Results 141 to 150 of about 2,553 (186)
NX-1607: lifting the Cbl-b brake to promote T cell activation through MAPK/ERK pathways. [PDF]
J Immunother CancerTo A, Sugimura R.
europepmc +1 more source
Screening biotoxin aptamer and their application of optical aptasensor in food stuff: a review. [PDF]
Front ChemSun J, Zhang M, Gao Q, Shao B.
europepmc +1 more source
Peeking behind the carbocation: identification of (alternative) catalytic bases in the class II active site of conifer resin acid diterpene synthases. [PDF]
Biochem JRaslan AMAA, Peters RJ.
europepmc +1 more source
Docking in the Abies grandis abietaenol synthase to investigate the mechanism underlying conifer resin acid diterpene synthase evolution. [PDF]
Biochem JSchmidt-Dannert M +4 more
europepmc +1 more source
In vitro selection of DNA aptamer against abrin toxin and aptamer-based abrin direct detection
Biosensors and Bioelectronics, 2007 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 specificity, and have the advantage of no cross-reaction with structure-similar protein ricin toxin ...
Ningsheng Shao, Jianwei Xie, Lei Guo
exaly +5 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. The entry of the protein inside the cell is through the binding of the B chain to cell surface glycoproteins followed by receptor-mediated endocytosis and retrograde ...
Sudarshan, Gadadhar +3 more
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Toxicon, 2017
Abrin, a type II ribosome inactivating protein from the Abrus precatorius plant, is extremely toxic. It has been shown to be 75 times more potent than its infamous sister toxin, ricin and their potential use in bio-warfare is a cause of major concern.
Anjali Karande, Vinita Tiwari
exaly +4 more sources
Abrin, a type II ribosome inactivating protein from the Abrus precatorius plant, is extremely toxic. It has been shown to be 75 times more potent than its infamous sister toxin, ricin and their potential use in bio-warfare is a cause of major concern.
Anjali Karande, Vinita Tiwari
exaly +4 more sources
Toxicon, 1971
Abstract Crystalline abrin contained 4·9 per cent of neutral sugar in addition to 9·3 residues of glucosamine per mole of abrin (molecular weight 65,000). The neutral sugars consist of mannose, xylose and fucose in ratios of 2·08:1·00:0·94. When abrin was treated with periodate, the residual toxicity was only a few per cent of that of native abrin ...
J Y, Lin, Y C, Cheng, K, Liu, T C, Tung
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Abstract Crystalline abrin contained 4·9 per cent of neutral sugar in addition to 9·3 residues of glucosamine per mole of abrin (molecular weight 65,000). The neutral sugars consist of mannose, xylose and fucose in ratios of 2·08:1·00:0·94. When abrin was treated with periodate, the residual toxicity was only a few per cent of that of native abrin ...
J Y, Lin, Y C, Cheng, K, Liu, T C, Tung
openaire +3 more sources
Correlation of abrin‐mediated inhibition of protein synthesis and apoptosis
IUBMB Life, 2019 The plant toxin, abrin, a type-II ribosome inactivating protein, is extremely lethal, the human fatal dose being similar to 1 mu g/kg body weight. Abrin has been classified as an agent for bioterrorism, which is of concern.
Anjali Karande +2 more
exaly +2 more sources
Journal of the Forensic Science Society, 1971
A method is described for the detection of abrin, the toxic principle of Abrus precatorius , in biological material.
E G, Clarke, D J, Humphreys
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A method is described for the detection of abrin, the toxic principle of Abrus precatorius , in biological material.
E G, Clarke, D J, Humphreys
openaire +2 more sources