Papers associated with inner ear (and kcnh2)

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	The evolutionarily conserved residue A653 plays a key role in HERG channel closing., Stepanovic SZ., J Physiol. June 1, 2009; 587 (Pt 11): 2555-66.
	Probing the binding sites and mechanisms of action of two human ether-a-go-go-related gene channel activators, 1,3-bis-(2-hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243)., Xu X., Mol Pharmacol. June 1, 2008; 73 (6): 1709-21.
	Probing the outer mouth structure of the HERG channel with peptide toxin footprinting and molecular modeling., Tseng GN., Biophys J. May 15, 2007; 92 (10): 3524-40.
	BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1., Zhang M., Biophys J. May 1, 2003; 84 (5): 3022-36.
	[K(+)](o)-dependent change in conformation of the HERG1 long QT mutation N629D channel results in partial reversal of the in vitro disease phenotype., Teng GQ., Cardiovasc Res. March 1, 2003; 57 (3): 642-50.
	Structural and functional role of the extracellular s5-p linker in the HERG potassium channel., Liu J., J Gen Physiol. November 1, 2002; 120 (5): 723-37.
	Trapping of a methanesulfonanilide by closure of the HERG potassium channel activation gate., Mitcheson JS., J Gen Physiol. March 1, 2000; 115 (3): 229-40.

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