Inactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase
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The phytochrome chromophore precursor, 3E-phytochromobilin, and the phycobiliprotein chromophore precursors, 3E-phycocyanobilin and 3E-phycoerythrobilin, are enzymatically converted to novel rubinoid products by purified rat liver biliverdin reductase. Phytochromobilin and phycocyanobilin are particularly good substrates for biliverdin reductase with Km and Vmax values very similar to those of the natural substrate, biliverdin IX alpha. Phycoerythrobilin is the least preferred of the three bilin substrates. 1H NMR spectroscopy of phycocyanorubin, the product of phycocyanobilin catalysis by biliverdin reductase, and comparison of absorption spectra of all three rubinoid products reveal that the C10 methine bridge is selectively reduced by biliverdin reductase without altering the A-ring ethylidene substituent. In vitro phytochrome assembly experiments demonstrate that the phytorubin products do not form photoactive adducts with recombinant apophytochrome. These results suggest that ectopic expression of biliverdin reductase in plants will prevent assembly of the functional photoreceptor and thus will potentially alter light-mediated plant growth and development.
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By suppressing adipocyte oxidative stress, spirulina may lead to systemic anti-inflammatory and insulin-sensitising effects.
“Thus, by suppressing adipocyte oxidative stress, spirulina may lead to systemic anti-inflammatory and insulin-sensitising effects.12–20”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
Phycocyanobilin is structurally similar to bilirubin and can inhibit NADPH oxidase.
“Phycocyanobilin is structurally similar to bilirubin and can inhibit NADPH oxidase.”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
The antioxidant activity of spirulina is directly proportional to the quantity of phycocyanin.
“The antioxidant activity of spirulina has been proven to be directly proportional to the quantity of phycocyanin (which contains phycocyanobilin).12–14 45”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Glazer, A. N. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31212-7 · Cited by 574 · see citing works
The Chemistry of Linear Oligopyrroles and Bile Pigments
Falk, H. (1989) · Monatshefte für Chemie. Supplementum · doi:10.1007/978-3-7091-6938-4 · Cited by 564 · see citing works
Isolation and Initial Characterization of Arabidopsis Mutants That Are Deficient in Phytochrome A
Nagatani, A., Reed, J. W., & Chory, J. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.1.269 · Cited by 463 · see citing works
PHYTOCHROME: A Light-activated Molecular Switch that Regulates Plant Gene Expression
Quail, P. H. (1991) · Annual Review of Genetics · doi:10.1146/annurev.ge.25.120191.002133 · Cited by 340 · see citing works
Purification and characterization of biliverdin reductase from rat liver.
Kutty, R. K., & Maines, M. D. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69552-9 · Cited by 302 · see citing works
Parks, B. M., & Quail, P. H. (1991) · The Plant Cell · doi:10.1105/tpc.3.11.1177 · Cited by 232 · see citing works
Chory, J., Peto, C. A., Ashbaugh, M., Saganich, R., Pratt, L. H., & Ausubel, F. M. (1989) · The Plant Cell · doi:10.1105/tpc.1.9.867 · Cited by 221 · see citing works
Beale, S. I. (1993) · Chemical Reviews · doi:10.1021/cr00018a008 · Cited by 165 · see citing works
Lagarias, J. C., Kelly, J. M., Cyr, K. L., & Smith, W. O. (1987) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1987.tb04729.x · Cited by 140 · see citing works
Biliverdin Reductase of Guinea Pig Liver
Singleton, J. W., & Laster, L. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97023-7 · Cited by 130 · see citing works
Cole, W. J., Chapman, D. J., & Siegelman, H. W. (1967) · Journal of the American Chemical Society · doi:10.1021/ja00990a055 · Cited by 125 · see citing works
Biosynthesis of the Plant Photoreceptor Phytochrome
Terry, M. J., Wahleithner, J. A., & Lagarias, J. C. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1473 · Cited by 121 · see citing works
Li, L., & Lagarias, J. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41762-0 · Cited by 107 · see citing works
Arciero, D. M., Bryant, D. A., & Glazer, A. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81365-0 · Cited by 106 · see citing works
Parks, B. M., & Quail, P. H. (1991) · The Plant Cell · doi:10.2307/3869225 · Cited by 106 · see citing works
McDonagh, A. F., & Palma, L. A. (1980) · Biochemical Journal · doi:10.1042/bj1890193 · Cited by 95 · see citing works
Parks, B. M., Shanklin, J., Koornneef, M., Kendrick, R. E., & Quail, P. H. (1989) · Plant Molecular Biology · doi:10.1007/bf00017582 · Cited by 91 · see citing works
WELLER, J. ‐., & Gossauer, A. (1980) · Chemische Berichte · doi:10.1002/cber.19801130439 · Cited by 87 · see citing works
Structure of phycoerythrobilin
Chapman, D. J., Cole, W. J., & Siegelman, H. W. (1967) · Journal of the American Chemical Society · doi:10.1021/ja00999a058 · Cited by 87 · see citing works
Phytochrome chromophore biosynthesis
Elich, T. D., McDonagh, A. F., Palma, L. A., & Lagarias, J. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31241-3 · Cited by 85 · see citing works
Chory, J., Peto, C. A., Ashbaugh, M., Saganich, R., Pratt, L. H., & Ausubel, F. M. (1989) · The Plant Cell · doi:10.2307/3868934 · Cited by 84 · see citing works
Arciero, D. M., Dallas, J., & Glazer, A. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81366-2 · Cited by 83 · see citing works
Fevery, J., Blanckaert, N. J. C., Leroy, P., Michiels, R., & Heirwegh, K. P. M. (1983) · Hepatology · doi:10.1002/hep.1840030207 · Cited by 77 · see citing works
Expression and assembly of spectrally active recombinant holophytochrome.
Wahleithner, J. A., Li, L. M., & Lagarias, J. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10387 · Cited by 76 · see citing works
Cornejo, J., Beale, S. I., Terry, M. J., & Lagarias, J. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42109-6 · Cited by 75 · see citing works
Formation of a Photoreversible Phycocyanobilin-Apophytochrome Adduct in vitro
Elich, T. D., & Lagarias, J. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51573-8 · Cited by 67 · see citing works
Beale, S. I., & Cornejo, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54576-2 · Cited by 64 · see citing works
Gossauer, A., & Hirsch, W. (1974) · Justus Liebig s Annalen der Chemie · doi:10.1002/jlac.197419740913 · Cited by 60 · see citing works
Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello.
Terry, M. J., & Lagarias, J. C. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54556-7 · Cited by 59 · see citing works
Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis
Huang, T., Trakshel, G. M., & Maines, M. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83119-2 · Cited by 56 · see citing works
Fakhrai, H., & Maines, M. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50627-5 · Cited by 56 · see citing works
In vitro attachment of bilins to apophycocyanin. III. Properties of the phycoerythrobilin adduct.
Arciero, D. M., Dallas, J., & Glazer, A. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81367-4 · Cited by 48 · see citing works
The preparation and characterization of bile pigments
Stoll, M. S., & GRAY, C. H. (1977) · Biochemical Journal · doi:10.1042/bj1630059 · Cited by 47 · see citing works
Biliverdin reductase: substrate specificity and kinetics
Frydman, R. B., Tomaro, M. L., Rosenfeld, J., Awruch, J., Sambrotta, L., Valasinas, A. L., & Frydman, B. (1987) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(87)90197-x · Cited by 22 · see citing works
The specificity of biliverdin reductase
Awruch, J., Tomaro, M. L., Frydman, R. B., & Frydman, B. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90073-6 · Cited by 15 · see citing works
Maines, M. D. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09506-9 · Cited by 14 · see citing works
Huang, T., & Maines, M. D. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09954-7 · Cited by 13 · see citing works
Huang, T., Trakshel, G. M., & Maines, M. D. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90477-3 · Cited by 10 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Production of phycocyanin—a pigment with applications in biology, biotechnology, foods and medicine
Eriksen, N. T. (2008) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-008-1542-y · Cited by 714 · see citing works
C-Phycocyanin: A potent peroxyl radical scavenger in Vivo and in Vitro
Bhat, V. B., & Madyastha, K. M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3270 · Cited by 477 · see citing works
A Brief History of Phytochromes
Rockwell, N. C., & Lagarias, J. C. (2010) · ChemPhysChem · doi:10.1002/cphc.200900894 · Cited by 360 · see citing works
Selective inhibition of cyclooxygenase-2 by C-phycocyanin, a biliprotein from Spirulina platensis
Reddy, C. M., Bhat, V. B., Kiranmai, G., Reddy, M. N., Reddanna, P., & Madyastha, K. M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3725 · Cited by 310 · see citing works
Bhat, V. B., & Madyastha, K. M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5195 · Cited by 277 · see citing works
Wagner, J. R., Zhang, J., Brunzelle, J. S., Vierstra, R. D., & Forest, K. T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611824200 · Cited by 237 · see citing works
Zheng, J., Inoguchi, T., Sasaki, S., Maeda, Y., McCarty, M. F., Fujii, M., Ikeda, N., Kobayashi, K., Sonoda, N., & Takayanagi, R. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00648.2011 · Cited by 201 · see citing works
Diverse two-cysteine photocycles in phytochromes and cyanobacteriochromes
Rockwell, N. C., Martin, S. S., Feoktistova, K., & Lagarias, J. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107844108 · Cited by 201 · see citing works
Clinical Potential of <i>Spirulina</i> as a Source of Phycocyanobilin
McCarty, M. F. (2007) · Journal of Medicinal Food · doi:10.1089/jmf.2007.621 · Cited by 199 · see citing works
Koníčková, R., Vaňková, K., Vaníková, J., Vanova, K. H., Lucie Muchova, A., Subhanová, I., Zadinová, M., Zelenka, J., Dvořák, A., Kolář, M., et al. (2014) · Annals of Hepatology · doi:10.1016/s1665-2681(19)30891-9 · Cited by 180 · see citing works
McCarty, M. F. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.12.069 · Cited by 137 · see citing works
Targeting microglia-mediated neurotoxicity: the potential of NOX2 inhibitors
Surace, M. J., & Block, M. L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1015-4 · Cited by 131 · see citing works
Rockwell, N. C., Njuguna, S. L., Roberts, L., Castillo, E., Parson, V. L., Dwojak, S. M., Lagarias, J. C., & Spiller, S. C. (2008) · Biochemistry · doi:10.1021/bi800088t · Cited by 130 · see citing works
Ankele, E., Kindgren, P., Pesquet, E., & Strand, A. (2007) · The Plant Cell · doi:10.1105/tpc.106.048744 · Cited by 125 · see citing works
Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803
Lamparter, T., Esteban, B., & Hughes, J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02395.x · Cited by 115 · see citing works
Efficient synthesis of phycocyanobilin in mammalian cells for optogenetic control of cell signaling
Uda, Y., Goto, Y., Oda, S., Kohchi, T., Matsuda, M., & Aoki, K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707190114 · Cited by 109 · see citing works
Phycobilins and Phycobiliproteins Used in Food Industry and Medicine
Myśliwa‐Kurdziel, B., & Solymosi, K. (2016) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557516666160912180155 · Cited by 105 · see citing works
Identification and Characterization of a New Class of Bilin Lyase
Shen, G., Saunée, N. A., Williams, S. R., Gallo, E. F., Schluchter, W. M., & Bryant, D. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602563200 · Cited by 105 · see citing works
Galvão, R. M., Li, M., Kothadia, S. M., Haskel, J. D., Decker, P. V., Buskirk, E. K. V., & Chen, M. (2012) · Genes & Development · doi:10.1101/gad.193219.112 · Cited by 103 · see citing works
Clack, T., Shokry, A. M., Moffet, M., Liu, P., Faul, M., & Sharrock, R. (2009) · The Plant Cell · doi:10.1105/tpc.108.065227 · Cited by 102 · see citing works
Andel, F., Murphy, J. T., Haas, J., McDowell, M. T., van der Hoef, I., Lugtenburg, J., Lagarias, J. C., & Mathies, R. A. (2000) · Biochemistry · doi:10.1021/bi991688z · Cited by 100 · see citing works
Effects of spirulina on weight loss and blood lipids: A review
DiNicolantonio, J. J., Bhat, A. G., & OKeefe, J. (2020) · Open Heart · doi:10.1136/openhrt-2018-001003 · Cited by 98 · see citing works
Mechanistic Insight into the Photosensory Versatility of DXCF Cyanobacteriochromes
Rockwell, N. C., Martin, S. S., & Lagarias, J. C. (2012) · Biochemistry · doi:10.1021/bi300171s · Cited by 94 · see citing works
Characterization of Cyanobacterial Biliverdin Reductase
Schluchter, W. M., & Glazer, A. N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13562 · Cited by 93 · see citing works
C-Phycocyanin prevents cisplatin-induced nephrotoxicity through inhibition of oxidative stress
Fernández-Rojas, B., Medina‐Campos, O. N., Hernández‐Pando, R., Negrette-Guzmán, M., Huerta‐Yépez, S., & Pedraza‐Chaverrí, J. (2014) · Food & Function · doi:10.1039/c3fo60501a · Cited by 91 · see citing works
Function and distribution of bilinbiosynthesis enzymes in photosynthetic organisms
Dammeyer, T., & Frankenberg‐Dinkel, N. (2008) · Photochemical & Photobiological Sciences · doi:10.1039/b807209b · Cited by 91 · see citing works
Benedetti, S., Benvenuti, F., Scoglio, S., & Canestrari, F. (2010) · Journal of Medicinal Food · doi:10.1089/jmf.2008.0257 · Cited by 83 · see citing works
YABUTA, Y., FUJIMURA, H., KWAK, C. S., ENOMOTO, T., & WATANABE, F. (2010) · Food Science and Technology Research · doi:10.3136/fstr.16.347 · Cited by 82 · see citing works
Strand, Å. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.09.004 · Cited by 82 · see citing works
Biochemical Characterization of Arabidopsis Wild-Type and Mutant Phytochrome B Holoproteins
Elich, T. D., & Chory, J. (1997) · The Plant Cell · doi:10.1105/tpc.9.12.2271 · Cited by 79 · see citing works
Synthesis of phycocyanobilin in mammalian cells
Müller, K., Engesser, R., Timmer, J., Nagy, F., Zurbriggen, M. D., & Weber, W. (2013) · Chemical Communications · doi:10.1039/c3cc45065a · Cited by 74 · see citing works
Cervantes-Llanos, M., Lagumersindez-Denis, N., Marín-Prida, J., Pavón-Fuentes, N., Falcon-Cama, V., Piniella-Matamoros, B., Camacho-Rodríguez, H., Fernández-Massó, J. R., Valenzuela-Silva, C., Raíces-Cruz, I., et al. (2018) · Life Sciences · doi:10.1016/j.lfs.2017.12.032 · Cited by 73 · see citing works
Pentón-Rol, G., Marín-Prida, J., & McCarty, M. F. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210408123807 · Cited by 73 · see citing works
Thiol-Based Photocycle of the Blue and Teal Light-Sensing Cyanobacteriochrome Tlr1999
Enomoto, G., Hirose, Y., Narikawa, R., & Ikeuchi, M. (2012) · Biochemistry · doi:10.1021/bi300020u · Cited by 71 · see citing works
Biosynthesis and Biological Functions of Bilins
Frankenberg‐Dinkel, N., & Lagarias, J. C. (2003) · Elsevier eBooks · doi:10.1016/b978-0-08-092387-1.50013-8 · Cited by 70 · see citing works
Wu, S., McDowell, M. T., & Lagarias, J. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25700 · Cited by 70 · see citing works
Ameliorative action of cyanobacterial phycoerythrin on CCl4-induced toxicity in rats
Soni, B., Visavadiya, N. P., & Madamwar, D. (2008) · Toxicology · doi:10.1016/j.tox.2008.03.008 · Cited by 68 · see citing works
The Phytochrome-Deficient pcd1 Mutant of Pea Is Unable to Convert Heme to Biliverdin IX[alpha].
Weller, J. L., Terry, M. J., Rameau, C., Reid, J. B., & Kendrick, R. E. (1996) · The Plant Cell · doi:10.1105/tpc.8.1.55 · Cited by 68 · see citing works
Park, C., Kim, J.-I., Yang, S., Kang, J., Kang, J.-H., Shim, J.-Y., Chung, Y., Park, Y.-M., & Song, P. (2000) · Biochemistry · doi:10.1021/bi992831r · Cited by 66 · see citing works
Jensen, G. S., Drapeau, C., Lenninger, M. R., & Benson, K. F. (2016) · Journal of Medicinal Food · doi:10.1089/jmf.2015.0143 · Cited by 63 · see citing works
Traditional medical records as a source of clinical data in the outpatient setting.
Tang, P. C., Fafchamps, D., & Shortliffe, E. H. (1994) · PubMed Central · Cited by 63 · see citing works
Marín-Prida, J., Pavón-Fuentes, N., Llópiz-Arzuaga, A., Fernández-Massó, J. R., Delgado-Roche, L., Mendoza-Marí, Y., Santana, S. P., Cruz-Ramírez, A., Valenzuela-Silva, C., Nazábal-Gálvez, M., et al. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.05.021 · Cited by 61 · see citing works
(3Z)- and (3E)-Phytochromobilin Are Intermediates in the Biosynthesis of the Phytochrome Chromophore
Terry, M. J., McDowell, M. T., & Lagarias, J. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11111 · Cited by 57 · see citing works
Chromophore−Apoprotein Interactions in Synechocystis sp. PCC6803 Phytochrome Cph1
Park, C., Shim, J.-Y., Yang, S., Kang, J., Kim, J., Luka, Z., & Song, P. (2000) · Biochemistry · doi:10.1021/bi992916s · Cited by 55 · see citing works
McCarty, M. F., Assanga, S. B. I., Luján, L. M. L., O’Keefe, J. H., & DiNicolantonio, J. J. (2020) · Nutrients · doi:10.3390/nu13010047 · Cited by 54 · see citing works
McCarty, M. F., & Lerner, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103624 · Cited by 51 · see citing works
Continuous Fluorescence Assay of Phytochrome Assembly in Vitro
Li, L., Murphy, J. T., & Lagarias, J. C. (1995) · Biochemistry · doi:10.1021/bi00024a017 · Cited by 50 · see citing works
Kefayat, A., Ghahremani, F. H., Safavi, A., Hajiaghababa, A., & Moshtaghian, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-55605-w · Cited by 49 · see citing works
Antioxidant bilirubin works in multiple ways to reduce risk for obesity and its health complications
DiNicolantonio, J. J., McCarty, M. F., & O’Keefe, J. H. (2018) · Open Heart · doi:10.1136/openhrt-2018-000914 · Cited by 50 · see citing works
Lagarias, D. M., Crepeau, M., Maines, M. D., & Lagarias, J. C. (1997) · The Plant Cell · doi:10.1105/tpc.9.5.675 · Cited by 49 · see citing works
McCarty, M. F., Barroso-Aranda, J., & Contreras, F. (2009) · Medical Hypotheses · doi:10.1016/j.mehy.2008.09.061 · Cited by 47 · see citing works
Phycocyanin as a nature-inspired antidiabetic agent: A systematic review
Ziyaei, K., Abdi, F., Mokhtari, M., Daneshmehr, M. A., & Ataie, Z. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154964 · Cited by 46 · see citing works
Radibratović, M., Minic, S. L., Stanić-Vučinić, D., Nikolic, M. R., Milčić, M. K., & Veličković, T. Ć. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167973 · Cited by 46 · see citing works
Memije-Lazaro, I. N., Blas-Valdivia, V., Franco-Colín, M., & Cano-Europa, E. (2018) · Journal of Functional Foods · doi:10.1016/j.jff.2018.01.013 · Cited by 46 · see citing works
Petit, L., Vernès, L., & Cadoret, J. (2021) · Journal of Applied Phycology · doi:10.1007/s10811-021-02372-9 · Cited by 45 · see citing works
Perspective: Prospects for Nutraceutical Support of Intestinal Barrier Function
McCarty, M. F., & Lerner, A. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa139 · Cited by 44 · see citing works
Taniguchi, M., & Lindsey, J. S. (2023) · Journal of Photochemistry and Photobiology C Photochemistry Reviews · doi:10.1016/j.jphotochemrev.2023.100585 · Cited by 41 · see citing works
Improvement of Phycocyanobilin Synthesis for Genetically Encoded Phytochrome-Based Optogenetics
Uda, Y., Miura, H., Goto, Y., Yamamoto, K., Mii, Y., Kondo, Y., Takada, S., & Aoki, K. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00477 · Cited by 41 · see citing works
Algae as a Source of Phycocyanin and Other Industrially Important Pigments
Dasgupta, C. N. (2015) · Springer eBooks · doi:10.1007/978-3-319-22813-6_12 · Cited by 40 · see citing works
Purification and Characterization of Recombinant Affinity Peptide‐Tagged Oat Phytochrome A
Murphy, J. T., & Lagarias, J. C. (1997) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1997.tb01920.x · Cited by 40 · see citing works
Biosynthesis of Phycobiliproteins in Cyanobacteria
Schluchter, W. M., & Glazer, A. N. (1999) · Springer eBooks · doi:10.1007/978-1-4615-4827-0_10 · Cited by 39 · see citing works
McCarty, M. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073321 · Cited by 40 · see citing works
Zhao, K., Ran, Y., Li, M., Sun, Y.-N., Zhou, M., Storf, M., Kupka, M., Böhm, S., Bubenzer, C., & Scheer, H. (2004) · Biochemistry · doi:10.1021/bi0491548 · Cited by 35 · see citing works
Excited-State Processes in Phycocyanobilin Studied by Femtosecond Spectroscopy
Bischoff, M., Hermann, G., Rentsch, S. K., Strehlow, D., Winter, S., & Chosrowjan, H. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp992083f · Cited by 34 · see citing works
Shang, L., Rockwell, N. C., Martin, S. S., & Lagarias, J. C. (2010) · Biochemistry · doi:10.1021/bi100756x · Cited by 33 · see citing works
Karizi, S. R., Armanmehr, F., Azadi, H. G., Zahroodi, H. S., Ghalibaf, A. M., Bazzaz, B. S. F., Abbaspour, M., Boskabadi, S. J., Eslami, S., & Taherzadeh, Z. (2023) · Phytotherapy Research · doi:10.1002/ptr.7674 · Cited by 32 · see citing works
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Knipp, B., Müller, M., Metzler‐Nolte, N., Balaban, T. S., Braslavsky, S. E., & Schaffner, K. (1998) · Helvetica Chimica Acta · doi:10.1002/hlca.19980810509 · Cited by 30 · see citing works
Sakai, K., Kondo, Y., Fujioka, H., Kamiya, M., Aoki, K., & Goto, Y. (2021) · Journal of Cell Science · doi:10.1242/jcs.259315 · Cited by 28 · see citing works
El-Sayed, E.-S., Hikal, M., Abo El- Khair, B., El-Ghobashy, R., & El-Assar, A. (2018) · Arab Universities Journal of Agricultural Sciences · doi:10.21608/ajs.2018.28365 · Cited by 26 · see citing works
“It contains an open-chain tetrapyrrole chromophore known as phycocyanobilin, which is covalently attached to the apoprotein called (phycocyanopeptide) (Terry et al 1993).”
BackgroundMcCarty, M. F., DiNicolantonio, J. J., & Lerner, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042140 · Cited by 26 · see citing works
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Fushimi, K., & Narikawa, R. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-8763-4_10 · Cited by 22 · see citing works
Franklin, K. A., Linley, P. J., Montgomery, B. L., Lagarias, J. C., Thomas, B., Jackson, S. D., & Terry, M. J. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01840.x · Cited by 20 · see citing works
Liu, J. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i18.5465 · Cited by 20 · see citing works
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Ito, T., Chen, D., Chang, C. T., Kenmochi, T., Saito, T., Suzuki, S., & Takemoto, J. Y. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00050 · Cited by 19 · see citing works
McCarty, M. F., DiNicolantonio, J. J., & Lerner, A. (2021) · Journal of Asthma and Allergy · doi:10.2147/jaa.s307549 · Cited by 18 · see citing works
Takao, H., Hirabayashi, K., Nishigaya, Y., Kouriki, H., Nakaniwa, T., HAGIWARA, Y., Harada, J., Sato, H., Yamazaki, T., Sakakibara, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms14397 · Cited by 16 · see citing works
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McCarty, M. F. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.08.041 · Cited by 15 · see citing works
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Oda, S., Sato-Ebine, E., Nakamura, A., Kimura, K. D., & Aoki, K. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.2c00461 · Cited by 11 · see citing works
Zhang, K., Yu, M., Li, W., Shan, X., Wang, N., & Feng, H. (2020) · BMC Plant Biology · doi:10.1186/s12870-020-2271-3 · Cited by 11 · see citing works
DiNicolantonio, J., McCarty, M., Barroso-Aranda, J., Assanga, S., Luján, L. M. L., O, & Keefe, J. H. (2021) · Open Heart · doi:10.1136/openhrt-2021-001663 · Cited by 11 · see citing works
Madji, S., Antih, J., Tabib, M., Silvestre, C., Ghennai, A., Warnery, A., Vaillant, F. E., Bichon, F., Echalier, A., & Poucheret, P. (2025) · Analytica—A Journal of Analytical Chemistry and Chemical Analysis · doi:10.3390/analytica6040044 · Cited by 12 · see citing works
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Jayanti, S. D., Vı́tek, L., Verde, C. D., Llido, J. P., Sukowati, C. H. C., Tiribelli, C., & Gazzin, S. (2024) · Biomolecules · doi:10.3390/biom14010063 · Cited by 9 · see citing works
Rashed, S. A., Hammad, S., Eldakak, M., Khalil, I. A. H., & Osman, A. I. (2022) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2022.08.038 · Cited by 9 · see citing works
Debrah, S. K., Anankware, J. P., Asomah, S., & Ofori, D. O. (2022) · Journal of Insects as Food and Feed · doi:10.3920/jiff2021.0219 · Cited by 8 · see citing works
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Stefanutti, D., Serva, L., Berlanda, M., Bonsembiante, F., Gabai, G., Franceschinis, E., Cavazzoni, M., Morelli, G., & Ricci, R. (2024) · Scientific Reports · doi:10.1038/s41598-024-80843-y · Cited by 5 · see citing works
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McCarty, M. F., & DiNicolantonio, J. J. (2021) · Healthcare · doi:10.3390/healthcare10010003 · Cited by 3 · see citing works
- Authors
- Terry, M. J., Maines, M. D., & Lagarias, J. C.
- Affiliations
- University of Rochester Medicine (US)
- University of California, Davis (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-12
- Volume
- 268
- Issue
- 35
- Pages
- 26099-26106
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1553174726
- Cited by
- 118
- References
- 39
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 4 · 2021: 10 · 2020: 7 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 3 · 2012: 5
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion, cc-by)
- Funders
- National Institute of Environmental Health Sciences (ES04066, R01ES004066)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Health Sciences › Medicine › Pediatrics, Perinatology and Child Health › Neonatal Health and Biochemistry
- Keywords
- biliverdin reductase, phytochrome, phycobiliproteins, phytochromobilin, phycocyanobilin, phycoerythrobilin, rat liver
- MeSH terms
- Animals, Apoproteins, Biliverdine, Catalysis, Liver, Oxidoreductases, Phycocyanin, Phycoerythrin, Phytochrome, Plants, Pyrroles, Substrate Specificity, Oxidoreductases Acting on CH-CH Group Donors, Tetrapyrroles, Rats, Phycobilins, Eukaryota
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