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2.8‐Å crystal structure of a nontoxic type‐II ribosome‐inactivating protein, ebulin l
Ebulin l is a type‐II ribosome‐inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type‐II RIP, ebulin is a disulfide‐linked heterodimer composed of a toxic A… Expand
Elderberry (Sambucus nigra) bark contains two structurally different Neu5Ac(alpha2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins.
- E. V. Van Damme, S. Roy, +7 authors W. Peumans
- Biology, Medicine
- European journal of biochemistry
- 1 May 1997
A second NeuAc(alpha2,6)Gal/GalNAc binding type 2 ribosome-inactivating protein (RIP), called SNAI' has been isolated from elderberry (Sambucus nigra) bark. SNAI' is a minor bark protein which… Expand
Sequence comparison and phylogenetic analysis by the Maximum Likelihood method of ribosome-inactivating proteins from angiosperms
- A. Di Maro, L. Citores, R. Russo, Rosario Iglesias, J. Ferreras
- Biology, Medicine
- Plant Molecular Biology
- 1 June 2014
Ribosome-inactivating proteins (RIPs) from angiosperms are rRNA N-glycosidases that have been proposed as defence proteins against virus and fungi. They have been classified as type 1 RIPs,… Expand
Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra : comparison with ricin
- M. Battelli, L. Citores, +4 authors T. Girbés
- Biology, Medicine
- Archives of Toxicology
- 1997
Abstract Nigrin b, a lectin isolated from the bark of elderberry (Sambucus nigra L.), has structure and enzymatic activity similar to that of ricin and other type 2 ribosome-inactivating proteins… Expand
Constitutive and inducible type 1 ribosome‐inactivating proteins (RIPs) in elderberry (Sambucus nigra L.)
- F. M. de Benito, R. Iglesias, +4 authors T. Girbés
- Chemistry, Medicine
- FEBS letters
- 22 May 1998
Two novel highly basic type 1 (single chain) ribosome‐inactivating proteins (RIPs) with N‐glycosidase activity have been found in elderberries (the fruits of Sambucus nigra L.). Mass spectrometry of… Expand
Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.
- T. Girbés, L. Citores, +7 authors M. Calonge
- Medicine, Biology
- The Journal of biological chemistry
- 25 August 1993
A novel type 2 ribosome-inactivating protein (RIP) that we named ebulin 1 has been isolated from leaves of Sambucus ebulus L. (Caprifoliaceae). In vitro ebulin 1 strongly inhibited protein synthesis… Expand
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
- Chemistry, Medicine
- Cancer letters
- 8 October 2002
Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 10(4) times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of… Expand
Isolation, cDNA cloning, biological properties, and carbohydrate binding specificity of sieboldin-b, a type II ribosome-inactivating protein from the bark of Japanese elderberry (Sambucus…
- M. Rojo, M. Yato, +5 authors N. Shibuya
- Biology, Medicine
- Archives of biochemistry and biophysics
- 15 April 1997
A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b. Sieboldin-b is a heterodimeric protein consisting… Expand
Isolation and characterization of a new non-toxic two-chain ribosome-inactivating protein from fruits of elder (Sambucus nigra L.)
- L. Citores, F. D. Benito, +6 authors T. Girbés
- Biology
- 1 October 1996
Sambucus (Caprifoliaceae) species contain nigrin b and ebulin I, which are two-chain ribosome-inactivating proteins (RIPs) belonging to a new type of RIPs which are non-toxic to mice and cultured… Expand
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
- Chemistry, Medicine
- The Biochemical journal
- 1 April 1996
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