Results 21 to 30 of about 1,593,797 (211)

Ribosomal RNA N-glycosylase Activity Assay of Ribosome-inactivating Proteins [PDF]

open access: yesBio-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
doaj   +2 more sources

Ribosome inactivating proteins and apoptosis [PDF]

open access: yesFEBS Letters, 2005
Ribosome inactivating proteins (RIPs) are protein toxins that are of plant or microbial origin that inhibit protein synthesis by inactivating ribosomes. Recent studies suggest that RIPs are also capable of inducing cell death by apoptosis.
Karande, Anjali A.   +10 more
core   +3 more sources

Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases [PDF]

open access: yesToxins, 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
doaj   +2 more sources

Ribosome-Inactivating Proteins: From Plant Defense to Tumor Attack

open access: yesToxins, 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
doaj   +3 more sources

Suicide nanoplasmids coding for ribosome-inactivating proteins [PDF]

open access: yesEuropean 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
Sonntag, A.   +8 more
core   +4 more sources

Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy

open access: yesToxins, 2011
The type 2 ribosome-inactivating proteins (RIPs) isolated from some species belonging to the Sambucus genus, have the characteristic that although being even more active than ricin inhibiting protein synthesis in cell-free extracts, they lack the high ...
Pilar Jiménez   +4 more
doaj   +3 more sources

Evolution of plant ribosome-inactivating proteins [PDF]

open access: yes, 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.
Van Damme, Els   +3 more
core   +3 more sources

Hyperuricaemia, Xanthine Oxidoreductase and Ribosome‐Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research [PDF]

open access: yesMolecules, 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
doaj   +2 more sources

Biophysical and Biochemical Assays for Screening Small Molecule Inhibitors Targeting Toxin–Ribosome Interactions [PDF]

open access: yesToxins
Ribosome-inactivating proteins are a class of toxins that target eukaryotic ribosomes, inhibit protein synthesis, and ultimately induce cell death. Several of these toxins pose significant clinical and public health threats.
Eric J. Bryan   +6 more
doaj   +2 more sources

Ribosome-inactivating proteins: progress and problems.

open access: yesCellular and Molecular Life Sciences, 2006
Ribosome-inactivating proteins (RIPs), mostly from plants, are enzymes which depurinate rRNA, thus inhibiting protein synthesis, and depurinate also other polynucleotide substrates.
BATTELLI, MARIA GIULIA, STIRPE, FIORENZO
core   +3 more sources

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