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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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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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Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy
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 proteinExpand
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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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Purification, characterization and cytotoxicity assessment of Ageritin: The first ribotoxin from the basidiomycete mushroom Agrocybe aegerita.
BACKGROUND Several species belonging to Ascomycota phylum produce extracellular ribonucleases, known as ribotoxins, which exhibit RNase activity through the cleavage of a single phosphodiester bond,Expand
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Cusativin, a new cytidine-specific ribonuclease accumulated in seeds of Cucumis sativus L.
Dry seeds of Cucumis sativus L. were found to contain a heat-sensitive endoribonuclease of a novel type which we have named cusativin. It was purified to apparent electrophoretic homogeneity byExpand
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Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally related new homodimeric lectin in fruits of Sambucus ebulus L.
Abstract. Mature leaves of dwarf elder (Sambucus ebulus L.) contain the non-toxic type 2 ribosome-inactivating protein ebulin 1 (Girbés et al., 1993b, J. Biol. Chem. 268: 18195–18199). We have nowExpand
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Elicitor-dependent expression of the ribosome-inactivating protein beetin is developmentally regulated.
BE27 and BE29 are two forms of beetin, a virus-inducible type 1 ribosome-inactivating protein isolated from leaves of Beta vulgaris L. Western blot analysis revealed the presence of beetin forms inExpand
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Biological and antipathogenic activities of ribosome-inactivating proteins from Phytolacca dioica L.
BACKGROUND The species from the genus Phytolacca constitute one of the best sources of ribosome-inactivating proteins (RIPs) that have been used both in the therapy against virus and tumors and inExpand
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Biological activities of the antiviral protein BE27 from sugar beet (Beta vulgaris L.)
AbstractMain conclusionThe ribosome inactivating protein BE27 displays several biological activities in vitrothat could result in a broad action against several types of pathogens. Beetin 27 (BE27),Expand
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