Luciferine (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Luciferine" in German language version.

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cas.org

commonchemistry.cas.org

chemspider.com

doi.org

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  • Emil H. White, Eliezer Rapaport, Howard H. Seliger, Thomas A. Hopkins: The chemi- and bioluminescence of firefly luciferin: an efficient chemical production of electronically excited states. In: Bioorg. Chem., Band 1, Nr. 1–2, September 1971, S. 92–122, doi:10.1016/0045-2068(71)90009-5.
  • G. A. Keller, S. Gould, M. Deluca, S. Subramani: Firefly luciferase is targeted to peroxisomes in mammalian cells. In: Proc Natl Acad Sci USA, Band 84, Nr. 10, Mai 1987, S. 3264–3268, doi:10.1073/pnas.84.10.3264.
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  • J. W. Hastings: Chemistries and colors of bioluminescent reactions: a review. In: Gene, Band 173, Nr. 1 special, 1996, S. 5–11, PMID 8707056, doi:10.1016/0378-1119(95)00676-1.
  • Osamu Shimomura, Toshio Goto, Frank H. Johnson: Source of oxygen in the CO2 produced in the bioluminescent oxidation of firefly luciferin. In: Proc Natl Acad Sci USA, Band 74, Nr. 7, Juli 1977, S. 2799–2802, doi:10.1073/pnas.74.7.2799.
  • M. DeLuca, M. E. Dempsey: Mechanism of oxidation in firefly luminescence. In: Biochem Biophys Res Commun, Band 40, Nr. 1, 1970, S. 117–122, PMID 5456946, doi:10.1016/0006-291X(70)91054-5.
  • F. I. Tsuji, M. DeLuca, P. D. Boyer, S. Endo, M. Akutagawa: Mechanism of the enzyme-catalyzed oxidation of Cypridina and firefly luciferins studied by means of 17O2 and H218O. In: Biochem Biophys Res Commun., Band 74, Nr. 2, Januar 1977, S. 606–613, doi:10.1016/0006-291X(77)90346-1.
  • Yoriko Ando, Kazuki Niwa, Nobuyuki Yamada, Toshiteru Enomoto, Tsutomu Irie, Hidehiro Kubota, Yoshihiro Ohmiya, Hidefumi Akiyama: Firefly bioluminescence quantum yield and colour change by pH-sensitive green emission. In: Nature Photonics, Band 2, 2008, S. 44–47, doi:10.1038/nphoton.2007.251.
  • K. Gomi, N. Kajiyama: Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin. In: J Biol Chem., Band 276, Nr. 39, 2001, S. 36508–36513, doi:10.1074/jbc.M105528200 (PDF).
  • Kazuki Niwa, Mitsuhiro Nakamura, Yoshihiro Ohmiya: Stereoisomeric bio-inversion key to biosynthesis of firefly D-luciferin. In: FEBS Letters, Band 580, Nr. 22, 2006, S. 5283–5287, doi:10.1016/j.febslet.2006.08.073 (PDF).
  • N. Lembert: Firefly luciferase can use L-luciferin to produce light. In: Biochem J., Band 317, Teil 1, Juli 1996, S. 273–277, doi:10.1042/bj3170273. PMC 1217473 (freier Volltext).
  • Yuichi Oba, Naoki Yoshida, Shusei Kanie, Makoto Ojika, Satoshi Inouye: 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, Band 8, Nr. 12, Dezember 2013, doi:10.1371/journal.pone.0084023; dazu gibt es eine Korrektur: PMC 3978032 (freier Volltext).
  • Yuichi Oba, Makoto Ojika, Satoshi Inouye: Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase. In: FEBS Lett., Band 540, Nr. 1–3, April 2003, S. 251–254, doi:10.1016/S0014-5793(03)00272-2 (PDF).
  • Y. Oba, K. Konishi, D. Yano, H. Shibata, D. Kato: Resurrecting the ancient glow of the fireflies. In: Science Advances. Band 6, Nr. 49, 2. Dezember 2020, doi:10.1126/sciadv.abc5705, PMID 33268373, PMC 7710365 (freier Volltext).
  • Oliver C. Watkins, Miriam L. Sharpe, Nigel B. Perry, Kurt L. Krause: New Zealand glowworm (Arachnocampa luminosa) bioluminescence is produced by a firefly-like luciferase but an entirely new luciferin. In: Scientific Reports. Band 8, Nr. 1, 19. Februar 2018, S. 3278, doi:10.1038/s41598-018-21298-w, PMID 29459729.
  • S. M. Marques, J. C. da Silva Esteves: Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. In: IUBMB Life, Band 61, Nr. 1, 2009, S. 6–17, doi:10.1002/iub.134.
  • Carlos Fajardo, Marcos De Donato, Hectorina Rodulfo, Gonzalo Martinez-Rodriguez, Benjamin Costas: New Perspectives Related to the Bioluminescent System in Dinoflagellates: Pyrocystis lunula, a Case Study. In: International Journal of Molecular Sciences. Band 21, Nr. 5, 5. März 2020, doi:10.3390/ijms21051784, PMID 32150894, PMC 7084563 (freier Volltext).
  • D. Morse, M. Mittag: Dinoflagellate luciferin-binding protein. In: Methods Enzymol., Band 305, 2000, S. 258–276, doi:10.1016/s0076-6879(00)05493-8.
  • Margaret Fogel, J. Woodland Hastings: A substrate-binding protein in the Gonyaulax bioluminescence reaction. In: Arch Biochem Biophys., Band 142, Nr. 1, Januar 1971, S. 310–321, doi:10.1016/0003-9861(71)90289-X.
  • L. Wayne Schultz, Liyun Liu, Margaret Cegielski, J. Woodland Hastings: Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. In: Proc Natl Acad Sci USA, Band 102, Nr. 5, 2005, S. 1378–1383, doi:10.1073/pnas.0409335102 (PDF).
  • Margaret Fogel, J. W. Hastings: Bioluminescence: mechanism and mode of control of scintillon activity. In: Proc Natl Acad Sci USA, Band 69, Nr. 3, März 1972, S. 690–369, doi:10.1073/pnas.69.3.690 (PDF).
  • Chun Wu, Hidetoshi Akimoto, Yoshihiro Ohmiya: Tracer studies on dinoflagellate luciferin with [15N]-glycine and [15N]-l-glutamic acid in the dinoflagellate Pyrocystis lunula. In: Tetrahedron Letters, Band 44, Nr. 6, 2003, S. 1263–1266, doi:10.1016/S0040-4039(02)02815-0.
  • Lee F. Greer, Aladar A. Szalay: Imaging of light emission from the expression of luciferases in living cells and organisms: a review. In: Luminescence, Band 17, Januar-Februar 2002, S. 43–74, doi:10.1002/bio.676 (PDF).
  • S. C. Tu: Activity coupling and complex formation between bacterial luciferase and flavin reductases. In: Photochem Photobiol Sci., Band 7, Nr. 2, 2008, 2008, S. 183–188, doi:10.1039/b713462b.
  • A. J. Fisher, T. B. Thompson, J. B. Thoden, T. O. Baldwin, I. Rayment: The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. In: J Biol Chem., Band 271, Nr. 36, September 1996, S. 21956–21968, doi:10.1074/jbc.271.36.21956 (PDF).
  • W. Duane, J. W. Hastings: Flavin mononucleotide reductase of luminous bacteria. In: Mol Cell Biochem., Band 6, Nr. 1, Januar 1975, S. 53–64, doi:10.1007/BF01731866.
  • John Lee, Franz Müller, Antonie J. W. G. Visser: The Sensitized Bioluminescence Mechanism of Bacterial Luciferase. In: Photochemistry and Photobiology. 28. November 2018, doi:10.1111/php.13063, PMID 30485901.
  • Osamu Shimomura, Shoji Inoue, Frank H. Johnson, Yata Haneda: Widespread occurrence of coelenterazine in marine bioluminescence. In: Comp. Biochem. Physiol., Band 65, Nr. 2, 1980, S. 435–437, doi:10.1016/0305-0491(80)90044-9.
  • A. K. Campbell, P. J. Herring: Imidazolopyrazine bioluminescence in copepods and other marine organisms. In: Mar. Biol., Band 104, Nr. 2, 1990, S. 219–225, doi:10.1007/BF01313261.
  • Osamu Shimomura: Presence of coelenterazine in non-bioluminescent marine organisms. In: Comp Biochem Physiol. Teil B, Band 86, Nr. 2, 1987, S. 361–363, doi:10.1016/0305-0491(87)90306-3.
  • O. Shimomura, F. H. Johnson, Y. Saiga: Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. In: J Cell Comp Physiol., Band 59, Juni 1963, S. 223–239, doi:10.1002/jcp.1030590302 (PDF).
  • Osamu Shimomura, Frank H. Johnson, Hiroshi Morise: Mechanism of the luminescent intramolecular reaction of aequorin. In: Biochemistry, Band 13, Nr. 16, Juli 1974, S. 3278–3286, doi:10.1021/bi00713a016.
  • J. F. Head, S. Inouye, K. Teranishi, O. Shimomura: The crystal structure of the photoprotein aequorin at 2.3 Å resolution. In: Nature, Band 405, Nr. 6784, Mai 2000, S. 291–293, doi:10.1038/35012659 (PDF).
  • Shoji Inoue, Hisae Kakoi, Toshio Goto: Squid bioluminescence III. Isolation and structure of Watasenia luciferin. In: Tetrahedron Lett., Band 17, Nr. 34, August 1976, S. 2971–2972, doi:10.1016/S0040-4039(01)85503-9.
  • Katsunori Teranishi, Osamu Shimomura: Bioluminescence of the arm light organs of the luminous squid Watasenia scintillans. In: Biochim Biophys Acta., Band 1780, Nr. 5, Mai 2008, S. 784–792, doi:10.1016/j.bbagen.2008.01.016 (PDF).
  • Frederick I. Tsuji: Role of molecular oxygen in the bioluminescence of the firefly squid, Watasenia scintillans. In: Biochem Biophys Res Commun., Band 338, Nr. 1, September 2005, S. 250–253, doi:10.1016/j.bbrc.2005.08.215.
  • J. G. Morin: 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, Band 26, Nr. 1, 2011, S. 1–4, doi:10.1002/bio.1178.
  • Shin-ichi Kato, Yuichi Oba, Makoto Ojika, Satoshi Inouye: Identification of the biosynthetic units of Cypridina luciferin in Cypridina (Vargula) hilgendorfii by LC/ESI-TOF-MS. In: Tetrahedron, Band 60, Nr. 50, 2004, S. 11427–11434, doi:10.1016/j.tet.2004.09.080 (PDF).
  • Shin-ichi Kato, Yuichi Oba, Makoto Ojika, Satoshi Inouye: Stereoselective incorporation of isoleucine into Cypridina luciferin in Cypridina hilgendorfii (Vargula hilgendorfii). In: Bioscience, Biotechnology, and Biochemistry, Band 70, Nr. 6, März 2006, S. 1528–1532, doi:10.1271/bbb.60066 (PDF).
  • Frederick I. Tsuji, Gary B. Leisman: K/Na-triggered bioluminescence in the oceanic squid Symplectoteuthis oualaniensis. In: Proc Natl Acad Sci USA, Band 78, Nr. 11, November 1981, S. 6719–6723, doi:10.1073/pnas.78.11.6719 (PDF).
  • Konstantin V. Purtov, Valentin N. Petushkov, Mikhail S. Baranov, Konstantin S. Mineev, Natalja S. Rodionova, Zinaida M. Kaskova, Aleksandra S. Tsarkova, Alexei I. Petunin, Vladimir S. Bondar, Emma K. Rodicheva, Svetlana E. Medvedeva, Yuichi Oba, Yumiko Oba, Alexander S. Arseniev, Sergey Lukyanov, Josef I. Gitelson, Ilia V. Yampolsky: The chemical basis of fungal bioluminescence. In: Angew Chem Int Ed Engl., Band 54, Nr. 28, 2015, S. 8124–8128, doi:10.1002/anie.201501779 (PDF).
  • Alexey A. Kotlobay, Karen S. Sarkisyan, Yuliana A. Mokrushina, Marina Marcet-Houben, Ekaterina O. Serebrovskaya, Nadezhda M. Markina, Louisa Gonzalez Somermeyer, Andrey Y. Gorokhovatsky, Andrey Vvedensky, Konstantin V. Purtov, Valentin N. Petushkov, Natalja S. Rodionova, Tatiana V. Chepurnyh, Liliia I. Fakhranurova, Elena B. Guglya, Rustam Ziganshin, Aleksandra S. Tsarkova, Zinaida M. Kaskova, Victoria Shender, Maxim Abakumov, Tatiana O. Abakumova, Inna S. Povolotskaya, Fedor M. Eroshkin, Andrey G. Zaraisky, Alexander S. Mishin, Sergey V. Dolgov, Tatiana Y. Mitiouchkina, Eugene P. Kopantzev, Hans E. Waldenmaier, Anderson G. Oliveira, Yuichi Oba, Ekaterina Barsova, Ekaterina A. Bogdanova, Toni Gabaldón, Cassius V. Stevani, Sergey Lukyanov, Ivan V. Smirnov, Josef I. Gitelson, Fyodor A. Kondrashov, Ilia V. Yampolsky: Genetically encodable bioluminescent system from fungi. In: Proceedings of the National Academy of Sciences. Band 115, Nr. 50, 11. Dezember 2018, S. 12728–12732, doi:10.1073/pnas.1803615115, PMID 30478037.
  • Tatiana Mitiouchkina, Alexander S. Mishin, Louisa Gonzalez Somermeyer, Nadezhda M. Markina, Tatiana V. Chepurnyh, Elena B. Guglya, Tatiana A. Karataeva, Kseniia A. Palkina, Ekaterina S. Shakhova, Liliia I. Fakhranurova, Sofia V. Chekova, Aleksandra S. Tsarkova, Yaroslav V. Golubev, Vadim V. Negrebetsky, Sergey A. Dolgushin, Pavel V. Shalaev, Dmitry Shlykov, Olesya A. Melnik, Victoria O. Shipunova, Sergey M. Deyev, Andrey I. Bubyrev, Alexander S. Pushin, Vladimir V. Choob, Sergey V. Dolgov, Fyodor A. Kondrashov, Ilia V. Yampolsky, Karen S. Sarkisyan: Plants with genetically encoded autoluminescence. In: Nature Biotechnology. 38. Jahrgang, Nr. 8, 27. April 2020, S. 944–946, doi:10.1038/s41587-020-0500-9, PMID 32341562.
  • Osamu Shimomura, Frank H. Johnson, Yasuhiro Kohama: Reactions involved in bioluminescence systems of limpet (Latia neritoides) and luminous bacteria. In: Proc Natl Acad Sci, Band 69, Nr. 8, August, S. 2086–2089, doi:10.1073/pnas.69.8.2086 (PDF).
  • Ohmiya Yoshihiro, Kojima Satoshi, Nakamura Mitsuhiro, Niwa Haruki: Bioluminescence in the limpet-like snail, Latia neritoides. In: Bull. Chem. Soc. Jpn., Band 78, Nr. 7, 2005, S. 1197–1205, doi:10.1246/bcsj.78.1197.
  • Mitsuhiro Nakamura, Mizuki Masaki, Shojiro Maki, Ryo Matsui, Minako Hieda, Masashi Mamino, Takashi Hirano, Yoshihiro Ohmiya, Haruki Niwa: Synthesis of Latia luciferin benzoate analogues and their bioluminescent activity. In: Tetrahedron Letters, Band 45, Nr. 10, März 2004, S. 2203–2205, doi:10.1016/j.tetlet.2004.01.027 (PDF).
  • Natalja S. Rodionova, Emilia Rota, Aleksandra S. Tsarkova, Valentin N. Petushkov: Progress in the Study of Bioluminescent Earthworms. In: Photochemistry and Photobiology. Band 93, Nr. 2, März 2017, S. 416–428, doi:10.1111/php.12709, PMID 28063169.
  • N. G. Rudie, H. Ohtsuka, J. E. Wampler: Purification and properties of luciferin from the bioluminescent earthworm, Diplocardia longa. In: Photochem Photobiol., Band 23, Nr. 1, Januar 1976, S. 71–75, doi:10.1111/j.1751-1097.1976.tb06774.x.
  • N. G. Rudie, M. G. Mulkerrin, J. E. Wampler: Earthworm bioluminescence: characterization of high specific activity Diplocardia longa luciferase and the reaction it catalyzes. In: Biochemistry, Band 20, Nr. 2, Januar 1981, S. 344–350, doi:10.1021/bi00505a018.
  • Maxim A. Dubinnyi, Zinaida M. Kaskova, Natalja S. Rodionova, Mikhail S. Baranov, Andrey Yu. Gorokhovatsky, Alexey Kotlobay, Kyril M. Solntsev, Aleksandra S. Tsarkova, Valentin N. Petushkov, Ilia V. Yampolsky: Novel mechanism of bioluminescence: oxidative decarboxylation of a moiety adjacent to the light emitter of Fridericia luciferin. In: Angew Chem Int Ed Engl. 54(24), 2015, S. 7065–7067. PMID 25913753; doi:10.1002/anie.201501668
  • Valentin N. Petushkov, Maxim A. Dubinnyi, Aleksandra S. Tsarkova, Natalja S. Rodionova, Mikhail S. Baranov, Vadim S. Kublitski, Osamu Shimomura, Ilia V. Yampolsky: 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., Band 53, Nr. 22, April 2014, S. 5566–5568, doi:10.1002/anie.201400529 (Manuskript).
  • H. A. Neufeld, R. D. Towner, J. Pace: A rapid method for determining ATP by the firefly luciferin-luciferase system. In: Experientia, Band 31, Nr. 3, März 1975, S. 391–392, doi:10.1007/BF01922604.
  • Jane-Marie Hawronskyj, John Holah: ATP: a universal hygiene monitor. In: Trends Food Sci. Tech., Band 8, März 1997, S. 79–84, doi:10.1016/S0924-2244(97)01009-1.
  • M. R. Knight, A. K. Campbell, S. M. Smith, A. J. Trewavas: Recombinant aequorin as a probe for cytosolic free Ca2+ in Escherichia coli. In: FEBS Lett., Band 282, Nr. 2, Mai 1991, S. 405–408, doi:10.1016/0014-5793(91)80524-7 (PDF).
  • J. M. Kendall, R. L. Dormer, A. K. Campbell: Targeting aequorin to the endoplasmic reticulum of living cells. In: Biochem. Biophys. Res. Commun., Band 189, Nr. 2, Dezember 1992, S. 1008–1016, doi:10.1016/0006-291x(92)92304-g.
  • Mathias Hampf, Manfred Gossen: A protocol for combined Photinus and Renilla luciferase quantification compatible with protein assays. In: Anal Biochem., Band 356, Nr. 1, September 2006, S. 94–99, doi:10.1016/j.ab.2006.04.046 (PDF).
  • Ed Lim, Kshitij D. Modi, Jaebeom Kim: In vivo bioluminescent imaging of mammary tumors using IVIS spectrum. In: J Vis Exp., Band 26, April 2009, S. 1210, doi:10.3791/1210 mit Video (engl.).
  • Caitlin E. O'Connell-Rodwell, Mark A. Mackanos, Dmitrii M. Simanovski, Yu-An Cao, Michael H. Bachmann, H. Alan Schwettman, Christopher H. Contag: In vivo analysis of heat-shock-protein-70 induction following pulsed laser irradiation in a transgenic reporter mouse. In: J Biomed Opt., Band 13, Nr. 3, Mai 2008, S. 030501, doi:10.1117/1.2904665 (PDF).

europa.eu

echa.europa.eu

jbc.org

  • K. Gomi, N. Kajiyama: Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin. In: J Biol Chem., Band 276, Nr. 39, 2001, S. 36508–36513, doi:10.1074/jbc.M105528200 (PDF).
  • D. Morse, A. M. Pappenheimer Jr., J. W. Hastings: Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra. In: J Biol Chem., Band 264, Nr. 20, 1989, S. 11822–11826, (PDF).
  • A. J. Fisher, T. B. Thompson, J. B. Thoden, T. O. Baldwin, I. Rayment: The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. In: J Biol Chem., Band 271, Nr. 36, September 1996, S. 21956–21968, doi:10.1074/jbc.271.36.21956 (PDF).
  • A. Rodriguez, D. Riendeau, E. Meighen: 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., Band 258, Nr. 8, April 1983, S. 5233–5237, PMID 6833298 (PDF).

jove.com

  • Ed Lim, Kshitij D. Modi, Jaebeom Kim: In vivo bioluminescent imaging of mammary tumors using IVIS spectrum. In: J Vis Exp., Band 26, April 2009, S. 1210, doi:10.3791/1210 mit Video (engl.).

jst.go.jp

jstage.jst.go.jp

jstor.org

  • Thomas Eisner, Michael A. Goetz, David E. Hill, Scott R. Smedley, Jerrold Meinwald: Firefly »femmes fatales« acquire defensive steroids (lucibufagins) from their firefly prey. In: Proc Natl Acad Sci USA, Band 94, Nr. 18, September 1997, S. 9723–9728, (PDF).

mblwhoilibrary.org

darchive.mblwhoilibrary.org

  • Valentin N. Petushkov, Maxim A. Dubinnyi, Aleksandra S. Tsarkova, Natalja S. Rodionova, Mikhail S. Baranov, Vadim S. Kublitski, Osamu Shimomura, Ilia V. Yampolsky: 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., Band 53, Nr. 22, April 2014, S. 5566–5568, doi:10.1002/anie.201400529 (Manuskript).

nature.com

  • J. F. Head, S. Inouye, K. Teranishi, O. Shimomura: The crystal structure of the photoprotein aequorin at 2.3 Å resolution. In: Nature, Band 405, Nr. 6784, Mai 2000, S. 291–293, doi:10.1038/35012659 (PDF).

nih.gov

ncbi.nlm.nih.gov

  • P. J. Herring: Systematic distribution of bioluminescence in living organisms. In: J Biolumin Chemilumin., Band 1, Nr. 3, 1987, S. 147–163, PMID 3503524.
  • Eveline Brodl, Andreas Winkler, Peter Macheroux: Molecular Mechanisms of Bacterial Bioluminescence. In: Computational and Structural Biotechnology Journal. Band 16, 15. November 2018, S. 551–564, doi:10.1016/j.csbj.2018.11.003, PMID 30546856, PMC 6279958 (freier Volltext).
  • J. W. Hastings: Chemistries and colors of bioluminescent reactions: a review. In: Gene, Band 173, Nr. 1 special, 1996, S. 5–11, PMID 8707056, doi:10.1016/0378-1119(95)00676-1.
  • M. DeLuca, M. E. Dempsey: Mechanism of oxidation in firefly luminescence. In: Biochem Biophys Res Commun, Band 40, Nr. 1, 1970, S. 117–122, PMID 5456946, doi:10.1016/0006-291X(70)91054-5.
  • N. Lembert: Firefly luciferase can use L-luciferin to produce light. In: Biochem J., Band 317, Teil 1, Juli 1996, S. 273–277, doi:10.1042/bj3170273. PMC 1217473 (freier Volltext).
  • Yuichi Oba, Naoki Yoshida, Shusei Kanie, Makoto Ojika, Satoshi Inouye: 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, Band 8, Nr. 12, Dezember 2013, doi:10.1371/journal.pone.0084023; dazu gibt es eine Korrektur: PMC 3978032 (freier Volltext).
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