Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins [PDF]
Molecules, 2016 Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA.
Wei-Wei Shi +3 more
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Plants Producing Ribosome-Inactivating Proteins in Traditional Medicine [PDF]
Molecules, 2016 Ribosome-inactivating proteins (RIPs) are enzymes that deadenylate nucleic acids and are broadly distributed in the plant kingdom. Many plants that contain RIPs are listed in the pharmacopoeias of folk medicine all over the world, mostly because of their
Letizia Polito +4 more
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Special Issue: Ribosome-Inactivating Proteins—Commemorative Issue in Honor of Professor Fiorenzo Stirpe [PDF]
Molecules, 2017 The family of ribosome-inactivating proteins (RIPs) groups all enzymes (EC.3.2.2.22) with a so-called RIP domain which comprises N-glycosidase activity and enables these proteins to catalytically inactivate ribosomes.[...]
Els J.M. Van Damme
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The Use of Plant-Derived Ribosome Inactivating Proteins in Immunotoxin Development: Past, Present and Future Generations [PDF]
Toxins, 2017 Ribosome inactivating proteins (RIPs) form a class of toxins that was identified over a century ago. They continue to fascinate scientists and the public due to their very high activity and long-term stability which might find useful applications in the ...
Aleksander Rust +3 more
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Ribosome-Inactivating Proteins of Bougainvillea glabra Uncovered Polymorphism and Active Site Divergence [PDF]
Toxins, 2021 Ribosome-inactivating proteins (RIPs) are toxic proteins that can inhibit protein synthesis. RIPs purified from Bougainvillea have low nonspecific toxicity, showing promise for processing applications in the agricultural and medical fields.
Yihua Lin +6 more
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Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins [PDF]
Toxins, 2018 Ribosome-inactivating proteins (RIPs) are potent toxins that inactivate ribosomes by catalytically removing a specific adenine from the α-sarcin/ricin loop (SRL) of the large rRNA.
Yijun Zhou +3 more
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Ribosomal RNA N-glycosylase Activity Assay of Ribosome-inactivating Proteins [PDF]
Bio-Protocol, 2017 Ribosome-inactivating proteins (RIPs) are enzymes that irreversibly inactivate ribosomes as a consequence of their N-glycosylase (EC 3.2.2.22) activity. The enzyme cleaves the N-glycosidic bond between the adenine No.
José Ferreras +2 more
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Ribosome-inactivating proteins: potent poisons and molecular tools. [PDF]
Virulence, 2013 Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two classes.
Walsh MJ, Dodd JE, Hautbergue GM.
europepmc +4 more sources
Structures of Eukaryotic Ribosomal Stalk Proteins and Its Complex with Trichosanthin, and Their Implications in Recruiting Ribosome-Inactivating Proteins to the Ribosomes [PDF]
Toxins, 2015 Ribosome-inactivating proteins (RIP) are RNA N-glycosidases that inactivate ribosomes by specifically depurinating a conserved adenine residue at the α-sarcin/ricin loop of 28S rRNA. Recent studies have pointed to the involvement of the C-terminal domain
Andrew K. H. Choi +3 more
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Evolution of Plant Ribosome-Inactivating Proteins [PDF]
, 2010 This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago. This ancestral RIP domain gave rise to a direct lineage of type 1 RIPs (i.e. primary type 1 RIPs) still present today in
Willy J. Peumans, Els J. M. Van Damme
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