Results 201 to 210 of about 25,873 (253)

Improving Cytotoxicity of Saporin with Saponin SO1406 Isolated from the Roots of Saponaria Officinalis. [PDF]

Biomedicines
Lim-Paik C, Zeng Q, Beyea R, Boohaker R, Wang P.   +4 more
europepmc   +1 more source

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

Synthetic overlapping genes stabilize genetic systems. [PDF]

mBio
Leonard SP, Halvorsen TM, Lim B, McCall NA, Park DM, Jiao Y, Yung MC, Ricci DP.   +7 more
europepmc   +1 more source

Ribosome specialization by cancer-associated ribosomal protein mutations: progress made and open questions. [PDF]

Philos Trans R Soc Lond B Biol Sci
Caruso M, De Keersmaecker K.
europepmc   +1 more source

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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
openaire   +2 more sources

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.
openaire   +3 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, M, Rothe, J, Eck, B, Möckel, H, Zinke   +4 more
openaire   +2 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
openaire   +2 more sources