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Ribosome-inactivating proteins

open access: yesToxicon, 2004
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
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Ribosome-inactivating proteins from plants

BBA - Biomembranes, 1993
Maria Giulia Battelli   +2 more
exaly   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

Ribosome-inactivating proteins up to date

open access: yesFEBS 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   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +3 more sources

Ribosome-Inactivating Proteins: A Family of Plant Proteins That Do More Than Inactivate Ribosomes

Critical Reviews in Plant Sciences, 2001
ABSTRACT 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

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
openaire   +2 more sources

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