erythrina/tyrosine

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Cytotoxic and PTP1B inhibitory activities from Erythrina abyssinica.

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Bioassay-guided fractionation of the EtOAc extract of the stem bark of Erythrina abyssinica (Leguminosae) resulted in the isolation of three new (1-3), along with 12 known (4-15) pterocarpan derivatives. Their chemical structures were determined by physicochemical and spectroscopic data analysis

Pterocarpans with inhibitory effects on protein tyrosine phosphatase 1B from Erythrina lysistemon Hutch.

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Bioassay-guided fractionation of the MeOH extract of the stem bark of Erythrina lysistemon Hutch. resulted in isolation of pterocarpans (1-3), named erylysins A-C, along with nine known pterocarpans (4-12). Their structures were determined to be

Inhibitory effect of 2-arylbenzofurans from Erythrina addisoniae on protein tyrosine phosphatase-1B.

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Bioassay-guided fractionation of an EtOAc-soluble extract of the stem bark of Erythrina addisoniae (Leguminosae), using an in vitro PTP1B inhibitory assay, resulted in the isolation of three new (1-3) and three known (4-6) 2-arylbenzofuran derivatives. The new compounds were identified as

New prenylated isoflavonoids as protein tyrosine phosphatase 1B (PTP1B) inhibitors from Erythrina addisoniae.

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Bioassay-guided fractionation of the EtOAc extract of the root of Erythrina addisoniae (Leguminosae) resulted in the isolation of four new (1-4), along with 2 known prenylated isoflavonoids (5-6). The structures of the isolates were assigned on the basis of spectroscopic data analysis, focusing on

Protein tyrosine phosphatase-1B inhibitory activity of isoprenylated flavonoids isolated from Erythrina mildbraedii.

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Inhibition of protein tyrosine phosphatase-1B (PTP1B) has been proposed as a therapy for treatment of type-2 diabetes and obesity. Bioassay-guided fractionation of an EtOAc-soluble extract of the root bark of Erythrina mildbraedii, using an in vitro PTP1B inhibitory assay, resulted in the isolation

New prenylated flavanones from Erythrina abyssinica with protein tyrosine phosphatase 1B (PTP1B) inhibitory activity.

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As the insulin and leptin signaling pathway can be regulated by PTP1B, it has been suggested that compounds that reduce PTP1B activity or expression levels can be used for treating type 2 diabetes and obesity. In the course of our screening efforts on new PTP1B inhibitors, six new flavanones ( 1- 6)

Biosynthesis of the Erythrina alkaloids. The incorporation of tyrosine-2-C14 into the erythroidines.

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Inhibition of protein tyrosine phosphatase 1B by prenylated isoflavonoids isolated from the stem bark of Erythrina addisoniae.

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It has been suggested that protein tyrosine phosphatase 1B (PTP1B) inhibitors might be a therapeutic target for the treatment of type 2 diabetes and obesity. A bioassay-guided phytochemical study of the EtOAc extract of the stem bark of Erythrina addisoniae (Leguminosae) resulted in the

Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin.

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High-resolution X-ray crystallography of the complex of the Gal/GalNAc-specific Erythrina corallodendron lectin with lactose identified the amino acid side chains that form contacts with the galactose moiety of the disaccharide. The contribution of these amino acids to the binding of different

Isolation, purification, and physicochemical characterization of a D-galactose-binding lectin from seeds of Erythrina speciosa.

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A lectin was isolated from the saline extract of Erythrina speciosa seeds by affinity chromatography on lactose-Sepharose. The lectin content was about 265 mg/100g dry flour. E. speciosa seed lectin (EspecL) agglutinated all human RBC types, showing no human blood group specificity; however a slight

Purification, some properties of a D-galactose-binding leaf lectin from Erythrina indica and further characterization of seed lectin.

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Lectin from a leaf of Erythrina indica was isolated by affinity chromatography on Lactamyl-Seralose 4B. Lectin gave a single band in polyacrylamide gel electrophoresis (PAGE). In SDS-gel electrophoresis under reducing and non-reducing conditions Erythrina indica leaf lectin (EiLL) split into two

Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin.

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A mutant of Erythrina corallodendron lectin was generated with the aim of enhancing its affinity for N-acetylgalactosamine. A tyrosine residue close to the binding site of the lectin was mutated to a glycine in order to facilitate stronger interactions between the acetamido group of the sugar and

Redefinition of the carbohydrate specificity of Erythrina corallodendron lectin based on solid-phase binding assays and molecular modeling of native and recombinant forms obtained by site-directed mutagenesis.

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Binding of the N-acetyllactosamine-specific lectin from Erythrina corallodendron (ECorL) to four glycosphingolipids has been tested using the microtiter well assay. The role of several amino acids in the binding site region was studied by combining binding assays and molecular modeling for native

New 5-deoxyflavonoids and their inhibitory effects on protein tyrosine phosphatase 1B (PTP1B) activity.

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In the course of our program to search for protein tyrosine phosphatase 1B (PTPB) inhibitors, five new 5-deoxyflavonoids along with eight known derivatives were isolated from EtOAc layer of the root bark of Erythrina abyssinica. Their structures were elucidated on the basis of spectroscopic (IR, UV,

Induction of muscle protein degradation and weight loss by a tumor product.

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Splenocytes from mice bearing a cachexia-inducing tumor (MAC16) have been fused with mouse myeloma cells to produce hybridomas, which have been cloned to produce antibody reactive to a material which copurified with a lipid-mobilizing factor isolated from the same tumor. The monoclonal antibody has

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