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Unveiling key genetic loci and candidate genes for brown spot disease resistance in rice based on QTL analysis. [PDF]
Zhao DD +9 more
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Improving Cytotoxicity of Saporin with Saponin SO1406 Isolated from the Roots of Saponaria Officinalis. [PDF]
Lim-Paik C +4 more
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Ricin and Abrin in Biosecurity: Detection Technologies and Strategic Responses. [PDF]
Zajaczkowski W +8 more
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Synthetic overlapping genes stabilize genetic systems. [PDF]
Leonard SP +7 more
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Detection and Characterization of the Eukaryotic Vacant Ribosome. [PDF]
Delaney CE, Becskei A.
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Ribosome specialization by cancer-associated ribosomal protein mutations: progress made and open questions. [PDF]
Caruso M, De Keersmaecker K.
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The Structure of Ribosome Inactivating Proteins
Mini-Reviews in Medicinal Chemistry, 2004Ribosome Inactivating Proteins, RIPs, depurinate an invariant adenine from the 28S rRNA of eukaryotic ribosomes; they have evolved to near enzymatic perfection for this task. The N-glycosidase fold is conserved in plant and bacterial enzymes. RIPs can form complexes with cell surface recognition proteins that dramatically increase the cytotoxicity of ...
Jon D, Robertus, Arthur F, Monzingo
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Genetics of Ribosome-Inactivating Proteins
Mini-Reviews in Medicinal Chemistry, 2004Ribosome-inactivating proteins (RIPs) are a heterogeneous group of enzymes found mainly in plants and a few bacteria that possess N-glycosidase activity on ribosomes and a related polynucleotide adenosine glycosidase activity on naked nucleic acids. They encompass single enzymatic chains, heterodimeric toxic lectins and related agglutinins.
Martin R, Hartley, J Michael, Lord
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A Nonradioactive Assay for Ribosome-Inactivating Proteins
Analytical Biochemistry, 1996A sensitive nonradioactive method to determine the activity of ribosome-inactivating proteins (RIPs) based on a combined transcription/translation in vitro assay was established. Using this assay we investigated the RIP activities of the heterodimeric toxic plant lectins ricin and mistletoe lectin I (ML-I).
M, Langer +4 more
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