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Search for "ricin" in Full Text gives 6 result(s) in Beilstein Journal of Organic Chemistry.
Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin
Beilstein J. Org. Chem. 2024, 20, 306–320, doi:10.3762/bjoc.20.31
- one of the three potential binding sites. In contrast to other R-type lectins such as ricin, it lacks a catalytic domain. As R-type lectins are both a well-investigated family of lectins and widely used in research and beyond, we first wanted to analyze where CMA1 would be situated in the broader
- context of R-type lectins. A multiple sequence alignment of binding domains of representative R-type lectins (Figure 1a) showed that CMA1 exhibited a binding domain with a sequence relatively similar to those of the plant lectins SNA and ricin. However, we note that, in general, the substantial
- heterogeneity of binding motifs of even closely related lectins (SNA: Neu5Acα2-6, ricin: Gal/GalNAc) does not allow for a strong a priori hypothesis of what CMA1 would bind, even though R-type lectins in general are thought to prefer the Gal/GalNAc type motif mentioned in the context of ricin [21]. We next
Exploring the scope of DBU-promoted amidations of 7-methoxycarbonylpterin
Beilstein J. Org. Chem. 2020, 16, 509–514, doi:10.3762/bjoc.16.46
- , pterins have been a useful scaffold in the development of inhibitors of ricin [3][4], methionine synthase [5], nitric oxide synthase [6], shigella [7], and aldose reductase [8], as well as for treatment of leishmaniosis [9]. In addition to their therapeutic potential, pterin derivatives have been an
- for ricin toxin A (RTA) inhibitors [14]. By deprotonation of the lactam NH, and conversion to the DBU salt, the pterin easily dissolves in methanol at high concentrations, unprecedented for unfunctionalized pterins. This greatly accelerated the development of a library of bioactive pterins, as it
Lectins of Mycobacterium tuberculosis – rarely studied proteins
Beilstein J. Org. Chem. 2019, 15, 1–15, doi:10.3762/bjoc.15.1
- containing a carbohydrate-recognition domain similar to the CRD in ricin, a toxin of the poisonous plant Ricinus communis. R-type lectins have been detected in plants, animals, and bacteria. Plant R-type lectins often contain a separate subunit functioning as a toxin. Furthermore, ricin-type lectin domains
- have been found in glycosyltransferases as well as in bacterial hydrolases [95]. The Mtb gene product of Rv1419 shows 41% amino acid sequence similarity to R-type lectins and encodes the Mtb protein sMTL-13 (see Figure 5 for secondary structure prediction and alignment with the ricin B-like lectin from
- shown as blue arrows. B) sMTL-13 (aa28-155), encoded by Rv1419, showed with 100% confidence sequence similarity to a ricin B-like lectin of Streptomyces olivaceoviridis, the sequence identity was 22%. C) Known domain structure of HBHA (Rv0475): Transmembrane domain (TM), coiled coil domain, and heparin
Bis(β-lactosyl)-[60]fullerene as novel class of glycolipids useful for the detection and the decontamination of biological toxins of the Ricinus communis family
Beilstein J. Org. Chem. 2014, 10, 1504–1512, doi:10.3762/bjoc.10.155
- , Tsukuba, 305-8565, Japan 10.3762/bjoc.10.155 Abstract Glycosyl-[60]fullerenes were first used as decontaminants against ricin, a lactose recognition proteotoxin in the Ricinus communis family. A fullerene glycoconjugate carrying two lactose units was synthesized by a [3 + 2] cycloaddition reaction
- ; ricin; Introduction Carbohydrate-binding proteins (lectins) and proteotoxins, e.g., verotoxins [1][2] and cholera toxins [3], can cause serious damages to human cells. The carbohydrate binding proteins are able to interact with cell-surface glycoconjugates such as glycoproteins and glycolipids to
- aggregate the cells. Proteotoxins penetrate into the target cells after binding with glycoconjugates and disturb vital cell functions. Ricin, a proteotoxin isolated from the castor bean of the Ricinus communis family, is one of the strongest biological toxins and is registered as a scheduled compound in the
Carbohydrate PEGylation, an approach to improve pharmacological potency
Beilstein J. Org. Chem. 2014, 10, 1433–1444, doi:10.3762/bjoc.10.147
- of an O- or N-linked glycan by a chemical modification. The terminal residue of the N-linked carbohydrate in ricin A-chain has been PEGylated by mild oxidation with periodate followed by reaction with hydrazide-derivatized PEG [39]. The carbohydrate-specifically modified ricin showed better
- pharmacokinetic properties than the peptide amino-PEGylated or the unmodified ricin. The same technique was applied to glucose oxidase (GOx), a glycosylated dimeric protein. In this case the hydrazone was further stabilized by reduction with cyanoborohydride to afford a bioconjugate with retention of its activity
Synthesis of 2-substituted 9-oxa-guanines {5-aminooxazolo[5,4-d]pyrimidin- 7(6H)-ones} and 9-oxa-2-thio- xanthines {5-mercaptooxazolo[5,4-d]pyrimidin- 7(6H)-ones}
Beilstein J. Org. Chem. 2008, 4, No. 26, doi:10.3762/bjoc.4.26
- can be considered as 9-oxa-purine analogs of naturally occurring nucleic acid bases. Interest in this ring system has increased due to recent reports of biologically active derivatives. In particular, 5-aminooxazolo[5,4-d]pyrimidine-7(6H)-ones (9-oxa-guanines) have been shown to inhibit ricin. The
- prepared were found to inhibit ricin with IC50 ca. 1–3 mM. Keywords: Annulation; Click Chemistry; Cyclization; Purine Analogs; Ricin; Introduction Oxazolo[5,4-d]pyrimidines have been reported to possess a variety of biological activities including kinase inhibition [1][2], adenosine receptor antagonism
- [3] and tumor growth inhibition [4]. In particular, 5-aminooxazolo[5,4-d]pyrimidin-7(6H)-ones [9-oxa-guanines] and related heterocycles have been shown to inhibit the ability of ricin to inactivate ribosomes [5]. Given these reports, and the expectation of further applications based upon similarity
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