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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 AExpand
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Elderberry (Sambucus nigra) bark contains two structurally different Neu5Ac(alpha2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins.
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 whichExpand
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Sequence comparison and phylogenetic analysis by the Maximum Likelihood method of ribosome-inactivating proteins from angiosperms
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
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Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra : comparison with ricin
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 proteinsExpand
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Constitutive and inducible type 1 ribosome‐inactivating proteins (RIPs) in elderberry (Sambucus nigra L.)
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 ofExpand
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Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.
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 synthesisExpand
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Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin l.
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 ofExpand
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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
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 consistingExpand
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Isolation and characterization of a new non-toxic two-chain ribosome-inactivating protein from fruits of elder (Sambucus nigra L.)
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 culturedExpand
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