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
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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
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Toxins, 2016 Ricin is a type 2 ribosome-inactivating protein (RIP), containing a catalytic A chain and a lectin-like B chain. It inhibits protein synthesis by depurinating the N-glycosidic bond at α-sarcin/ricin loop (SRL) of the 28S rRNA, which thereby prevents the ...
Wei-Wei Shi +5 more
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Brazilian Journal of Pharmaceutical Sciences, 2022 The present study deals with the computational design and analysis of a novel fusion protein based on a single chain variable fragment that binds to the extracellular domain of human epidermal growth factor receptor 2 (HER2) in breast cancer cells. Alpha
Farzaneh Barkhordari +5 more
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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
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Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation
Toxins, 2016 To improve the pharmacological properties of maize ribosome-inactivating protein (maize RIP) for targeting HIV-infected cells, the previously engineered TAT-fused active form of maize RIP (MOD) was further engineered for cysteine-directed PEGylation.
Ka-Yee Au +4 more
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Small-molecule inhibitor leads of ribosome-inactivating proteins developed using the doorstop approach. [PDF]
PLoS ONE, 2011 Ribosome-inactivating proteins (RIPs) are toxic because they bind to 28S rRNA and depurinate a specific adenine residue from the α-sarcin/ricin loop (SRL), thereby inhibiting protein synthesis.
Yuan-Ping Pang +11 more
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Ribosome-inactivating proteins (RIPs) and their important health promoting property
RSC Advances, 2016 Ribosome-inactivating proteins (RIPs), widely present in plants, certain fungi and bacteria, can inhibit protein synthesis by removing one or more specific adenine residues from the large subunit of ribosomal RNAs (rRNAs).
Shuzhen Wang +5 more
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Protein folding on the ribosome studied using NMR spectroscopy [PDF]
, 2013 NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution.
Christodoulou, J +9 more
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Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases
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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