Results 21 to 30 of about 21,600 (215)

Evolution of plant ribosome-inactivating proteins [PDF]

open access: yes, 2010
This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago.
Peumans, Willy J, Van Damme, Els
core   +1 more source

Role of Phospholipase A2 in Retrograde Transport of Ricin

open access: yesToxins, 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

Active Immunity Induced by Passive IgG Post-Exposure Protection against Ricin

open access: yesToxins, 2014
Therapeutic antibodies can confer an instant protection against biothreat agents when administered. In this study, intact IgG and F(ab’)2 from goat anti-ricin hyperimmune sera were compared for the protection against lethal ricin mediated intoxication ...
Charles Chen Hu   +4 more
doaj   +1 more source

Ricin and Ricin-Containing Immunotoxins: Insights into Intracellular Transport and Mechanism of action in Vitro

open access: yesAntibodies, 2013
Ricin is a type II ribosome inactivating protein (RIP) isolated from castor beans. Its high toxicity classifies it as a possible biological weapon. On the other hand, ricin linked to specific monoclonal antibodies or used in other conjugates has powerful
Monika Słomińska-Wojewódzka   +1 more
doaj   +1 more source

The isolation and characterisation of temperature-dependent Ricin A chain molecules in Saccharomyces cerevisiae. [PDF]

open access: yes, 2007
Ricin is a heterodimeric plant protein that is potently toxic to mammalian cells. Toxicity results from the catalytic depurination of eukaryotic ribosomes by ricin A chain (RTA) that follows toxin endocytosis to, and translocation across, the ...
Allen   +41 more
core   +1 more source

Characterization of Ricin and R. communis Agglutinin Reference Materials

open access: yesToxins, 2015
Ricinus communis intoxications have been known for centuries and were attributed to the toxic protein ricin. Due to its toxicity, availability, ease of preparation, and the lack of medical countermeasures, ricin attracted interest as a potential ...
Sylvia Worbs   +9 more
doaj   +1 more source

Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]

open access: yes, 2017
Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core   +2 more sources

Equal Neutralization Potency of Antibodies Raised against Abrin Subunits

open access: yesAntibodies, 2020
Abrin and ricin are potent AB toxins, which are considered biological threats. To date, there are no approved treatments against abrin or ricin intoxications.
Yoav Gal   +9 more
doaj   +1 more source

Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins [PDF]

open access: yes, 2007
Retrograde transport allows proteins and lipids to leave the endocytic pathway to reach other intracellular compartments, such as trans-Golgi network (TGN)/Golgi membranes, the endoplasmic reticulum and, in some instances, the cytosol. Here, we have used
Amessou, Mohamed   +7 more
core   +3 more sources

"Alternative" endocytic mechanisms exploited by pathogens: new avenues for therapeutic delivery? [PDF]

open access: yes, 2007
Some pathogens utilize unique routes to enter cells that may evade the intracellular barriers encountered by the typical clathrin-mediated endocytic pathway.
Medina-Kauwe, LK
core   +1 more source

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