A structural basis for drug-induced long QT syndrome.
By J. Mitcheson, Jun Chen, Monica Lin, C. Culberson, Michael Sanguinetti. Proceedings of the National Academy of Sciences of the United States of America, 2000
925 citations recorded by the source corpus.
Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/3767559f48ff88e3d02e6affc2c15c431cce97b6
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In Cardiology and Cardiovascular Medicine
- Kiril Lanevskij
- Remigijus Didziapetris
- Adam P. Hill
- Jamie I. Vandenberg
- M. Perrin
- Stefan A. Mann
- M. Perry
- Ying Ke
In Molecular Biology
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- Meryck F B Silva
Citations in the corpus
- Tuning hERG out: Antitarget QSAR Models for Drug Development (2014, background): “Those diverse chemicals can indeed interact with hERG because of its notorious ligand promiscuity, mainly due to its large hydrophobic intracellular binding pocket and its multiple states (open, inactive, and closed) [7].”
- The open pore conformation of potassium channels (2002, background): “The structure of the open pore builds on our understanding of the susceptibility of K p channels to block by organic cations, including many commonly prescribed pharmacological agent”
- Defects in cardiac function precede morphological abnormalities in fish embryos exposed to polycyclic aromatic hydrocarbons. (2004, background): “, 2003), suggesting the cardiac-specific KCNH2 potassium channel subunit as a possible molecular target (Keating and Sanguinetti, 2001; Mitcheson et al., 2000).”
- Compilation and physicochemical classification analysis of a diverse hERG inhibition database (2016, positive): “Several key residues participating in binding many potent hERG inhibitors, such as terfenadine, cisapride, or MK-499 had been identified using site directed mutagenesis approach [2, 5, 6].”
- hERG potassium channels and cardiac arrhythmia (2006, background): “Mutation of the putative Gly hinge in hERG alters gating but does not prevent channel openin”
- hERG K(+) channels: structure, function, and clinical significance. (2012, background): “In contrast, numerous studies have confirmed that aromatic S6 residues Tyr652 and Phe656 are crucial for high-affinity block by a range of different chemical entities (172, 356, 419).”