Acta Pharmaceutica Sinica B, 2020 Ricin is a highly toxic type 2 ribosome-inactivating protein (RIP) which is extracted from the seeds of castor beans. Ricin is considered a potential bioterror agent and no effective antidote for ricin exists so far.
Wu Zhong, Xingzhou Li
exaly +3 more sources
Antibodies, 2013 Ricin is a type II ribosome inactivating protein (RIP) isolated from castor beans. Its high toxicity classifies it as a possible biological weapon. On the other hand, ricin linked to specific monoclonal antibodies or used in other conjugates has powerful
Monika Słomińska-Wojewódzka +2 more
exaly +3 more sources
Ricin Antibodies’ Neutralizing Capacity against Different Ricin Isoforms and Cultivars
Toxins, 2021 Ricin, a highly toxic protein from Ricinus communis, is considered a potential biowarfare agent. Despite the many data available, no specific treatment has yet been approved.
François Fenaille +2 more
exaly +3 more sources
A Monoclonal Antibody with a High Affinity for Ricin Isoforms D and E Provides Strong Protection against Ricin Poisoning [PDF]
ToxinsRicin is a highly potent toxin that has been used in various attempts at bioterrorism worldwide. Although a vaccine for preventing ricin poisoning (RiVax™) is in clinical development, there are currently no commercially available prophylaxis or ...
Loïs Lequesne +11 more
doaj +2 more sources
Ricin Toxicity to Intestinal Cells Leads to Multiple Cell Death Pathways Mediated by Oxidative Stress [PDF]
ToxinsRicin, a type 2 ribosome-inactivating protein, is a lethal toxin found in castor bean seeds. Although the systemic toxicity of ricin has been extensively studied, its localized effect on the gastrointestinal tract remains a critical concern, particularly
Francesco Biscotti +5 more
doaj +2 more sources
Differential Thermal Inactivation Enables Simultaneous Quantitation of Ricin and Abrin [PDF]
ToxinsRicin and abrin are highly lethal Type II ribosome-inactivating proteins. They depurinate the same site of the 28S rRNA to inhibit protein synthesis. Consequently, standard molecular-level activity assays used to detect the toxic activity of ricin or ...
Woo-Hyeon Jeong
doaj +2 more sources
Cell toxicity by ricin and elucidation of mechanism of Ricin inactivation
International Journal of Biological Macromolecules, 2018 Castor cake is a by-product of the extraction of oil from from seeds of castor plants (Ricinus communis). This by-product contains high levels of proteins, but a toxic protein, ricin, limits its use as an animal feed. Ricin can be efficiently inactivated by treatment with calcium oxide (CaO), which can be evaluated by a cytotoxicity assay using LLC-MK2
L C, Meneguelli de Souza +4 more
exaly +3 more sources
Development of a Graphene Oxide-Based Aptamer Nanoarray for Improved Neutralization and Protection Effects Against Ricin [PDF]
PharmaceuticsBackground/Objectives: Ricin’s high toxicity and potential as a bioweapon underscore the need for effective antidotes. Monoclonal antibodies, though effective, are limited by complex production.
Huafei Li +7 more
doaj +2 more sources
Spiroplasma Are Protective Heritable Symbionts With Low Physiological Impact in the Drosophilid Fly Zaprionus kolodkinae. [PDF]
Environ Microbiol RepZaprionus kolodkinae flies carry a maternally inherited ixodetis clade Spiroplasma that protects its host against wasp attack but has low overall physiological impact. Genome analysis presented a set of known symbiosis‐relevant effectors, and one encoding—a ricin B domain protein—that is novel to this Spiroplasma genome.
Alamer N +5 more
europepmc +2 more sources
Purified Immunoglobulin F(ab′) 2 Protects Mice and Rhesus Monkeys against Lethal Ricin Intoxication
Zoonoses, 2023 Ricin is a highly toxic ribosome-inactivating lectin derived from castor beans. To date, no antidote is available to treat ricin-poisoned patients, and the development of a safe and effective antidote is urgently needed.
Jingjing Tian +16 more
doaj +1 more source