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Gene Review

cRIP30  -  ribosome-inactivating protein

Hordeum vulgare

 
 
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Disease relevance of cRIP30

  • An antimelanoma-barley ribosome inactivating protein conjugate is cytotoxic to melanoma cells in vitro [1].
 

High impact information on cRIP30

  • JIP60, a methyl jasmonate-induced ribosome-inactivating protein involved in plant stress reactions [2].
  • One of the recently identified jasmonate-induced proteins, designated JIP60, in barley is a ribosome-inactivating protein that cleaves polysomes of both animal and plant origin into their ribosomal subunits [2].
  • Upon jasmonate treatment barley leaf segments express a putative ribosome-inactivating protein (JIP60) [3].
  • Expression of the ribosome-inactivating protein JIP60 from barely in transgenic tobacco leads to an abnormal phenotype and alterations on the level of translation [4].
  • Cysteine analogs of recombinant barley ribosome inactivating protein form antibody conjugates with enhanced stability and potency in vitro [5].
 

Biological context of cRIP30

 

Associations of cRIP30 with chemical compounds

 

Analytical, diagnostic and therapeutic context of cRIP30

References

  1. An antimelanoma-barley ribosome inactivating protein conjugate is cytotoxic to melanoma cells in vitro. Ovadia, M., Hager, C.C., Oeltmann, T.N. Anticancer Res. (1990) [Pubmed]
  2. JIP60, a methyl jasmonate-induced ribosome-inactivating protein involved in plant stress reactions. Reinbothe, S., Reinbothe, C., Lehmann, J., Becker, W., Apel, K., Parthier, B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. The jasmonate-induced 60 kDa protein of barley exhibits N-glycosidase activity in vivo. Dunaeva, M., Goebel, C., Wasternack, C., Parthier, B., Goerschen, E. FEBS Lett. (1999) [Pubmed]
  4. Expression of the ribosome-inactivating protein JIP60 from barely in transgenic tobacco leads to an abnormal phenotype and alterations on the level of translation. Görschen, E., Dunaeva, M., Hause, B., Reeh, I., Wasternack, C., Parthier, B. Planta (1997) [Pubmed]
  5. Cysteine analogs of recombinant barley ribosome inactivating protein form antibody conjugates with enhanced stability and potency in vitro. Bernhard, S.L., Better, M., Fishwild, D.M., Lane, J.A., Orme, A.E., Garrison, D.A., Birr, C.A., Lei, S.P., Carroll, S.F. Bioconjug. Chem. (1994) [Pubmed]
  6. Nucleotide sequence of a genomic gene encoding tritin, a ribosome-inactivating protein from Triticum aestivum. Habuka, N., Kataoka, J., Miyano, M., Tsuge, H., Ago, H., Noma, M. Plant Mol. Biol. (1993) [Pubmed]
  7. Crystallization and preliminary X-ray crystallographic study of ribosome-inactivating protein from barley seeds. Song, H.K., Hwang, K.Y., Kim, K.K., Suh, S.W. Acta Crystallogr. D Biol. Crystallogr. (1994) [Pubmed]
 
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