Eutirucallin, a RIP-2 type lectin from the latex of Euphorbia tirucalli L. presents proinflammatory properties. [PDF]
PLoS ONE, 2014 Lectins are carbohydrate-binding proteins that recognize and modulate physiological activities and have been used as a toll for detection and identification of biomolecules, and therapy of diseases.
Sanzio Silva Santana +6 more
doaj +1 more source
Winter Aconite (Eranthis hyemalis) Lectin as a cytotoxic effector in the lifecycle of Caenorhabditis elegans [PDF]
PeerJ, 2015 The lectin found in the tubers of the Winter Aconite (Eranthis hyemalis) plant is an N-acetyl-D-galactosamine specific Type II Ribosome Inactivating Protein (RIP); Type II RIPs have shown anti-cancer properties, and hence have potential as therapeutic ...
Marie-Therese McConnell +4 more
doaj +2 more sources
Sapovaccarin-S1 and -S2, Two Type I RIP Isoforms from the Seeds of Saponaria vaccaria L.
Toxins, 2022 Type I ribosome-inactivating proteins (RIPs) are plant toxins that inhibit protein synthesis by exerting rRNA N-glycosylase activity (EC 3.2.2.22). Due to the lack of a cell-binding domain, type I RIPs are not target cell-specific. However once linked to
Louisa Schlaak +3 more
doaj +1 more source
Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins. [PDF]
PLoS ONE, 2012 Shiga-like toxins are ribosome-inactivating proteins (RIP) produced by pathogenic E. coli strains that are responsible for hemorrhagic colitis and hemolytic uremic syndrome.
Andrew J McCluskey +5 more
doaj +1 more source
The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity. [PDF]
PLoS ONE, 2015 Although the protein translation inhibition activity of ribosome inactivating proteins (RIPs) is well documented, little is known about the contribution of the lectin chain to the biological activity of these proteins.
Chenjing Shang +5 more
doaj +1 more source
A new age for biomedical applications of Ribosome Inactivating Proteins (RIPs): from bioconjugate to nanoconstructs [PDF]
Journal of Biomedical Science, 2016 Ribosome-inactivating proteins (RIPs) are enzymes (3.2.2.22) that possess N-glycosilase activity that irreversibly inhibits protein synthesis. RIPs have been found in plants, fungi, algae, and bacteria; their biological role is still under investigation, even if it has been recognized their role in plant defence against predators and viruses ...
Pizzo, Elio, DI MARO, Antimo
openaire +4 more sources
Toxins, 2015 Ribosome inactivating proteins (RIPs) inhibit protein synthesis by depurinating the large ribosomal RNA and some are found to possess anti-human immunodeficiency virus (HIV) activity. Maize ribosome inactivating protein (RIP) has an internal inactivation
Rui-Rui Wang +13 more
doaj +1 more source
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.
Peumans, Willy J, Van Damme, Els
core +1 more source
Special issue: Ribosome-inactivating proteins : commemorative issue in honor of Professor Fiorenzo Stirpe [PDF]
, 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.[...
Van Damme, Els
core +3 more sources
Isolation and Characterization of an RIP (Ribosome-Inactivating Protein)-Like Protein from Tobacco with Dual Enzymatic Activity [PDF]
Plant Physiology, 2004 Abstract Ribosome-inactivating proteins (RIPs) are N-glycosidases that remove a specific adenine from the sarcin/ricin loop of the large rRNA, thus arresting protein synthesis at the translocation step. In the present study, a protein termed tobacco RIP (TRIP) was isolated from tobacco (Nicotiana tabacum) leaves and purified using ion ...
SHARMA N. +7 more
openaire +3 more sources