Results 1 to 10 of about 10,421 (212)

A Monoclonal Antibody with a High Affinity for Ricin Isoforms D and E Provides Strong Protection against Ricin Poisoning [PDF]

open access: yesToxins
Ricin 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

Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks [PDF]

open access: yesBMC Genomics
Background 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]

open access: yesPharmaceutics
Background/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

Identification and Biological Evaluation of a Novel Small-Molecule Inhibitor of Ricin Toxin [PDF]

open access: yesMolecules
The plant-derived toxin ricin is classified as a type 2 ribosome-inactivating protein (RIP) and currently lacks effective clinical antidotes. The toxicity of ricin is mainly due to its ricin toxin A chain (RTA), which has become an important target for ...
Xinran Yang   +6 more
doaj   +2 more sources

Toxicity and Efficacy Evaluation of Soluble Recombinant Ricin Vaccine [PDF]

open access: yesVaccines
Background: Ricin, a toxin extracted from the seeds of Ricinus communis, is classified as a ribosome-inactivating protein. The A-subunit of ricin shows RNA N-glycosidase activity that cleaves ribosomal RNA (rRNA) and exhibits toxicity by inhibiting ...
Hyeongseok Yun   +8 more
doaj   +2 more sources

Purified Immunoglobulin F(ab′) 2 Protects Mice and Rhesus Monkeys against Lethal Ricin Intoxication

open access: yesZoonoses, 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

open access: yesToxins, 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

RIPpore: A Novel Host-Derived Method for the Identification of Ricin Intoxication through Oxford Nanopore Direct RNA Sequencing

open access: yesToxins, 2022
Ricin is a toxin which enters cells and depurinates an adenine base in the sarcin-ricin loop in the large ribosomal subunit, leading to the inhibition of protein translation and cell death.
Yan Ryan   +6 more
doaj   +1 more source

Influence of environmental conditions on the attenuation of ricin toxin on surfaces. [PDF]

open access: yesPLoS ONE, 2018
Ricin is a highly-toxic compound derived from castor plant beans. Several incidents involving contamination of residences and buildings due to ricin production or dissemination have occurred in recent years.
Joseph P Wood   +3 more
doaj   +1 more source

Ricin crosses polarized human intestinal cells and intestines of ricin-gavaged mice without evident damage and then disseminates to mouse kidneys. [PDF]

open access: yesPLoS ONE, 2013
Ricin is a potent toxin found in the beans of Ricinus communis and is often lethal for animals and humans when aerosolized or injected and causes significant morbidity and occasional death when ingested.
Alyssa D Flora   +5 more
doaj   +1 more source

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