings JW. (1996): Chemistries and colors of bioluminescent reactions: a review. In: Gene, 173(1 Spec No); 5–11; PMID 8707056; doi 10.1016/0378-1119(95)00676-1.
  • DeLuca, M. und Dempsey, ME. (1970): Mechanism of oxidation in firefly luminescence. In: Biochem Biophys Res Commun, 40(1); 117–122; PMID 5456946; doi 10.1016/0006-291X(70)91054-5.
  • Tsuji, FI. et al. (1977): Mechanism of the enzyme-catalyzed oxidation of Cypridina and firefly luciferins studied by means of 17O2 and H218O. In: Biochem Biophys Res Commun, 74(2); 606–613; PMID 836314; doi 10.1016/0006-291X(77)90346-1.
  • Ando, Y. et al. (2008): Firefly bioluminescence quantum yield and colour change by pH-sensitive green emission, in: Nat. Photonics 2; 44–47; doi 10.1038/nphoton.2007.251.
  • Marques, SM. und Esteves, da Silva JC. (2009): Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. In: IUBMB Life, 61(1):6–17; PMID 18949818; doi 10.1002/iub.134.
  • Wu, C. et al. (2003): Tracer studies on dinoflagellate luciferin with [15N]-glycine and [15N]-l-glutamic acid in the dinoflagellate Pyrocystis lunula, in: Tetrahedron Letters, 44(6); 1263–1266; doi 10.1016/S0040-4039(02)02815-0.
  • Greer III., LF. und Szalay, AA. (2002): Imaging of light emission from the expression of luciferases in living cells and organisms: a review, in: Luminescence, 17, 43–74; PMID 11816060; doi 10.1002/bio.676.
  • Tu, SC. (2008): Activity coupling and complex formation between bacterial luciferase and flavin reductases. In: Photochem Photobiol Sci, 7(2); 183–188; PMID 18264585; doi 10.1039/b713462b
  • Shimomura, O. et al. (1980): Widespread occurrence of coelenterazine in marine bioluminescence, in: Comp. Biochem. Physiol., 65B, 435–437(doi 10.1016/0305-0491(80)90044-9).
  • Campbell, AK. und Herring, PJ. (1990): Imidazolopyrazine bioluminescence in copepods and other marine organisms, in: Mar. Biol. 104(2); 219–225; doi 10.1007/BF01313261.
  • Shimomura, O. (1987): Presence of coelenterazine in non-bioluminescent marine organisms, in: Comp Biochem Physiol, 86B (1987); 361–363 (doi 10.1016/0305-0491(87)90306-3).
  • Inoue, S. et al. (1976): Squid bioluminescence III. Isolation and structure of Watasenia luciferin. In: Tetrahedron Lett, 17(34); 2971–2972; doi 10.1016/S0040-4039(01)85503-9.
  • Teranishi, K. und Shimomura, O. (2008): Bioluminescence of the arm light organs of the luminous squid Watasenia scintillans.. In: Biochim Biophys Acta 1780(5); 784–792; PMID 18294462; doi 10.1016/j.bbagen.2008.01.016
  • Morin, JG. (2011): Based on a review of the data, use of the term 'cypridinid' solves the Cypridina/Vargula dilemma for naming the constituents of the luminescent system of ostracods in the family Cypridinidae. In: Luminescence 26(1); 1–4; PMID 19862683; doi 10.1002/bio.1178
  • Kato, S. et al. (2004): Identification of the biosynthetic units of Cypridina luciferin in Cypridina (Vargula) hilgendorfii by LC/ESI-TOF-MS, in: Tetrahedron 60(50); 11427–11434; doi 10.1016/j.tet.2004.09.080.
  • Kato S. et al. (2006): Stereoselective incorporation of isoleucine into Cypridina luciferin in Cypridina hilgendorfii (Vargula hilgendorfii), in: Biosci Biotechnol Biochem, 70(6); 1528–1532; PMID 16794342; doi 10.1271/bbb.60066; PDF (freier Volltextzugriff, engl.).
  • Ohmiya, Y. et al. (2005): Bioluminescence in the Limpet-Like Snail, Latia neritoides, in: Bull. Chem. Soc. Jpn., 78 (7); 1197–1205; doi 10.1246/bcsj.78.1197.
  • Nakamura, M. et al. (2004): Synthesis of Latia luciferin benzoate analogues and their bioluminescent activity, in: Tetrahedron Letters, 45 (10), 2203–2205, doi 10.1016/j.tetlet.2004.01.027.
  • Petushkov, VN. et al. (2014): A novel type of luciferin from the Siberian luminous earthworm Fridericia heliota: structure elucidation by spectral studies and total synthesis. In: Angew Chem Int Ed Engl. 53(22); 5566–5568; PMID 24737705; doi 10.1002/anie.201400529
  • Hawronskyj, J.-M. und Holah, J. (1997): ATP: a universal hygiene monitor. In: Trends Food Sci. Tech., 8; 79–84; doi 10.1016/S0924-2244(97)01009-1.
  • Lim, E. et al. (2009): In vivo bioluminescent imaging of mammary tumors using IVIS spectrum. In: J Vis Exp, 26. pii: 1210. PMID 19404236; doi 10.3791/1210; mit Video (engl).

jbc.org

  • Gomi K. und Kajiyama N. (2001): Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin, in: J Biol Chem, 276 (39); 36508–36513; PMID 11457857; PDF (freier Volltextzugriff, engl.)
  • Morse, D. et al. (1989): Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra, in: J Biol Chem, 264 (20), 11822–11826; PMID 2745419; PDF (freier Volltextzugriff, engl.)
  • Fisher, AJ. et al. (1996): The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. In: J Biol Chem, 271(36); 21956–21968; PMID 8703001; PDF Archivado el 30 de marzo de 2008 en Wayback Machine. (freier Volltextzugriff, engl.)
  • Rodriguez A. et al. (1983): Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria. Properties and acyltransferase activity, in: J Biol Chem, 258(8); 5233–5237; PMID 6833298; PDF (freier Volltextzugriff, engl.)

jove.com

jst.go.jp

jstage.jst.go.jp

  • Kato S. et al. (2006): Stereoselective incorporation of isoleucine into Cypridina luciferin in Cypridina hilgendorfii (Vargula hilgendorfii), in: Biosci Biotechnol Biochem, 70(6); 1528–1532; PMID 16794342; doi 10.1271/bbb.60066; PDF (freier Volltextzugriff, engl.).

nature.com

  • Head JF. et al. (2000): The crystal structure of the photoprotein aequorin at 2.3 Å resolution, in: Nature, 405 (6784); 291–293; PMID 10830969; PDF (freier Volltextzugriff, engl.)

nih.gov

ncbi.nlm.nih.gov

  • Herring PJ. (1987): Systematic distribution of bioluminescence in living organisms, in: J Biolumin Chemilumin, 1 (3); 147–163; PMID 3503524.
  • Keller, GA. et al. (1987): Firefly luciferase is targeted to peroxisomes in mammalian cells, in: Proc Natl Acad Sci USA, 84 (10): 3264–3268; PMID 3554235; PMC 304849.
  • Fraga, H. (2008): Firefly luminescence: a historical perspective and recent developments. In: Photochem Photobiol Sci. 7(2); 146–158; PMID 18264582; doi 10.1039/b719181b.
  • Day, JC. et al. (2004): Evolution of beetle bioluminescence: the origin of beetle luciferin. In: Luminescence, 19(1); 8–20; PMID 14981641; doi 10.1002/bio.749.
  • Hastings JW. (1996): Chemistries and colors of bioluminescent reactions: a review. In: Gene, 173(1 Spec No); 5–11; PMID 8707056; doi 10.1016/0378-1119(95)00676-1.
  • Shimomura, O. et al. (1977): Source of oxygen in the CO2 produced in the bioluminescent oxidation of firefly luciferin. In: Proc Natl Acad Sci USA, 74(7); 2799–2802; PMID 16592418; PMC 431296.
  • DeLuca, M. und Dempsey, ME. (1970): Mechanism of oxidation in firefly luminescence. In: Biochem Biophys Res Commun, 40(1); 117–122; PMID 5456946; doi 10.1016/0006-291X(70)91054-5.
  • Tsuji, FI. et al. (1977): Mechanism of the enzyme-catalyzed oxidation of Cypridina and firefly luciferins studied by means of 17O2 and H218O. In: Biochem Biophys Res Commun, 74(2); 606–613; PMID 836314; doi 10.1016/0006-291X(77)90346-1.
  • Eisner T. et al. (1997): Firefly»femmes fatales« acquire defensive steroids (lucibufagins) from their firefly prey, in: Proc Natl Acad Sci USA, 94 (18), 9723–9728; PMID 9275191; PMC 23257.
  • Gomi K. und Kajiyama N. (2001): Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin, in: J Biol Chem, 276 (39); 36508–36513; PMID 11457857; PDF (freier Volltextzugriff, engl.)
  • Niwa, K. et al. (2006): Stereoisomeric bio-inversion key to biosynthesis of firefly D-luciferin, in: FEBS Lett, 580 (22); 5283–5287; PMID 16979628; PDF (freier Volltextzugriff, engl.)
  • Lembert N. (1996): Firefly luciferase can use L-luciferin to produce light, in: Biochem J, 317 (Pt 1); 273–277; PMID 8694774; PMC 1217473.
  • Oba Y. et al. (2013): Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of L-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis. In: PLoS ONE 8(12): PMC 3877152; PMID 24391868
  • Oba, Y. et al. (2003): Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase. In: FEBS Lett, 540(1–3); 251–254; PMID 12681517; PDF (freier Volltextzugriff, engl.)
  • Marques, SM. und Esteves, da Silva JC. (2009): Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. In: IUBMB Life, 61(1):6–17; PMID 18949818; doi 10.1002/iub.134.
  • Morse, D. und Mittag, M. (2000): Dinoflagellate luciferin-binding protein, in: Methods Enzymol, 305, 258–276; PMID 10812606.
  • Morse, D. et al. (1989): Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra, in: J Biol Chem, 264 (20), 11822–11826; PMID 2745419; PDF (freier Volltextzugriff, engl.)
  • Fogel, M. und Hastings, JW. (1971): A substrate-binding protein in the Gonyaulax bioluminescence reaction, in: Arch Biochem Biophys, 142(1): 310–321; PMID 5545485.
  • Schultz, LW. et al. (2005): Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole, in: Proc Natl Acad Sci USA, 102(5): 1378–1383; PMID 15665092; PDF (freier Volltextzugriff, engl.).
  • Fogel M und Hastings JW. (1972): Bioluminescence: mechanism and mode of control of scintillon activity, in: Proc Natl Acad Sci USA, 69(3):690–369; PMID 4501583; PMC 426536.
  • T. Wilson and JW. Hastings (1998): Bioluminscence, in: Annu. Rev. Cell Dev., 14; 197–230; PMID 9891783.
  • Greer III., LF. und Szalay, AA. (2002): Imaging of light emission from the expression of luciferases in living cells and organisms: a review, in: Luminescence, 17, 43–74; PMID 11816060; doi 10.1002/bio.676.
  • Tu, SC. (2008): Activity coupling and complex formation between bacterial luciferase and flavin reductases. In: Photochem Photobiol Sci, 7(2); 183–188; PMID 18264585; doi 10.1039/b713462b
  • Fisher, AJ. et al. (1996): The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. In: J Biol Chem, 271(36); 21956–21968; PMID 8703001; PDF Archivado el 30 de marzo de 2008 en Wayback Machine. (freier Volltextzugriff, engl.)
  • Duane, W. und Hastings, JW. (1975): Flavin mononucleotide reductase of luminous bacteria, in: Mol Cell Biochem. 6(1); 53–64; PMID 47604.
  • Rodriguez A. et al. (1983): Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria. Properties and acyltransferase activity, in: J Biol Chem, 258(8); 5233–5237; PMID 6833298; PDF (freier Volltextzugriff, engl.)
  • Shimomura, O. et al. (1963): Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea, in: J Cell Comp Physiol, 59; 223–239; PMID 13911999.
  • Shimomura, O. et al. (1974): Mechanism of the luminescent intramolecular reaction of aequorin, in: Biochemistry, 13(16); 3278–3286; PMID 4152180.
  • Head JF. et al. (2000): The crystal structure of the photoprotein aequorin at 2.3 Å resolution, in: Nature, 405 (6784); 291–293; PMID 10830969; PDF (freier Volltextzugriff, engl.)
  • Shimomura, O. und Johnson, FH. (1970): Calcium binding, quantum yield, and emitting molecule in aequorin bioluminescence, in: Nature, 227 (5265); 1356–1357; PMID 4393938.
  • Teranishi, K. und Shimomura, O. (2008): Bioluminescence of the arm light organs of the luminous squid Watasenia scintillans.. In: Biochim Biophys Acta 1780(5); 784–792; PMID 18294462; doi 10.1016/j.bbagen.2008.01.016
  • Tsuji FI. (2005): Role of molecular oxygen in the bioluminescence of the firefly squid, Watasenia scintillans, in: Biochem Biophys Res Commun, 338(1): 250–253; PMID 16165097.
  • Morin, JG. (2011): Based on a review of the data, use of the term 'cypridinid' solves the Cypridina/Vargula dilemma for naming the constituents of the luminescent system of ostracods in the family Cypridinidae. In: Luminescence 26(1); 1–4; PMID 19862683; doi 10.1002/bio.1178
  • Johnson, FH. und Shimomura, O. (1972): Enzymatic and nonenzymatic bioluminescence, in: Photophysiology, (7); 275–334; PMID 4376836.
  • Kato S. et al. (2006): Stereoselective incorporation of isoleucine into Cypridina luciferin in Cypridina hilgendorfii (Vargula hilgendorfii), in: Biosci Biotechnol Biochem, 70(6); 1528–1532; PMID 16794342; doi 10.1271/bbb.60066; PDF (freier Volltextzugriff, engl.).
  • Tsuji, FI. und Leisman, GB. (1981): K/Na-triggered bioluminescence in the oceanic squid Symplectoteuthis oualaniensis. In: Proc Natl Acad Sci USA, 78(11); 6719–6723; PMID 16593119; PMC 349121.
  • Shimomura, O. und Johnson, FH. (1968): The structure of Latia luciferin, in: Biochemistry 7(5): 1734–1738; PMID 5650377.
  • Shimomura, O. et al. (1972): Reactions Involved in Bioluminescence Systems of Limpet (Latia neritoides) and Luminous Bacteria, in: Proc Natl Acad Sci USA, 69 (8), 2086–2089; PMID 4506078; PMC 426874.
  • Rudie, NG. et al. (1976): Purification and properties of luciferin from the bioluminescent earthworm, Diplocardia longa, in: Photochem Photobiol, 23 (1): 71–75; PMID 1265130.
  • Rudie, NG. et al. (1981): Earthworm bioluminescence: characterization of high specific activity Diplocardia longa luciferase and the reaction it catalyzes, in: Biochemistry, 20 (2): 344–350; PMID 6258637.
  • Petushkov, VN. et al. (2014): A novel type of luciferin from the Siberian luminous earthworm Fridericia heliota: structure elucidation by spectral studies and total synthesis. In: Angew Chem Int Ed Engl. 53(22); 5566–5568; PMID 24737705; doi 10.1002/anie.201400529
  • Neufeld HA. et al. (1975): A rapid method for determining ATP by the firefly luciferin-luciferase system, in: Experientia, 31 (3), 391–392; PMID 1116561.
  • Knight, MR. et al. (1991): Recombinant aequorin as a probe for cytosolic free Ca2+ in Escherichia coli, in: FEBS Lett., 282 (2); 405–408; PMID 2037058; PDF (freier Volltextzugriff, engl.)
  • Kendall, JM et al. (1992): Targeting aequorin to the endoplasmic reticulum of living cells., in: Biochem. Biophys. Res. Commun., 189 (2); 1008–1016; PMID 1472014.
  • Knight, MR. et al. (1991): Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium, in: Nature, 352(6335); 524–526; PMID 1865907.
  • Hampf M, Gossen M: A protocol for combined Photinus and Renilla luciferase quantification compatible with protein assays. Anal Biochem. 2006 Sep 1;356(1):94–99, PMID 16750160.
  • Lim, E. et al. (2009): In vivo bioluminescent imaging of mammary tumors using IVIS spectrum. In: J Vis Exp, 26. pii: 1210. PMID 19404236; doi 10.3791/1210; mit Video (engl).
  • O’Connell-Rodwell, CE. et al. (2008): In vivo analysis of heat-shock-protein-70 induction following pulsed laser irradiation in a transgenic reporter mouse. In: J Biomed Opt. 13(3); 030501; PMID 18601518; PDF (freier Volltextzugriff, engl.).

pubchem.ncbi.nlm.nih.gov

pnas.org

  • Schultz, LW. et al. (2005): Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole, in: Proc Natl Acad Sci USA, 102(5): 1378–1383; PMID 15665092; PDF (freier Volltextzugriff, engl.).

promega.de

sciencedirect.com

pdn.sciencedirect.com

  • Niwa, K. et al. (2006): Stereoisomeric bio-inversion key to biosynthesis of firefly D-luciferin, in: FEBS Lett, 580 (22); 5283–5287; PMID 16979628; PDF (freier Volltextzugriff, engl.)
  • Oba, Y. et al. (2003): Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase. In: FEBS Lett, 540(1–3); 251–254; PMID 12681517; PDF (freier Volltextzugriff, engl.)
  • Knight, MR. et al. (1991): Recombinant aequorin as a probe for cytosolic free Ca2+ in Escherichia coli, in: FEBS Lett., 282 (2); 405–408; PMID 2037058; PDF (freier Volltextzugriff, engl.)

web.archive.org