Intracellular Transport and Cytotoxicity of the Protein Toxin Ricin
Toxins, 2019 Ricin can be isolated from the seeds of the castor bean plant (Ricinus communis). It belongs to the ribosome-inactivating protein (RIP) family of toxins classified as a bio-threat agent due to its high toxicity, stability and availability.
Natalia Sowa-Rogozińska +2 more
exaly +4 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
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
Combining deep mutational scanning and SPR binning approaches for large-scale epitope identification of anti-ricin antibodies [PDF]
mAbsRicin, a ribosome-inactivating lectin from Ricinus communis seeds, has been used as a bioterrorism agent in multiple cases. While passive immunotherapy with anti-ricin antibodies shows promise in preclinical studies, no approved countermeasure exists ...
Ophélie Kot +10 more
doaj +2 more sources
Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks [PDF]
BMC GenomicsBackground The CBM13 family comprises carbohydrate-binding modules that occur mainly in enzymes and in several ricin-B lectins. The ricin-B lectin domain resembles the CBM13 module to a large extent.
Tibo De Coninck +4 more
doaj +2 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
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
Autophagic Degradation Is Involved in Cell Protection against Ricin Toxin
Toxins, 2023 Autophagy is a complex and highly regulated degradative process, which acts as a survival pathway in response to cellular stress, starvation and pathogen infection.
Yu Wu +8 more
doaj +1 more source
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.
Xu Zhao +7 more
doaj +1 more source
Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum [PDF]
, 2008 The plant cytotoxin ricin enters target mammalian cells by receptor-mediated endocytosis and undergoes retrograde transport to the endoplasmic reticulum (ER).
R. A. Spooner +32 more
core +4 more sources