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Pharmacology of cardiac potassium channels.
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Stereoselective block of cardiac sodium channels by bupivacaine in guinea pig ventricular myocytes.
TLDR
The large level of pulse-dependent block and the failure of the pure inactivated-state block model indicate that bupivacaine interacts with the activated (or open) state of the cardiac sodium channel in addition to its block of the inactivated state.
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Immunomodulatory effects of diclofenac in leukocytes through the targeting of Kv1.3 voltage-dependent potassium channels.
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Stereoselective block of a human cardiac potassium channel (Kv1.5) by bupivacaine enantiomers.
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Molecular determinants of stereoselective bupivacaine block of hKv1.5 channels.
TLDR
The results suggest that (1) the bupivacaine binding site is located in the inner mouth of the pore, (2) stereoselective block displays subfamily selectivity, and (3) a polar interaction with T505 combined with hydrophobic interactions with L508 and V512 are required for stereoselectedive block.
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Immunomodulation of voltage-dependent K+ channels in macrophages: molecular and biophysical consequences
TLDR
It is demonstrated that the biophysical properties of voltage-dependent K+ currents are modified upon activation or immunosuppression in macrophages, in accordance with changes in the molecular characteristics of the heterotetrameric Kv1.3/KV1.5 hybrid channel.
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{Omega}-3 and {omega}-6 polyunsaturated fatty acids block HERG channels.
TLDR
The results obtained suggest that both PUFAs bind preferentially to the open state of the channel, although an interaction with inactivated HERG channels cannot be ruled out for AA.
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Putative binding sites for benzocaine on a human cardiac cloned channel (Kv1.5).
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(cid:1) -3 and (cid:1) -6 polyunsaturated fatty acids block HERG channels
TLDR
The results obtained suggest that both PUFAs bind preferentially to the open state of the channel, although an interaction with inactivated HERG channels cannot be ruled out for AA.
Class III antiarrhythmic effects of zatebradine. Time-, state-, use-, and voltage-dependent block of hKv1.5 channels.
TLDR
Results indicate that zatebradine is an open-channel blocker of hKv 1.5, binding occurs in the internal mouth of the ion pore, unbinding is required before the channel can close, and zate bradine-induced block is use dependent because of slower recovery kinetics in the presence of the drug.
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