nothofagin/necrosis

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Aspalathin and nothofagin from rooibos (Aspalathus linearis) inhibit endothelial protein C receptor shedding in vitro and in vivo.

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Aspalathin (Asp) and nothofagin (Not) are two major active dihydrochalcones found in green rooibos, which have been reported for their anti-oxidant activity. Increasing evidence has demonstrated that beyond its role in the activation of protein C, endothelial cell protein C receptor (EPCR) is also

Ameliorative Effect of Aspalathin and Nothofagin from Rooibos (Aspalathus linearis) on HMGB1-Induced Septic Responses In Vitro and In Vivo.

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The ubiquitous nuclear protein, high mobility group box 1 (HMGB1), is released by activated macrophages and human umbilical vein endothelial cells (HUVECs) and functions as a late mediator of experimental sepsis. Aspalathin (Asp) and nothofagin (Not), which have been reported to have anti-oxidant

Antithrombotic activities of aspalathin and nothofagin via inhibiting platelet aggregation and FIIa/FXa.

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Aspalathin (Asp) and nothofagin (Not) are two major active dihydrochalcones found in green rooibos tea (Aspalathus linearis; family, Fabaceae; tribe, Crotalarieae), which have been reported for their anti-oxidant activity. Here, the anticoagulant activities of Asp and Not were examined by monitoring

Renal protective effects of aspalathin and nothofagin from rooibos (Aspalathus linearis) in a mouse model of sepsis.

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BACKGROUND Aspalathin (Aspt) and nothofagin (Not) were reported to have antioxidant activity and are the two major active dihydrochalcones in green rooibos. This study was conducted to determine whether Asp and Not can modulate renal functional damage in a mouse model of sepsis and to elucidate the

Anti-inflammatory Effects of Aspalathin and Nothofagin from Rooibos (Aspalathus linearis) In Vitro and In Vivo.

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Aspalathin (Asp) and nothofagin (Not) are two major active dihydrochalcones found in green rooibos, which have been reported for their anti-oxidant activity. Here, we investigated the anti-inflammatory effects and underlying mechanisms of Asp and Not against lipopolysaccharide (LPS)-mediated

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