oldenlandia/l cysteín

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Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif.

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The cyclotides are a family of circular proteins with a range of biological activities and potential pharmaceutical and agricultural applications. The biosynthetic mechanism of cyclization is unknown and the discovery of novel sequences may assist in achieving this goal. In the present study, we

Ethanol Extract of Oldenlandia diffusa - an Effective Chemotherapeutic for the Treatment of Colorectal Cancer in Humans: -Anti-Cancer Effects of Oldenlandia diffusa.

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OBJECTIVE Oldenlandia diffusa is traditionally used to relieve the symptoms of and to treat various diseases, but its anti-cancer activity has not been well studied. In the present study, the authors investigated the anti-cancer effects of an ethanol extract of Oldenlandia diffusa (EOD) on HT-29

A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides.

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A common structural motif consisting of a cystine knot and a small triple-stranded beta-sheet has been defined from comparison of the 3-dimensional structures of the polypeptides omega-conotoxin GVIA (Conus geographus), kalata BI (Oldenlandia affinis DC), and CMTI-I (Curcurbita maxima). These 3

Cyclotide discovery in Gentianales revisited--identification and characterization of cyclic cystine-knot peptides and their phylogenetic distribution in Rubiaceae plants.

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Cyclotides are a unique class of ribosomally synthesized cysteine-rich miniproteins characterized by a head-to-tail cyclized backbone and three conserved disulfide-bonds in a knotted arrangement. Originally they were discovered in the coffee-family plant Oldenlandia affinis (Rubiaceae) and have

Cyclotides are a component of the innate defense of Oldenlandia affinis.

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Cyclotides are small cysteine-rich plant peptides similar in size and processing to the defensins. Long-term growth of the Rubiaceae family plant Oldenlandia affinis under different conditions reveals a diverse cyclotide gene and peptide expression profile, including tissue specificity, suggesting

Refined structure and metal binding site of the kalata B1 peptide.

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The cyclic polypeptide kalata B1 from the African plant Oldenlandia affinis DC consists of 29 amino acid residues with three disulfide linkages. In this study we used two-dimensional NMR spectroscopy to investigate the three-dimensional structure of the peptide and to determine the disulfide

Circular micro-proteins and mechanisms of cyclization.

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Transpeptidation reactions result in the formation of new peptide bonds and this can occur between two separate peptides or within the one peptide. These reactions are catalyzed by enzymes and when the N- and C-terminus of the one peptide are joined it results in the formation of cyclic proteins.

Circular proteins and mechanisms of cyclization.

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Cyclization via head-to-tail linkage of the termini of a peptide chain occurs in only a small percentage of proteins, but engenders the resultant cyclic proteins with exceptional stability. The mechanisms involved are poorly understood and this review attempts to summarize what is known of the

Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1.

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The amino acid sequence and structure of a uterotonic polypeptide extracted from the African plant Oldenlandia affinis DC have been determined. The peptide, kalata B1, consists of 29 amino acid residues and is rich in cysteine (6), threonine (5), and glycine (5). Enzyme cleavage studies show that

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