Results 171 to 180 of about 24,039 (208)

Ricin and Abrin in Biosecurity: Detection Technologies and Strategic Responses. [PDF]

Toxins (Basel)
Zajaczkowski W, Bojarska E, Furtak E, Bijak M, Szelenberger R, Niemcewicz M, Podogrocki M, Stela M, Cichon N.   +8 more
europepmc   +1 more source

Recombinant tritin protein exhibits antiviral activity against zucchini yellow mosaic virus. [PDF]

BMC Plant Biol
Demi̇rel S, Usta M, Korkmaz G, Kurt Z.
europepmc   +1 more source

Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus. [PDF]

Mol Cell
Lawrence IR, Sutton EC, Bhaskar S, Baserga SJ.   +3 more
europepmc   +1 more source

Unveiling the Mechanisms of Bacterial Resistance and Countermeasures. [PDF]

Pathogens
Xie Y, Lu H, Liu Y, Hu G, Lian S, Liu J, Pang S, Zhu G, Ding X.   +8 more
europepmc   +1 more source

Detection and Characterization of the Eukaryotic Vacant Ribosome. [PDF]

Int J Mol Sci
Delaney CE, Becskei A.
europepmc   +1 more source

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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

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, Ramarao, Vepachedu, Neelam, Sharma, Jorge M, Vivanco   +3 more
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