Results 171 to 180 of about 10,488 (210)
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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
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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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Membrane destabilization by ricin
European Biophysics Journal, 2004Ricin is a promising candidate for the treatment of cancer because it can be selectively targeted to tumor cells via linkage to monoclonal antibodies. Biochemical evidence suggests that escape of ricin or its ribosome-inactivating subunit from an intracellular compartment is mediated by retrograde transport to the endoplasmic reticulum and subsequent ...
Jan, Sun +6 more
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Photophysical Properties of Ricin
Photochemistry and Photobiology, 2007ABSTRACTThe molar absorption coefficient of ricin in phosphate‐buffered saline (PBS) at 279 nm was measured as (93 900 ± 3300) L mol−1 cm−1. The concentration of ricin was determined using amino acid analysis. The absorption spectrum of ricin was interpreted in terms of 69% contribution from absorption by tryptophan residues and 31% contribution from ...
A K, Gaigalas +4 more
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2020
A variety of strategies have been used to obtain cDNA and genomic clones encoding ricin. Since their isolation these sequences have been manipulated to allow expression of A chain (19) and A chain mutants (15,20,34), B chain (14,21-23) and proricin (24).
L M, Roberts, J W, Tregear, J M, Lord
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A variety of strategies have been used to obtain cDNA and genomic clones encoding ricin. Since their isolation these sequences have been manipulated to allow expression of A chain (19) and A chain mutants (15,20,34), B chain (14,21-23) and proricin (24).
L M, Roberts, J W, Tregear, J M, Lord
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Sepharose-unbinding ricin E as a source for ricin A chain immunotoxin
Journal of Immunological Methods, 2001To evaluate the Sepharose-unbinding ricin E as a preference source material for ricin A chain (RTA) in immunotoxin studies, RTA of ricin E (RTA(E)) was characterized and compared with RTA of the Sepharose-binding ricin D (RTA(D)). RTA(E) and RTA(D) were separated into two subunits of A(1) and A(2) by capillary electrophoresis. The isoelectric points of
B H, Woo, J T, Lee, D H, Na, K C, Lee
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1988
Bacterial and plant toxins composed of different protein subunits with diverse biological functions have provided an investigational focal point for researchers in many areas of specialization. Potent catalytic toxins have been linked to monoclonal antibodies (MoAb) for antibody directed cell targeting.
D A, Vallera, D E, Myers
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Bacterial and plant toxins composed of different protein subunits with diverse biological functions have provided an investigational focal point for researchers in many areas of specialization. Potent catalytic toxins have been linked to monoclonal antibodies (MoAb) for antibody directed cell targeting.
D A, Vallera, D E, Myers
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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
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2000
Abstract Ricin is a highly cytotoxic lectin derived from the seed of the castor bean, Ricinis communis (Euphorbiaceae). Aqueous extracts of the bean contain two different lectins: the cytotoxic RCA11 (ricin) and a hemagglutinin RCA1. The entire plant of the castor bean is toxic: in addition to the lectins, there is a powerful allergen
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Abstract Ricin is a highly cytotoxic lectin derived from the seed of the castor bean, Ricinis communis (Euphorbiaceae). Aqueous extracts of the bean contain two different lectins: the cytotoxic RCA11 (ricin) and a hemagglutinin RCA1. The entire plant of the castor bean is toxic: in addition to the lectins, there is a powerful allergen
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