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Intrinsic Gating in Inward Rectifier Potassium Channels (Kir2.1) with Low Polyamine Affinity Generated by Site Directed Mutagenesis

So I, Ashmole I, Soh H, Park C, Spencer P, Leyland M, Stanfield

  • KMID: 2071587
  • Korean J Physiol Pharmacol.
  • 2003 Jun;7(3):131-142.
We have studied mutant forms of Kir2.1 in which an aspartate residue (D172), important for gating by intracellular polyamines, is replaced by one of three basic residues (Arg, Lys or...
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The Substates with Mutants That Negatively Charged Aspartate in Position 172 Was Replaced with Positive Charge in Murine Inward Rectifier Potassium Channel (Murine Kir2.1)

So I, Ashmole I, Stanfield

  • KMID: 1517043
  • Korean J Physiol Pharmacol.
  • 2003 Oct;7(5):267-273.
We have investigated the effect on inducing substate (s) of positively charged residues replaced in position 172 of the second transmembrane domain in murine inward rectifier potassium channels, formed by...
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Multiple Residues in the P-Region and M2 of Murine Kir 2.1 Regulate Blockage by External Ba2+

Lee YM, Thompson G, Ashmole I, Leyland M, So I, Stanfield

We have examined the effects of certain mutations of the selectivity filter and of the membrane helix M2 on Ba2+ blockage of the inward rectifier potassium channel, Kir 2.1. We...
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