Results 21 to 30 of about 25,572 (194)

Cytotoxicity Effect of Quinoin, Type 1 Ribosome-Inactivating Protein from Quinoa Seeds, on Glioblastoma Cells [PDF]

open access: yesToxins, 2021
Ribosome-inactivating proteins (RIPs) are found in several edible plants and are well characterized. Many studies highlight their use in cancer therapy, alone or as immunoconjugates, linked to monoclonal antibodies directed against target cancer cells ...
Rossella Rotondo   +7 more
doaj   +2 more sources

Antiviral Activity of Ribosome-Inactivating Proteins [PDF]

open access: yesToxins, 2021
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases from plants (EC 3.2.2.22) that inactivate ribosomes thus inhibiting protein synthesis. The antiviral properties of RIPs have been investigated for more than four decades. However, interest in these proteins is rising due to the emergence of infectious diseases caused by new viruses and the ...
Citores González, Lucía   +2 more
openaire   +4 more sources

Biological Activities of Ribosome-Inactivating Proteins

open access: yesToxins, 2023
After more than 50 years of research, studies on the structure and biological activities of ribosome-inactivating proteins (RIPs) continue to provide a field of great interest within the scientific community, both for the health risks they pose and their applications in medicine and biotechnology [...]
Citores González, Lucía   +1 more
openaire   +5 more sources

Ribosome Inactivating Proteins from Rosaceae [PDF]

open access: yesMolecules, 2016
Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry.
Chenjing Shang   +2 more
openaire   +5 more sources

Ribosome-inactivating proteins [PDF]

open access: yesVirulence, 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, M.J.   +2 more
openaire   +4 more sources

Ribosome-Inactivating and Related Proteins [PDF]

open access: yesToxins, 2015
Ribosome-inactivating proteins (RIPs) are toxins that act as N-glycosidases (EC 3.2.2.22). They are mainly produced by plants and classified as type 1 RIPs and type 2 RIPs. There are also RIPs and RIP related proteins that cannot be grouped into the classical type 1 and type 2 RIPs because of their different sizes, structures or functions. In addition,
Schrot, Joachim   +2 more
openaire   +4 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 considerable production costs.
Mitdank, Hardy   +8 more
openaire   +2 more sources

Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]

open access: yes, 2017
Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core   +2 more sources

Functional analysis of RIP toxins from the Drosophila endosymbiont Spiroplasma poulsonii

open access: yesBMC Microbiology, 2019
Background Insects frequently live in close relationship with symbiotic bacteria that carry out beneficial functions for their host, like protection against parasites and viruses. However, in some cases, the mutualistic nature of such associations is put
Mario Gonzalo Garcia-Arraez   +3 more
doaj   +1 more source

Winter Aconite (Eranthis hyemalis) Lectin as a cytotoxic effector in the lifecycle of Caenorhabditis elegans [PDF]

open access: yesPeerJ, 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

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