Results 181 to 190 of about 1,593,838 (216)
Ribosome-inactivating proteins
The known toxic and non-toxic ribosome-inactivating proteins are listed and classified and their nature, distribution mechanism of action and other properties are described.
Fiorenzo Stirpe
exaly +5 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Ribosome-inactivating proteins from plants
BBA - Biomembranes, 1993Maria Giulia Battelli +2 more
exaly +3 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Ribosome-inactivating proteins up to date
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, 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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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
openaire +1 more source
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
openaire +2 more sources

