Results 31 to 40 of about 3,204 (212)
A neutralizing antibody to the a chain of abrin inhibits abrin toxicity both in vitro and in vivo [PDF]
Clinical and Vaccine Immunology, 2008 Plant ribosome-inactivating proteins (RIPs) are RNA N-glycosidases that inhibit protein synthesis in cells. Abrin, a type II RIP, is an AB type toxin, which is one of the most lethal types of toxin known. The B chain facilitates the entry of the molecule
Karande A.A. +5 more
core +3 more sources
Modulation of Ricin Intoxication by the Autophagy Inhibitor EACC [PDF]
Toxins, 2022 The compound EACC (ethyl (2-(5-nitrothiophene-2-carboxamido) thiophene-3-carbonyl) carbamate) was recently reported to inhibit fusion of autophagosomes with lysosomes in a reversible manner by inhibiting recruitment of syntaxin 17 to autophagosomes.
Kirsten Sandvig +4 more
doaj +2 more sources
Abrin immunotoxin: targeted cytotoxicity and intracellular trafficking pathway.
PLoS ONE, 2013 BackgroundImmunotherapy is fast emerging as one of the leading modes of treatment of cancer, in combination with chemotherapy and radiation. Use of immunotoxins, proteins bearing a cell-surface receptor-specific antibody conjugated to a toxin, enhances ...
Sudarshan Gadadhar, Anjali A Karande
doaj +2 more sources
Simultaneous Detection of Ricin and Abrin DNA by Real-Time PCR (qPCR)
Toxins, 2012 Ricin and abrin are two of the most potent plant toxins known and may be easily obtained in high yield from the seeds using rather simple technology. As a result, both toxins are potent and available toxins for criminal or terrorist acts. However, as the
Roman Wölfel +3 more
doaj +2 more sources
A Monoclonal–Monoclonal Antibody Based Capture ELISA for Abrin
Toxins, 2017 Abrin, one of the most highly potent toxins in the world, is derived from the plant, Abrus precatorius. Because of its high toxicity, it poses potential bioterror risks.
Christina C. Tam +5 more
doaj +2 more sources
Biochemical Journal, 2014 Abrin, a type II ribosome-inactivating protein, comprises A and B subunits wherein the A subunit harbours toxin activity and the B subunit has a galactose-specific lectin activity.
Bora, Namrata +3 more
core +3 more sources
In vitro selection of DNA aptamer against abrin toxin and aptamer-based abrin direct detection
Biosensors and Bioelectronics, 2006 Abrin toxin as the target protein, belongs to class II ribosome-inactivating proteins family, has high toxicity to eukaryotic cells. Here, we firstly report the DNA aptamers, isolated by in vitro selection, recognize abrin toxin with high affinity and ...
Xie, Jianwei +6 more
core +4 more sources
The complete primary structure of abrin-a B chain
FEBS Letters, 1992 The complete 267 amino acid sequence of abrin-a B chain was determined by analysis of peptides obtained by digestion with trypsin, chymotrypsin, lysyl endopeptidase, Staphylacaccus aureus V8 protease and thermolysin.
Lin, Jung-Yaw +7 more
core +3 more sources
Trace level detections of abrin with high SNR piezoresistive cantilever biosensor
Sensors and Actuators B: Chemical, 2015 In this paper, sensitive detections on abrin are demonstrated in real-time by piezoresistive (PZR) cantilever sensors. With attempts to optimize the design and fabrication of the PZR cantilevers, the voltage fluctuation of the PZR sensors was decreased ...
Rui Zhao, Yongzheng Wen
exaly +2 more sources
Chimerolectins: Classification, structural architecture, and functional perspectives. [PDF]
Protein SciAbstract Lectins are proteins or glycoproteins capable of binding specifically and reversibly to carbohydrates, a property that, in itself, gives them great functional versatility in organisms from all kingdoms of nature. A subclass of these proteins, called chimerolectins, is composed of proteins that have at least one lectin domain associated with ...
Pinto-Junior VR +2 more
europepmc +2 more sources