Results 231 to 240 of about 25,229 (271)
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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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Ribosome-inactivating proteins
Toxicon, 1997Abstract Ribosome-inactivating proteins (RIPs, review by Barbieri et a/. 1993) are a class of proteins present in various tissues of several plants which inactivate mammalian ribosomes and, with less activity and to variable extent, plant, fungal, and bacterial ribosomes. They are enzymes, N-glycosidases, which release adenine from rRNA.
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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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Ribosome-inactivating proteins in plant biology
Planta, 2004Ribosome-inactivating proteins (RIPs) are a group of cytotoxic Af-glycosidases that specifically cleave nucleo tide N-C glycosidic bonds. RIPs have been classified into three types: type I is composed of a single polypeptide chain, whereas type II is a heterodimer consisting of an A chain, functionally equivalent to a type I, which is attached to a ...
Sang-Wook, Park +3 more
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Ribosome-inactivating proteins: progress and problems
Cellular and Molecular Life Sciences, 2006Ribosome-inactivating proteins (RIPs), mostly from plants, are enzymes which depurinate rRNA, thus inhibiting protein synthesis. They also depurinate other polynucleotide substrates. The biological activity of RIPs is not completely clarified, and sometimes independent of the inhibition of protein synthesis. There are differences in the cytotoxicity of
STIRPE, FIORENZO, BATTELLI, MARIA GIULIA
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Occupational sensitization to ribosome‐inactivating proteins in researchers
Clinical & Experimental Allergy, 2005SummaryBackground Ribosome‐inactivating proteins (RIPs) are expressed in many plants. Because of their anti‐infectious and anti‐proliferative effects, intensive research is going on for applying these toxins in therapy against viral infections or malignancies.
K, Szalai +9 more
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Isolation and Purification of Ribosome-Inactivating Proteins
2005Ribosome-inactivating proteins (RIPs) are cytotoxic N-glycosidases identified in plants, fungi, and bacteria. RIPs inhibit protein synthesis by virtue of their enzymatic activity, selectively cleaving a specific adenine residue from a highly conserved, surface-exposed, stem-loop (S/R loop) structure in the 28S rRNA of ribosomes.
Sang-Wook, Park +3 more
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Ribosome-Inactivating Proteins: A Family of Plant Proteins That Do More Than Inactivate Ribosomes
Critical Reviews in Plant Sciences, 2001ABSTRACT Many plants contain proteins that are commonly designated as ribosome-inactivating proteins (RIPs). Based on the structure of the genes and the mature proteins a novel system is proposed to unambiguously classify all RIPs in type-1, type-2, and type-3 RIPs. In addition, the concept of one- and two-chain type-1 RIPs is introduced.
Els J. M. Van Damme +7 more
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The Genetics and Properties of Cereal Ribosome-Inactivating Proteins
Mini-Reviews in Medicinal Chemistry, 2004Plants contain proteins that are capable of inactivating ribosomes, commonly referred to as Ribosome Inactivating Proteins (RIPs). These particular plant proteins have received attention in biological and biomedical research because of their unique biological activities towards animals and human cells as cell-killing agents.
Mario, Motto, Elisabetta, Lupotto
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Comparison of ribosome-inactivating proteins in the induction of apoptosis
Toxicology Letters, 1997The aim of this study was to evaluate the ability of verocytotoxin-1 (VT1), VT1 B chain alone, ricin and a hybrid toxin (RASTA2) consisting of ricin A chain linked to VT1 B chain to inhibit protein synthesis and to induce apoptosis. The lethal effects of the toxins were compared using vero cells (originating from green African monkey kidney tissue). As
J M, Williams +5 more
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