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2015

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Articles 31 - 32 of 32

Full-Text Articles in Chemicals and Drugs

Phytochemical Analysis And Biological Activities Of Cola Nitida Bark, Durand Dah-Nouvlessounon, Mamoudou H. Dicko Prof., Lamine Baba-Moussa Jan 2015

Phytochemical Analysis And Biological Activities Of Cola Nitida Bark, Durand Dah-Nouvlessounon, Mamoudou H. Dicko Prof., Lamine Baba-Moussa

Pr. Mamoudou H. DICKO, PhD

The aim of this study is to investigate some biological effects of Cola nitida’s bark after phytochemical screening. The bark was collected, dried, and then powdered for the phytochemical screening and extractions. Ethanol and ethyl acetate extracts of C. nitida were used in this study. The antibacterial activity was tested on ten reference strains and 28 meat isolated Staphylococcus strains by disc diffusionmethod. The antifungal activity of three fungal strains was determined on the Potato-Dextrose Agar medium mixed with the appropriate extract. The antioxidant activity was determined by DPPH and ABTS methods. Our data revealed the presence of various potent …


Dysfunctional Conformational Dynamics Of Protein Kinase A Induced By A Lethal Mutant Of Phospholamban Hinder Phosphorylation, Jonggul Kim, Larry R. Masterson, Alessandro Cembran, Raffaello Verardi, Lei Shi, Jiali Gao, Susan S. Taylor, Gianluigi Veglia Dec 2014

Dysfunctional Conformational Dynamics Of Protein Kinase A Induced By A Lethal Mutant Of Phospholamban Hinder Phosphorylation, Jonggul Kim, Larry R. Masterson, Alessandro Cembran, Raffaello Verardi, Lei Shi, Jiali Gao, Susan S. Taylor, Gianluigi Veglia

Larry Masterson

In the heart, phospholamban regulates Ca2+-ATPase function, controlling cardiac output. A single deletion (R14del) in the phospholamban recognition sequence kinase A is linked to the progression of familial dilated cardiomyopathy, a leading cause of death worldwide. Here, we provide the molecular mechanism for the sluggish phosphorylation of R14del by protein kinase A. We found that the R14 deletion affects the organization of the active site, which remains partially open and quite dynamic, preventing the formation of catalytically committed complex. We conclude that well-tuned structural and dynamic interplay between kinase and substrate is crucial for efficient phosphorylation. These results …