Results 11 to 20 of about 10,421 (212)
Ricin Antibodies’ Neutralizing Capacity against Different Ricin Isoforms and Cultivars [PDF]
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.
Maria Lucia Orsini Delgado +13 more
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Inhibitors of the Cellular Trafficking of Ricin [PDF]
Toxins, 2012 Throughout the last decade, efforts to identify and develop effective inhibitors of the ricin toxin have focused on targeting its N-glycosidase activity.
Daniel Gillet +3 more
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Biochemical studies on ricin. XII. Iodination of ricin D.
Agricultural and Biological Chemistry, 1977 Approximately five tyrosine residues of ricin D were iodinated preferentially under appropriate conditions probably forming diiodotyrosine. Iodination of this toxin carried out in 0.1 m phosphate buffer at pH 7.0 and 0°C for 60 min with a 20 fold molar excess of iodine per mole of protein, yielded a main component which appeared as a single band on ...
Masatsune Ishiguro +5 more
openalex +4 more sources
Agricultural and Biological Chemistry, 1971 The purification of ricin was reinvestigated. Ricin can be purified by CM-cellulose column chromatography at pH 6.5, followed by gel filtration on Sephadex G-75 at pH 8.0 and finally CM-cellulose column chromatography at pH 7.0. The purified ricin preparation is electrophoretically and ultracentrifugally homogeneous and identical with ricin D in ...
Masatsune Ishiguro +2 more
openalex +5 more sources
Ricin Trafficking in Cells [PDF]
Toxins, 2015 The heterodimeric plant toxin ricin binds exposed galactosyls at the cell surface of target mammalian cells, and, following endocytosis, is transported in vesicular carriers to the endoplasmic reticulum (ER). Subsequently, the cell-binding B chain (RTB) and the catalytic A chain (RTA) are separated reductively, RTA embeds in the ER membrane and then ...
Robert A. Spooner, J. Michael Lord
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Toxins, 2019 Ricin, a lethal toxin derived from castor oil beans, is a potential bio-threat due to its high availability and simplicity of preparation. Ricin is prepared according to simple recipes available on the internet, and was recently considered in terrorist ...
Anita Sapoznikov +8 more
doaj +1 more source
Ricin toxicokinetics and its sensitive detection in mouse sera or feces using immuno-PCR. [PDF]
PLoS ONE, 2010 Ricin (also called RCA-II or RCA(60)), one of the most potent toxins and documented bioweapons, is derived from castor beans of Ricinus communis. Several in vitro methods have been designed for ricin detection in complex food matrices in the event of ...
Xiaohua He +4 more
doaj +1 more source
Differential ER stress as a driver of cell fate following ricin toxin exposure
FASEB BioAdvances, 2022 Inhalation of trace amounts of ricin toxin, a plant‐derived ribosome‐inactivating protein, results in ablation of alveolar macrophages, widespread epithelial damage, and the onset of acute respiratory distress syndrome (ARDS). While ricin's receptors are
Claire Peterson‐Reynolds +1 more
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Role of Phospholipase A2 in Retrograde Transport of Ricin
Toxins, 2011 Ricin is a protein toxin classified as a bioterror agent, for which there are no known treatment options available after intoxication. It is composed of an enzymatically active A-chain connected by a disulfide bond to a cell binding B-chain.
Kirsten Sandvig +3 more
doaj +1 more source
ISOLATION OF CRYSTALLINE RICIN [PDF]
Journal of General Physiology, 1948 A toxic crystalline protein has been isolated from crude extracts of castor bean meal. Ultracentrifuge and electrophoresis tests show the crystalline protein to become fairly homogeneous after three or four crystallizations. This is also confirmed by toxicity measurements.
M. Kunitz, Margaret R. McDonald
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