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Unveiling key genetic loci and candidate genes for brown spot disease resistance in rice based on QTL analysis. [PDF]

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Zhao DD   +9 more
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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
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
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Ribosome-inactivating proteins from plants

BBA - Biomembranes, 1993
Maria Giulia Battelli   +2 more
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
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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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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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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

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   +2 more
exaly   +8 more sources

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