Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases [PDF]
Toxins, 2018 Ribosome inactivating proteins (RIPs) form a vast family of hundreds of toxins from plants, fungi, algae, and bacteria. RIP activities have also been detected in animal tissues.
Julien Barbier, Daniel Gillet
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Ribosome-Inactivating Proteins: From Plant Defense to Tumor Attack [PDF]
Toxins, 2010 Ribosome-inactivating proteins (RIPs) are EC3.2.32.22 N-glycosidases that recognize a universally conserved stem-loop structure in 23S/25S/28S rRNA, depurinating a single adenine (A4324 in rat) and irreversibly blocking protein translation, leading ...
Maria Serena Fabbrini +3 more
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Plant Ribosome-Inactivating Proteins: Progesses, Challenges and Biotechnological Applications (and a Few Digressions) [PDF]
Toxins, 2017 Plant ribosome-inactivating protein (RIP) toxins are EC3.2.2.22 N-glycosidases, found among most plant species encoded as small gene families, distributed in several tissues being endowed with defensive functions against fungal or viral infections.
Maria Serena Fabbrini +3 more
doaj +2 more sources
Hyperuricaemia, Xanthine Oxidoreductase and Ribosome‐Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research [PDF]
Molecules, 2017 The enzymes called ribosome‐inactivating proteins (RIPs) that are able to depurinate nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline research field, mostly because of their promising medical ...
Andrea Bolognesi +3 more
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Analysis of castor bean ribosome-inactivating proteins and their gene expression during seed development [PDF]
Genetics and Molecular Biology, 2013 Ribosome-inactivating proteins (RIPs) are enzymes that inhibit protein synthesis after depurination of a specific adenine in rRNA. The RIP family members are classified as type I RIPs that contain an RNA-N-glycosidase domain and type II RIPs that contain
Guilherme Loss-Morais +7 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
Toxins, 2022 Targeted toxins (TT) for cancer treatment are a class of hybrid biologic comprised of a targeting domain coupled chemically or genetically to a proteinaceous toxin payload.
David J. Flavell, Sopsamorn U. Flavell
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Suicide nanoplasmids coding for ribosome-inactivating proteins [PDF]
European Journal of Pharmaceutical Sciences, 2022 Conventional eukaryotic expression plasmids contain a DNA backbone that is dispensable for the cellular expression of the transgene. In order to reduce the vector size, minicircle DNA technology was introduced. A drawback of the minicircle technology are considerable production costs.
Mitdank, Hardy +8 more
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Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site [PDF]
, 2007 Maize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form.
Amanda Nga-Sze Mak +40 more
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Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities. [PDF]
PLoS ONE, 2012 Ribosome-inactivating proteins (RIPs) inactivate prokaryotic or eukaryotic ribosomes by removing a single adenine in the large ribosomal RNA. Here we show maize RIP (MOD), an atypical RIP with an internal inactivation loop, interacts with the ribosomal ...
Yuen-Ting Wong +5 more
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