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Ribosome-inactivating proteins

Toxicon, 1997
Abstract 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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The Structure of Ribosome Inactivating Proteins

Mini-Reviews in Medicinal Chemistry, 2004
Ribosome 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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Ribosome-inactivating proteins: progress and problems

Cellular and Molecular Life Sciences, 2006
Ribosome-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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Ribosome-inactivating proteins in plant biology

Planta, 2004
Ribosome-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 from an evolutionary perspective

Toxicon, 2017
Ribosome Inactivating Proteins (RIPs) are rRNA N-glycosidases that inhibit protein synthesis through the elimination of a single adenine residue from 28S rRNA. Many of these toxins have been characterized in depth from a biochemical and molecular point of view.
Walter Jesús, Lapadula   +1 more
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A Nonradioactive Assay for Ribosome-Inactivating Proteins

Analytical Biochemistry, 1996
A 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 and Apoptosis

2010
Ribosome inactivating proteins (RIPs) are RNA N-glycosidases which potently inhibit translation by inactivating ribosomes. RIPs have also been shown to possess the ability to induce apoptosis. A number of RIPs from different sources have been used to study the mechanism of apoptosis induction.
Deepa Sikriwal, Janendra K. Batra
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Occupational sensitization to ribosome‐inactivating proteins in researchers

Clinical & Experimental Allergy, 2005
SummaryBackground 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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Ribosome-Inactivating Proteins in Cereals

2010
Plants constitutively accumulate proteins that are either toxic or inhibitory against pathogens, including ribosome-inactivating proteins (RIPs) and N-glycosidases that depurinate the universally conserved α-sarcin loop of large rRNAs. Cereal RIPs share a high similarity with all the other RIPs; however, they retain characteristic features forming a ...
Carlotta Balconi   +2 more
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Isolation and Purification of Ribosome-Inactivating Proteins

2005
Ribosome-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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