Ahmad baba, Sh., Jain, D., Abbas, N., & Ashraf, N. (2015). Overexpression of
Crocus Carotenoid cleavage dioxygenase,
CsCCD4b, in
Arabidopsis imparts tolerance dehydration, salt and oxidative stresses by modulating ROS machinery.
Journal of Plant Physiology, 189, 114- 125. https://doi.org/
10.1016/j.jplph.2015.11.001.
Ahrazem, O., Rubio-Moraga, A., Jimeno, M.L., & Gomez-Gomez, L. (2015). Structural characterization of highly glucosylation crocins and regulation of the biosynthesis during flower development in crosus. Frontiers in Plant Science, 6, 1-14. https://doi.org/10.3389/fpls.2015.00971.
Almagro Armenteros, J.J.,
Tsirigos, K.D.,
Sønderby, C.K.,
Petersen, T.N.,
Winther, O.,
Brunak, S.,
von Heijne, G., &
Nielsen, H. (2019). SignalP 5.0 improves signal peptide predictions using deep neural networks.
Nature Biotechnology, 37(4), 420-423. https://doi.org/10.1038/s41587-019-0036-z.
Artimo, P., Jonnalagedda, M., Arnold, K., Baratin, D., Csardi, G., de Castro, E., Duvaud, S., Flegel, V., Fortier, A., Gasteiger, E., Grosdidier, A., Hernandez, C., Ioannindis, V., Kuznetsov, D., Liechti, R., Moretti, S., Mostaguir, K., Redaschi, N., Rossier, G., Xenarios, I., & Stockinger, H. (2012). ExPASy: SIB bioinformatics resource portal. Nucleic Acids Research, 40(W1), W597-W603.
Bathaie, S.Z., Ashrafi, M., Bolhasani, A., Etemadi-kia, B., & Moosavi-movahedi, A.A. (2006). Purification of carotenoid and monoterpene aldehydes from Iranian saffron and investigation of their effect on the structure of DNA. Histone H1 and H1-DNA Complex. Iranian Journal of Medicinal and Aromatic Plants, 22(2), 85-97. (In Persian with English Summary).
Beiki, A., Keify, F., & Mozafari, J. (2011). Rapid genomic DNA isolation from corm of Crocus species for genetic diversity analysis. Journal of Medicinal Plants Research, 5, 4596-4600.
Bertoni, M., Kiefer, F., Biasini, M., Bordoli, L., & Schwede, T. (2017). Modeling protein quaternary structure of homo- and hetero-oligomers beyond binary interactions by homology. Scientific Reports, 7(1), 10480. https://doi.org/10.1038/s41598-017-09654-8.
Bienert, S., Waterhouse, A., de Beer, T.A.P., Tauriello, G., Studer, G., Bordoli, L., & Schwede, T. (2017). The SWISS-MODEL Repository - new features and functionality. Nucleic Acids Research, 45, D313-D319. https://doi.org/10.1093/nar/gkw1132.
Bouvier, F., Suire, C., Mutterer, J., & Camara, B. (2003). Oxidative remodeling of chromoplast carotenoids: identification of the carotenoid dioxygenase CsCCD and CsZCD genes involved in Crocus secondary metabolite biogenesis. Plant Cell, 15(1), 47-62. https://doi.org/10.1105/tpc.006536.
Brown, T.A. (2016). Gene Cloning and DNA Analysis: an Introduction. 7
th ed, Wiley Blackwell.
Combet, C., Blanchet, C., Geourjon, C., & Deleage, G. (2000). NPS@: Network Protein Sequence Analysis. Trends in Biochemical Science, 25(3), 147-150. https://doi.org/10.1016/S0968-0004 (99)01540-6.
Cote, F., Cormier, F., Dufresen, C., & Willemot, C. (2000). Properties of a glucosyltransferase involved in Crocin synthesis. Plant Science, 153, 55-63. https://doi.org/10.1016/S0168-9452(99)00248-4.
Cote, F., Cormier, F., Dufresen, C., & Willemot, C. (2001). A highly specific glucosyltransferase is involved in the synthesis of crocetin glucosylesters in Crocus sativus cells. Journal of plant physiology, 158, 553- 560. https://doi.org/10.1016/S0168-9452(99)00248-4.
Cunningham, FX., & Gantt, E. (1998). Genes and enzymes of carotenoid biosynthesis in plants. Annual Review of Plant Physiology and Molecular Biology, 49, 557-583. https://doi.org/10.1146/annurev.arplant.49.1.557.
Demurtas, O.S., Frusciante, S., Ferrante, P., Diretto, G., Hosseinpour Azad, N., Pietrella, M., e Aprea, G., Taddei, A.R., Romano, E., Mi, J., Al-Babili, S., Frigerio, L., & Giuliano, G. (2018). Candidate enzymes for saffron crocin biosynthesis are localized in multiple cellular compartments. Plant Physiology, 177(3), 990-1006. https://doi.org/10.1104/pp.17.01815.
Dong, T., & Hwang, I. (2014). Contribution of ABA UDP-glucosyltransferases in coordination of ABA biosynthesis and catabolism for ABA homeostasis. Plant Signal and Behavior, 9, e28888. https://doi.org/10.4161/psb.28888.
Dufresene, C., Cormier, F., & Dorion, S. (1997). In vitro formation of crocetin glucoyl esters by Crocus sativus callus extract. Planta Medica, 63(2), 150-153. https://doi.org/10.1055/s-2006-957633.
El-Gebali, S., Mistry, J., Bateman, A., Eddy, S.R., Luciani, A., Potter, S.C., Qureshi, M., Richardson, L.J., Salazar, J.A., Smart, A., Sonnhammer, E.L.L., Hirsh, L., Paladin, L., Piovesan, D., Tosatto, S.C.E., & Finn, R.D. (2019). The Pfam protein families database in 2019. Nucleic Acids Research, 48(D1), D427- D432. https://doi.org/10.1093/nar/gky995.
Frusciante, S., Diretto, G., Bruno, M., Ferrante, P., Pietrella, M., Prado-cabrero, A., Rubio-Morega, A., Beyer, P., Gomez-Gomez, L., Al-Babili, S., & Giuliano, G. (2014). Novel carotenoid cleavage dioxygenase catalyzes the first dedicated step in saffron crocin biosynthesis. Proceeding of the National Academy Sciences of the USA, 111(33), 12246- 12251. https://doi.org/10.1073/pnas.1404629111.
Gasteiger, E., Hoogland, Ch., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D., & Bairoch, A. (2005). Protein Identification and Analysis Tools on the ExPASy Server. The Proteomics Protocols Handbook. Humana Press, New York, 571-607. https://doi.org/ 10.1385/1-59259-584-7:531.
Gomez-Gomez, L., Parra-Vega, V., Rivas-sendra, A., Segui-Simmaro, J. M., Molina, R.V., Pallotti, C., Rubio-Moraga, A., Diretto, G., Prieto, A., & Ahrazem, O. (2017). Unraveling massive crocins transport and accumulation through proteome and microscopy tools during the development of saffron stigma. International Journal of Molecular Sciences, 18(1), E76. https://doi.org/10.3390/ijms18010076.
Hosseinpour Azad, N., Nematzadeh, G.A., Giuliano, G., Ranjbar, G.A., & Yamchi, A. (2017). Identification of Apo- Carotenoids' crocin and crocetin isomers in saffron crude extracts by HPLC coupled to atmospheric pressure chemical ionization and high resolution orbitrap mass spectrometry. Saffron Agronomy and Technology 4(4): 291-300. https://doi.org/10.22048/jsat.2016.38670.
Hosseinpour Azad, N. (2020). Identification and recombinant expression of crocin synthesis isoform gene in saffron stigma. Saffron Agronomy and Technology, 7(4): 481-490. (In Persian with English Summary). https://doi.org/10.22048/jsat.2019.133922.1302.
Hughes, J., & Hughes, M.A. (1994). Multiple secondary plant product UDP-glucose glucosyltransferase genes expressed in cassava (Manihot esculenta Crantz) cotyledons. DNA Sequencing and Mapping, 5(1), 41–49. https://doi.org/10.3109/10425179409039703.
Jones, PR., Moller, BL., & Hoj, PB. (1999). The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyses the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Journal of Biological Chemistry, 274(50), 35483–35491. https://doi.org/10.1074/jbc.274.50.35483.
Kite, J., & Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157(1), 105–32. https://doi.org/10.1016/0022-2836(82)90515-0.
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, EL. (2001). Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. Journal of Molecular Biology, 305(3): 567-580. https://doi.org/10.1006/jmbi.2000.4315.
Kumar, R., Sangwan, R.S., Mishra, S., Sabir, F., & Sangwan, N.S. (2012). In silico motif diversity analysis of the glycon preferentiality of plant secondary metabolic glycosyltransferases. Plant Omics, 5(3), 200-210.
Lee, H-I., & Raskin, I. (1999). Purification, cloning, and expression of a pathogen inducible UDP-glucose: salicylic acid glucosyltransferase from tobacco. Journal of Biological Chemistry, 274(51), 36637–36642. https://doi.org/10.1074/jbc.274.51.36637.
Lim, E-K., Baldauf, S., Li, Y., Elias, L., Worrall, D., Spencer, SP., Jackson, RG., Taguchi, G., Ross, J., & Bowles, DJ. 2003. Evolution of substrate recognition across a multigene family of glycosyltransferases in Arabidopsis. Glycobiology, 13(3), 139–145. https://doi.org/10.1093/glycob/cwg017.
Lomize, A.L., Pogozheva, I.D., Lomize, M.A., & Mosberg, H.I. (2007). The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Structural Biology, 7, 44. https://doi.org/10.1186/1472-6807-7-44.
Mai, N., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A., & Mizukami, H. (2012). UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides.
FEBS Letters, 586(7), 1055.
https://doi.org/10.1016/j.febslet.2012.03.003.
Maniatis, T., Fritsch, E., & Sambrook, F. (1995). Molecular cloning. A laboratory Manual. Cold Spring Harbor Laboratory, New York.
Moraga, A.R., Nohales, P.F, Perez, J.A., & Gomez-Gomez, L. (2004). Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta, 219, 955–66. https://doi.org/10.1007/s00425-004-1299-1.
Mozos, A.T. (2013). Isolation and characterization of enzymes involved in the biosynthesis of secondary metabolites with phytotherapeutic interest. PhD Thesis. Departamento de Ciencia y Tecnología Agroforestal y Genética, University of Castilla-La Mancha Facultad de Farmacia, Spain.
Mirhoseini, S.Z., Pezeshkian, Z., & Ghovvati, Sh. (2016). Phylogenetic and in silico analysis of interferon Beta-1b Protein. Journal of Mazandaran University of Medical Science, 26(145), 70-82. (In Persian with English Summary).
Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A., & Mizukami, H. (2012). UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett, 586(7), 1055–1061. https://doi.org/10.1016/j.febslet.2012.03.003.
Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., & Ferrin, T.E. (2004). UCSF Chimera-avisualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13), 1605-1612. https://doi.org/10.1002/jcc.20084.
Rubio, A., Rambla, J.L., Santaella, M., Gomez, D., Orzaez, D., Granell, A., & Gomez-Gpmez, L. (2008). Cytosolic and plastoglobule-targeted carotenoid dioxygenases from Crocus sativus are both involved in β-Ionone release. The Journal of Biological Chemistry, 283(36), 24816 –24825. https://doi.org/10.1074/jbc.M804000200.
Rubio Moraga, A., Nohales, P.F., Peres, J.A., & Gomez-Gomea, L. (2004). Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta, 219, 955- 966. https://doi.org/10.1007/s00425-004-1299-1.
Rubio Moraga, A., Rambla, J.L., Ahrazem, O., Granell, A., & Gomea-Gomez, L. (2009). Metabolite and target transcript analyses during Crocus sativus stigma development. Phytochemistry, 70, 1009- 1016. https://doi.org/10.1016/j.phytochem.2009.04.022.
Rubio-Moraga, A., Rambla, J.L., Fernández-de-Carmen, A., Trapero-Mozos, A., Ahrazem, O., Orzáez, D., Granell, A., & Gómez-Gómez, L. (2014). New target carotenoids for CCD4 enzymes are revealed with the characterization of a novel stress-induced carotenoid cleavage dioxygenase gene from Crocus sativus. Plant Molecular Biology, 86(4-5), 555-569. https://doi.org/10.1016/j.phytochem.2009.04.022.
Shao, H., He, X., Achnine, L., Blount, J.W., Dixon, R.A., & Wang, X. (2005). Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula. Plant Cell, 17, 3141–3154. https://doi.org/10.1105/tpc.105.035055.
Trapero, A., Ahrazem, O., Rubio-Moraga, A., Jimeno, M.L., Gomez, M.D., & Gomez-Gomez, L. (2012). Characterization of glucosyltransferase enzyme involved in the formation of kaempferol and quercetin sophorosides in Crocus sativus. Plant Physiology, 159(4), 1335- 1354. https://doi.org/10.1104/pp.112.198069.
Vogt, T., & Jones, P. (2000). Glycosyltransferases in plant natural product synthesis: characterization of a supergene family. Trends in Plant Science, 5(9), 380-386. https://doi.org/10.1016/S1360-1385(00)01720-9.
Wang, W., He, P., Zhao, D., Ye, L., & Dai, L. (2019). Construction of Escherichia coli cell factories for crocin biosynthesis. Microbial Cell Factories, 18:120. https://doi.org/10.1186/s12934-019-1166-1.
Wetterhorn, K.M., Newmister, S.A., Caniza, R.K., Busman, M., McCormick, S., Berthiller, F., Adam, G., & Rayment, I. (2016). Crystal structure of OS79 (Oso4go2oo66oo) from Oryza sativa: a UDP-glucosyltransferase involved in the detoxification of deoxynivalenol. Biochemistry, 55(44), 6175- 6186. https://doi.org/10.2210/pdb6BK3/pdb.
Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F.T., de Beer, T.A.P., Rempfer, C., Bordoli, L., Lepore, R., & Schwede, T. (2018). SWISS-MODEL: homology modeling of protein structures and complexes. Nucleic Acids Research, 46(W1): W296-W303. https://doi.org/10.1093/nar/gky427.
Xi, L., & Qian, Z. (2006). Pharmacological properties of crocetin and crocin (digentiobiosyl ester of crocetin) from saffron. Natural Product Communications, 1(1), 65-75.
Yousefi Javan, I., & Gharari, F. (2017). The structure of the protein and gene expression of PIC2 affecting blooming flowers (Crocus sativus L.). Saffron Agronomy and Technology, 5(1), 73-90. (In Persian with English Summary).
https://doi.org/10.22048/jsat.2017.63141.1200.