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Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria.
- T. Girbés, J. Ferreras, F. Arias, F. Stirpe
- BiologyMini reviews in medicinal chemistry
- 31 May 2004
The current belief is that they could play significant roles in the antipathogenic (viruses and fungi), stress and senescence responses, and their use as toxic effectors in the construction of immunotoxins and conjugates for target therapy.
Probiotic Lactic Acid Bacteria: A Review
- E. J. Quinto, P. Jiménez, I. Caro, J. Tejero, J. Mateo, T. Girbés
- Medicine
- 22 September 2014
The recent data in regard to the role of probiotic LAB in the preservation of foods, in the immunomodulation in the gastrointestinal tract, and in its health benefits are reviewed.
2.8‐Å crystal structure of a nontoxic type‐II ribosome‐inactivating protein, ebulin l
Ebulin l is shown to bind an A‐chain substrate analogue, pteroic acid, in the same manner as ricin, and is considered a nontoxic type‐II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type‐ II RIP like ricin.
Enzymatic activity of toxic and non‐toxic type 2 ribosome‐inactivating proteins
- L. Barbieri, M. Ciani, F. Stirpe
- Biology, ChemistryFEBS letters
- 9 April 2004
A non-toxic two-chain ribosome-inactivating protein co-exists with a structure-related monomeric lectin (SNA III) in elder (Sambucus nigra) fruits.
- T. Girbés, L. Citores, F. M. de Benito, R. Inglesias, J. Ferreras
- BiologyThe Biochemical journal
- 1 April 1996
It is found that the putative dimeric aggregate of SNA III is in fact a protein translation inhibitor which binds -galactose residues like SNAIII and strongly inhibits protein synthesis in rabbit reticulocyte lysates (IC &! 1.8 ng}ml).
Non-toxic type 2 ribosome-inactivating proteins (RIPs) from Sambucus: occurrence, cellular and molecular activities and potential uses.
- T. Girbés, J. Ferreras, M. Gayoso
- Biology, ChemistryCellular and molecular biology
- 1 June 2003
Conjugation of nigrin b or ebulin 1 to either transferrin or monoclonal antibodies provided highly active conjugates targeting cancer, and these non-toxic type 2 RIPs are promising tools for cancer therapy.
Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.
- T. Girbés, L. Citores, M. Calonge
- Biology, ChemistryThe Journal of biological chemistry
- 25 August 1993
Distribution and properties of major ribosome-inactivating proteins (28 S rRNA N-glycosidases) of the plant Saponaria officinalis L. (Caryophyllaceae).
- J. Ferreras, L. Barbieri, F. Stirpe
- Biology, ChemistryBiochimica et biophysica acta
- 19 October 1993
Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin l.
- L. Citores, J. Ferreras, R. Muñoz, J. Benítez, P. Jiménez, T. Girbés
- Biology, ChemistryCancer letters
- 8 October 2002
Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy
- J. Ferreras, L. Citores, Rosario Iglesias, P. Jiménez, T. Girbés
- BiologyToxins
- 29 April 2011
The type 2 ribosome-inactivating proteins (RIPs) isolated from some species belonging to the Sambucus genus, have the characteristic that although being even more active than ricin inhibiting protein…
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