Results 211 to 220 of about 25,369 (260)
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Critical Care Clinics, 2005
Ricin is a potent toxin found within the beans of the castor plant. Ricin's widespread availability makes it a viable biological weapon. Ricin intoxication mimics a variety of disease states, thus a low threshold of suspicion must be maintained to recognize a potential epidemic. Treatment is largely supportive.
Laura, Spivak, Robert G, Hendrickson
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Ricin is a potent toxin found within the beans of the castor plant. Ricin's widespread availability makes it a viable biological weapon. Ricin intoxication mimics a variety of disease states, thus a low threshold of suspicion must be maintained to recognize a potential epidemic. Treatment is largely supportive.
Laura, Spivak, Robert G, Hendrickson
+5 more sources
Disaster Management & Response, 2003
Ricin is a heterodimeric protein produced in the seeds of the castor oil plant (Ricinus communis). It is exquisitely potent to mammalian cells, being able to fatally disrupt protein synthesis by attacking the Achilles heel of the ribosome. For this enzyme to reach its substrate, it must not only negotiate the endomembrane system but it must also cross ...
Michael J, Lord +7 more
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Ricin is a heterodimeric protein produced in the seeds of the castor oil plant (Ricinus communis). It is exquisitely potent to mammalian cells, being able to fatally disrupt protein synthesis by attacking the Achilles heel of the ribosome. For this enzyme to reach its substrate, it must not only negotiate the endomembrane system but it must also cross ...
Michael J, Lord +7 more
openaire +4 more sources
Toxicon, 2001
The plant toxin ricin consists of two disulfide-linked polypeptides with different functions. The A-chain enters the cytosol and inactivates the ribosomes enzymatically, whereas the B-chain has lectin properties and binds to carbohydrates at the cell surface. This binding is a requirement for translocation of the A-chain to the cytosol. The bound toxin
S, Olsnes, J V, Kozlov
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The plant toxin ricin consists of two disulfide-linked polypeptides with different functions. The A-chain enters the cytosol and inactivates the ribosomes enzymatically, whereas the B-chain has lectin properties and binds to carbohydrates at the cell surface. This binding is a requirement for translocation of the A-chain to the cytosol. The bound toxin
S, Olsnes, J V, Kozlov
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Toxicological Reviews, 2003
Ricin is a naturally occurring toxin derived from the beans of the castor oil plant Ricinus communis. It is considered a potential chemical weapon. Ricin binds to cell surface carbohydrates, is internalised then causes cell death by inhibiting protein synthesis.
Sally M, Bradberry +4 more
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Ricin is a naturally occurring toxin derived from the beans of the castor oil plant Ricinus communis. It is considered a potential chemical weapon. Ricin binds to cell surface carbohydrates, is internalised then causes cell death by inhibiting protein synthesis.
Sally M, Bradberry +4 more
openaire +2 more sources
Revue de botanique appliquée et d'agriculture coloniale, 1930
Trochain Jean. Le Ricin (Suite).. In: Revue de botanique appliquee et d'agriculture coloniale, 10ᵉ annee, bulletin n°108, aout 1930. pp. 671-675.
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Trochain Jean. Le Ricin (Suite).. In: Revue de botanique appliquee et d'agriculture coloniale, 10ᵉ annee, bulletin n°108, aout 1930. pp. 671-675.
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2011
In this chapter we discuss vaccines to protect against the highly toxic plant-derived toxin, ricin. Due to its prevalence, ease of use, and stability it has been used in sporadic incidents of espionage. There is also concern that it will be used as an agent of bioterrorism.
Joan E, Smallshaw, Ellen S, Vitetta
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In this chapter we discuss vaccines to protect against the highly toxic plant-derived toxin, ricin. Due to its prevalence, ease of use, and stability it has been used in sporadic incidents of espionage. There is also concern that it will be used as an agent of bioterrorism.
Joan E, Smallshaw, Ellen S, Vitetta
openaire +2 more sources
Ricin, ricin agglutinin, and the ricin binding subunit structural comparison by Raman spectroscopy
Journal of Molecular Structure, 2005Raman spectroscopy is used to study conformation-sensitive vibrational bands of the plant toxins ricin and ricin agglutinin and the ricin binding subunit in aqueous solution. The analysis of the Raman data yields the conformational state of the protein molecules differing from that predicted by the X-ray data.
N.N. Brandt +5 more
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