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Yihong Zhang
Researcher at University of Bristol
Publications - 18
Citations - 336
Yihong Zhang is an academic researcher from University of Bristol. The author has contributed to research in topics: hERG & Potassium channel. The author has an hindex of 7, co-authored 18 publications receiving 251 citations. Previous affiliations of Yihong Zhang include University of Manchester.
Papers
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Journal ArticleDOI
hERG potassium channel blockade by the HCN channel inhibitor bradycardic agent ivabradine
Dario Melgari,Kieran E. Brack,Chuan Zhang,Yihong Zhang,Aziza El Harchi,John S. Mitcheson,Christopher E. Dempsey,G. André Ng,Jules C. Hancox +8 more
TL;DR: Ivabradine prolongs ventricular repolarization and alters electrical restitution properties at concentrations relevant to the upper therapeutic range, and may have important implications both clinically and for future bradycardic drug design.
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Molecular basis of hERG potassium channel blockade by the class Ic antiarrhythmic flecainide
TL;DR: It is concluded that flecainide accesses the hERG channel from the cell interior on channel gating, binding low in the inner cavity, with the S6 F656 residue acting as a principal binding determinant.
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Ranolazine inhibition of hERG potassium channels: drug-pore interactions and reduced potency against inactivation mutants
TL;DR: Docking simulations indicated that the larger size of ranolazine gives it potential for a greater range of interactions with hERG pore side chains compared to lidocaine, in particular enabling interaction of its two aromatic groups with side chains of both Y652 and F656.
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An Update on the Structure of hERG.
TL;DR: An update of recent research is described that addresses the nature of the particular gated state of hERG captured in the new structure, and the insight afforded by the structure into the molecular basis for high affinity drug block of h ERG, the binding ofhERG activators and the Molecular basis of hERG's peculiar gating properties are addressed.
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Structural implications of hERG K + channel block by a high-affinity minimally structured blocker
Matthew V. Helliwell,Yihong Zhang,Aziza El Harchi,Chunyun Du,Jules C. Hancox,Christopher E. Dempsey +5 more
TL;DR: HERG channel inhibition by a minimally structured high-affinity hERG inhibitor, Cavalli-2, composed of three phenyl groups linked by polymethylene spacers around a central amino group, chosen to probe the spatial arrangement of side chain groups in the high-Affinity drug-binding site of the hERG pore is characterized.