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Ribosome-inactivating proteins plant

Chaudhry, B., Muller-Uri, F., Cameron-Mills, V., Gough, S., Simpson, D., Skriver, K. and Mundy, J. (1994) The barley 60 kDa jasmonate-induced protein (JIP60) is a novel ribosome-inactivating protein. Plant J, 6, 815-824. [Pg.454]

Van Damme, E.J., Roy, S., Barre, A., Rouge, P, Van Leuven, F. and Penmans, W.J., The major elderberry (Sambucus nigra) fruit protein is a lectin derived from a truncated type 2 ribosome-inactivating protein. Plant J., 12, 1251-1260 (1997). [Pg.485]

Delayed-action cytotoxins that inhibits protein synthesis (ribosomal inactivating protein). They are obtained from the seed of the Jequirity beans plant (Abrus precatorius). Typically yellowish-white powders that are insoluble in distilled water but soluble in salt water. They are fairly heat stable. [Pg.478]

Cytotoxin that inhibits protein synthesis (ribosomal inactivating protein). It is obtained from the roots of Adenia digitata plant. [Pg.481]

Barbieri, L., Battelli, M. G., and Stiipe, F. (1993) Ribosome-inactivating proteins from plants. Biochim. Biophys. Acta 1154, 237-282. [Pg.144]

Toxin entry retrograde transport through the secretory pathway (Lord and Roberts, 1998) Ribosome-inactivating proteins a plant perspective (Nielsen and Boston, 2001)... [Pg.426]

Bass, H.W., Webster, C., OBrian, G.R., Roberts, J.K. and Boston, R.S. (1992) A maize ribosome-inactivating protein is controlled by the transcriptional activator Opaque-2. Plant Cell, 4, 225-234. [Pg.453]

Harms (kilyambiti plant), a type 2 ribosome-inactivating protein. Eur J Biochem, 271, 108-117. [Pg.454]

Chen, Y., Rouge, P., Van Damme, E.J.M., Penmans, W.J., Barre, A., Vandenbussche, F., Desmyter, S. and Hao, Q. (2001) Ribosome-inactivating proteins a family of plant proteins that do more than inactivate ribosomes. Crit Rev Plant Sci, 20, 395. [Pg.454]

Endo, Y., Tsurugi, K. and Lamberf, J.M. (1988a) The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes the RNA A-glycosidase activity of the proteins. Biochem Biophys Res Commun, 150, 1032-1036. [Pg.455]

Funatsu, G., Islam, M.R., Minami, Y., Sung-Sil, K. and Kimura, M. (1991) Conserved amino acid residues in ribosome-inactivating proteins from plants. Biochimie, 13, 1157-1161. [Pg.456]

Nielsen, K. and Boston, R.S. (2001) Ribosome-inactivating proteins a plant perspective. Amnu Rev Plant Physiol Plant Mol Biol, 52, 785-816. [Pg.462]

Hartley MR, Chaddock JA and Bonness MS (1996). The structure and function of ribosome inactivating proteins. Trends Plant Sci, 1, 254-259. [Pg.627]

Peumans WJ, Hao Q and van Damme EJM (2001). Ribosome-inactivating proteins from plants more than RNA /V-glycosidascs FASEB J, 15, 1493-1506. [Pg.629]

Stirpe F, Barbieri L, Battelli MG et al. (1992). Ribosome-inactivating proteins from plants present status and future prospects. Biotechnology,... [Pg.630]

Various plant toxins, mostly ribosome-inactivating proteins (RIPs), have been identified that bind to any mammalian cell surface expressing galactose units and are subsequently internalized by RME (67). Toxins such as nigrin b (68), a-sarcin (69), ricin and saporin (70), viscumin (71), and modeccin (72) are highly toxic upon oral administration (i.e., are rapidly internalized). The possibility exists, therefore, that modified and, most important, less toxic subunits of these compound can be used to facilitate the uptake of macro-molecular compounds or microparticulates. [Pg.263]

Nielsen, K., Boston, R. S. Ribosome-inactivating proteins a plant perspective. Annu. Rev. Plant Physiol. Plant Mol. Biol. 2001, 52, 785— 816... [Pg.492]

L., De Torre, C., Carbajales, M.L, Jimenez, P., De Benito, F.M., Munoz, R. Recent advances in the uses and applications of ribosome-inactivating proteins from plants. Cell. Mol. Biol. (Noisy-le-grand) 1996, 42, 461-471... [Pg.493]

Ricin toxin, found in the bean of the castor plant, Ricinis communis, is one of the most toxic and easily produced plant toxins. It is a lectin consisting of two polypeptide chains, the A-chain and the B-chain, linked by a disulfide bond. It is one of a group of dichain ribosome-inactivating proteins, which are specific for the depurination of a single adenosine in ribosomal ribonucleic acid (RNA).1 The active chain (ie, the A-chain) has the ability to modify catalytically the 28S subunit of... [Pg.632]

Barbieri L, Baltelli M, Stirpe F. Ribosomes-inactivating proteins from plants. Biochemica Biophysica Acta. 1993 1154 237-282. [Pg.639]

Nielsen K, Boston RS (2001) RIBOSOME-INACTIVATING PROTEINS A Plant Perspective. Annu Rev Plant Physiol Plant Mol Biol 52 785-816... [Pg.293]


See other pages where Ribosome-inactivating proteins plant is mentioned: [Pg.45]    [Pg.113]    [Pg.1844]    [Pg.135]    [Pg.752]    [Pg.753]    [Pg.130]    [Pg.51]    [Pg.488]    [Pg.341]    [Pg.540]    [Pg.558]    [Pg.263]    [Pg.426]    [Pg.457]    [Pg.12]    [Pg.613]    [Pg.496]    [Pg.931]    [Pg.564]    [Pg.332]    [Pg.332]    [Pg.282]   
See also in sourсe #XX -- [ Pg.351 ]




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