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The role of the selectivity filter i...
~
Macri, Vincenzo Salvatore.
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The role of the selectivity filter in pacemaker channel gating.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
The role of the selectivity filter in pacemaker channel gating./
作者:
Macri, Vincenzo Salvatore.
面頁冊數:
92 p.
附註:
Source: Masters Abstracts International, Volume: 42-02, page: 0514.
Contained By:
Masters Abstracts International42-02.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MQ81874
ISBN:
0612818748
The role of the selectivity filter in pacemaker channel gating.
Macri, Vincenzo Salvatore.
The role of the selectivity filter in pacemaker channel gating.
- 92 p.
Source: Masters Abstracts International, Volume: 42-02, page: 0514.
Thesis (M.Sc.)--Simon Fraser University (Canada), 2002.
The pacemaker current (Ih) is important in the generation of action potentials in neurons and pacemaker cells of the sinoatrial node. Ih is a slowly activating inward current that is carried by sodium (Na+) and potassium (K+) ions, and is activated by hyperpolarization. Ih channel subunits have been cloned and are known as the h&barbelow;yperpolarization-activated c&barbelow;yclic-n&barbelow;ucleotide gated (HCN) subunits. The primary amino acid sequences of HCN channels are most similar to cyclic nucleotide-gated channels and voltage-gated potassium channels. Despite permeability to both Na+ and K+, a conserved GYG amino-acid motif known as the selectivity filter is located in the pore region of HCN channels as well as structurally related potassium channels where it is responsible for ion selectivity and conduction.
ISBN: 0612818748Subjects--Topical Terms:
1017686
Biology, Cell.
The role of the selectivity filter in pacemaker channel gating.
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The pacemaker current (Ih) is important in the generation of action potentials in neurons and pacemaker cells of the sinoatrial node. Ih is a slowly activating inward current that is carried by sodium (Na+) and potassium (K+) ions, and is activated by hyperpolarization. Ih channel subunits have been cloned and are known as the h&barbelow;yperpolarization-activated c&barbelow;yclic-n&barbelow;ucleotide gated (HCN) subunits. The primary amino acid sequences of HCN channels are most similar to cyclic nucleotide-gated channels and voltage-gated potassium channels. Despite permeability to both Na+ and K+, a conserved GYG amino-acid motif known as the selectivity filter is located in the pore region of HCN channels as well as structurally related potassium channels where it is responsible for ion selectivity and conduction.
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In order to examine the role of the selectivity filter, wild type (wt) and mutant mouse HCN subunit 2 (mHCN2) channels were expressed in c&barbelow;hinese h&barbelow;amster o&barbelow;vary (CHO) cells and currents were measured using the whole-cell patch clamp technique (n = 6--27 cells for the various experiments). (Abstract shortened by UMI.)
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