• Reference :1

    Ajji, P.K., Walder, K., Puri, M., 2016. Functional analysis of a type-I ribosome inactivating protein Balsamin from Momordica balsamina with anti-microbial and DNase Activity. Plant Foods Human Nutrition 71, 265–271.

    Ali, N., Mohammed, S., Kenoth, R., Swamy, M.J., 2004. Purification, physicochemical characterization, saccharide specificity, and chemical modification of a Gal/GalNAc specific lectin from the seeds of Trichosanthes dioica. Arch Biochem Biophysics 432, 212–221.

    Asano, K., Svensson, B., Poulsen, F.M., 1984. Isolation and characterization of inhibitors of animal cell-free protein synthesis from barley seeds. Carlsberg Research Communications 49, 619–626.

    Barbieri, L., Battelli, M.G., Stirpe, F., 1993. Ribosome-inactivating proteins from plants. Biochim. Biophys. Acta 1154, 237–282.

    Bass, H.W., Webster, C., OBrian, G.R, Roberts, J.K.M., Boston, A., 1992. Maize ribosome-inactivating protein is controlled by the transcriptional activator Opaque- 2. Plant Cell4, 225–34.

    Cassady, J.M., Douros, J.D., 1980. Anticancer agents Based on Natural Product Models. (Academic press, New York), 134–142.

    Chaudhry, B., Mueller, U.F., Cameron-Mills, V., Gough, S., Simpson, D., Skriver, K., Mundy, J., 1994. The barley 60 kDajasmonate-induced protein (JIP60) is a novel ribosome-inactivating protein. The Plant Journal 6, 815–824.

    Freshney, R.I., 2010.  Culture of animal cells. a manual of basic technique and specialized applications. 6th ed., Wiley, New Jersey, 373.

    Gordon, M.C., David, J., 2005. Plants as a source of anticancer agents. Journal of Ethnopharmacology 100, 72–79.

    Griffiths, G.D, Leek, M.D., Gee, D.J., 1987. The toxic plant proteins ricin and abrin induce apoptotic changes in mammalian lymphoid tissues and intestine. The Journal of Pathology 151, 221–222.

    Husain, J., Tickle, I.J., Wood, S.P., 1994. Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia. FEBS Letters 342, 154–58.

    Ignacimuthu, S., Ayyanar, M., Sivaraman, S.K., 2006. Ethnobotanical investigations among tribes in Madurai district of Tamil Nadu (India). Journal of Ethnobiology and Ethnomedicine 2, 25.

    Irvin, J.D., 1975. Purification and partial characterization of the antiviral protein from Phytolacca americana which inhibits eukaryotic protein synthesis. Archives of Biochemistry and Biophysics 169, 522–528.

    Kokorina, A., Weiseb, C., Samaa, S., Weng, A., 2019. A new type 1 ribosome-inactivating protein from the seeds of Gypsophila elegans  M.Bieb. Photochemistry 157, 121–127.

    Li, X.D., Chen, W.F., Liu, W.Y., Wang, G.H., 1997. Large-scale preparation of two new ribosome-inactivating proteins—Cinnamomin and camphorin from the seeds of Cinnamomum camphora.Protein Expression and Purification 10, 27–31.

    Mlsna, D., Monzingo, A.F., Katzin, B.J.,  1993. Ernst S and Robertus J D, Structure of recombinant ricin A chain at 2.3 A. ProteinScience  2, 429–435.

    Monzingo, A.F., Robertus, J.D, 1992. Xray analysis of substrate analogs in the ricin A-chain active site. Journal of Molecular Biology 227, 1136–1145.

    Mundy, J., Leah, R., Boston, R., Endo, Y., Stirpe, F., 1994. Genes encoding ribosome-inactivating proteins. Plant Molecular Biology Reports 12, S60–62.

    Oliver, F.J., de la Rubia, G., Rolli, V., Ruiz-Ruiz, M.C., de Murcia, G.,Menissier-de Murcia, J., 1998. Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavablemutant. Journal of Biological Chemistry  273, 33533–33539.

    Olsnes, S., Pihl, A., 1973. Isolation and properties of abrin: a toxic protein inhibiting protein synthesis, Evidence for different biological functions of its two constituent-peptide chains. European Journal of Biochemistry 35, 179–185.

    Reinbothe, S., Reinbothe, C., Lehmann, J., Becker, W., Apel, K., Parthier, B., 1994. JIP60 a methyl jasmonate-induced ribosome-inactivating protein involved in plant stress reactions. Proceedings of the National Academy of Sciences of the United States of America 91, 7012–7016.

    Sivandzade, F., Bhalerao, A., Cucullo, L., 2019. Analysis of the mitochondrial membrane potential using the cationic JC-1 dye as a sensitive fluorescent probe. Bio Protocol 9, e3128

    Stirpe, F., Gasperi-Campani, A., Barbieri, L., Lorenzoni, E., Montanaro, L., et al.,  1978. Inhibition of protein synthesis by modeccin, the toxin of Modecca digitate. FEBS Letters 85, 65–67.

    Tomlinson, T.R., Akerele, O., 1998. Medicinal plants: their role in health and biodiversity. University of Pennsylvania Press, Philadelphia 11–41.

    Walsh, T.A., Morgan, A.E., Hey, T.D., 1991. Characterization and molecular cloning of a proenzyme form of a ribosome inactivating protein from maize: novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment. The Journal of Biological Chemistry 266, 23422–23427.

People also read

Innovative Technology

High Intensity Transplanting Increases Yield in Indigenous Aromatic Rice, Tulaipanji- a Case Study

Dhiman Sen and N. C. Sarkar

Aromatic rice, tulaipanji, high intensity, transplanting, yield

Published Online : 07 Jun 2010