Results 181 to 190 of about 1,593,797 (211)

Genetics of Ribosome-Inactivating Proteins

Mini-Reviews in Medicinal Chemistry, 2004
Ribosome-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 up to date

FEBS Letters, 1986
Ribosome‐inactivating proteins (RIPs) from plants inactivate eukaryotic ribosomes, as far as studied by rendering their 60 S subunit unable to bind elongation factor 2. These proteins seem widely distributed and possibly ubiquitous in plants. They are either type 1, those consisting of a single polypeptide chain, or type 2 (ricin and related toxins ...
Stirpe, Fiorenzo, Barbieri, Luigi
exaly   +3 more sources

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, Ramarao, Vepachedu, Neelam, Sharma, Jorge M, Vivanco   +3 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, M, Rothe, J, Eck, B, Möckel, H, Zinke   +4 more
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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, I, Schöll, E, Förster-Waldl, L, Polito, A, Bolognesi, E, Untersmayr, A B, Riemer, G, Boltz-Nitulescu, F, Stirpe, E, Jensen-Jarolim   +9 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, Balakrishnan, Prithiviraj, Ramarao, Vepachedu, Jorge M, Vivanco   +3 more
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The Genetics and Properties of Cereal Ribosome-Inactivating Proteins

Mini-Reviews in Medicinal Chemistry, 2004
Plants 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, 1997
The 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, N, Lea, J M, Lord, L M, Roberts, D V, Milford, C M, Taylor   +5 more
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On the Distribution of Ribosome-Inactivating Proteins amongst Plants

Journal of Natural Products, 1985
The extracts from various parts (mostly seeds) of 56 different plants were examined for inhibition of protein synthesis by a rabbit reticulocyte lysate. Most extracts inhibited protein synthesis with an ID50 (concentration giving 50% inhibition) of 100 micrograms extract protein per ml, or less.
A, Gasperi-Campani, L, Barbieri, M G, Battelli, F, Stirpe   +3 more
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Ribosome-inactivating proteins in edible plants and purification and characterization of a new ribosome-inactivating protein from Cucurbita moschata

Biochimica Et Biophysica Acta - General Subjects, 2006
The basic protein fraction of tissue extracts from 40 edible plants inhibited cell-free protein synthesis and released adenine from herring sperm DNA, thus having adenine glycosylase activity. This suggested the presence of ribosome-inactivating proteins (RIPs) in the plant extracts.
Jorge Vivanco, Andrea Bolognesi, Letizia Polito   +2 more
exaly   +8 more sources