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E. P. Mitchell

Researcher at University of Oxford

Publications -  8
Citations -  403

E. P. Mitchell is an academic researcher from University of Oxford. The author has contributed to research in topics: Glycogen phosphorylase & Glycogen synthase. The author has an hindex of 5, co-authored 8 publications receiving 398 citations.

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Potent inhibition of glycogen phosphorylase by a spirohydantoin of glucopyranose : first pyranose analogues of hydantocidin

TL;DR: This work reports the first example of specific enzyme inhibition by a spirohydantoin at the anomeric position of a sugar in the presence of glycogen phosphorylase.
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Design of inhibitors of glycogen phosphorylase: a study of alpha- and beta-C-glucosides and 1-thio-beta-D-glucose compounds.

TL;DR: It appears that hydration by a water molecule may provide sufficient stabilization to retain the chair conformation and the best inhibitor was N-methyl-beta-glucose-C-carboxamide, which showed a 46-fold improvement in Ki from the parent beta-D-glUCose.
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Glucose analogue inhibitors of glycogen phosphorylase: from crystallographic analysis to drug prediction using GRID force-field and GOLPE variable selection.

TL;DR: The computational procedure described in this work involves the use of the program GRID to describe the molecular structures and the progam GOLPE to obtain the partial least squares regression model with the highest prediction ability and forms the basis of a training set suitable for three-dimensional quantitative structure-activity relationship studies.
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Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.

TL;DR: The structural and kinetic results suggest that nojirimycin tetrazole in combination with phosphate exhibits properties consistent with a transition state analogue and demonstrate how one promotes the binding of the other.
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The design of potential antidiabetic drugs: experimental investigation of a number of β-D-glucose analogue inhibitors of glycogen phosphorylase

TL;DR: The three-dimensional structures of T state rabbit muscle GPb and the GPb-α-D-glucose complex have been exploited in the design of better regulators of GP that could shift the balance between glycogen synthesis and glycogen degradation in favour of the former.