December 1, 1993The Journal of General PhysiologyOpen Access

Functional role of the NH2-terminal cytoplasmic domain of a mammalian A-type K channel.

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Population

Mammalian fast-inactivating K channel RHK1 (Kv1.4)

Comparison

Deletion of different domains in the… vs Wild-type RHK1 channel

Design

Preclinical

Authors

JTJulie Tseng-CrankEpigen Biosciences (United States)JYJianan YaoSun Yat-sen University MBMitchell F. BermanColumbia University Irving Medical Center

Discussion

Member takes

Implication

Extends ball-and-chain inactivation to mammalian RHK1; leaves open relevance to native cardiac K+ channel function.

Structured PICO

Population

Mammalian fast-inactivating K channel RHK1 (Kv1.4)

Intervention

Deletion of different domains in the NH2-terminal region (domain A, domain I, multiple domains)

Comparator

Wild-type RHK1 channel

Outcome

Changes in channel properties at whole cell and single channel levels (decay of whole cell currents, burst durations, probability of reopening)surrogate

The inactivation mechanism of the mammalian RHK1 potassium channel relies on a positively charged NH2-terminal cytoplasmic domain, similar to the 'ball and chain' model in Shaker channels.

Cite This Study

Tseng-Crank et al. (1993) studied this question.

synapsesocial.com/papers/6a844a47cdf3a848bdbd8a60 https://doi.org/10.1085/jgp.102.6.1057

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December 1, 1993The Journal of General PhysiologyOpen Access

Functional role of the NH2-terminal cytoplasmic domain of a mammalian A-type K channel.

View Full Paper

Ask AI

Bookmark

Population

Mammalian fast-inactivating K channel RHK1 (Kv1.4)

Comparison

Deletion of different domains in the… vs Wild-type RHK1 channel

Design

Preclinical

Authors

JTJulie Tseng-CrankEpigen Biosciences (United States)JYJianan YaoSun Yat-sen University MBMitchell F. BermanColumbia University Irving Medical Center

Discussion

Member takes

Implication

Extends ball-and-chain inactivation to mammalian RHK1; leaves open relevance to native cardiac K+ channel function.

Structured PICO

Population

Mammalian fast-inactivating K channel RHK1 (Kv1.4)

Intervention

Deletion of different domains in the NH2-terminal region (domain A, domain I, multiple domains)

Comparator

Wild-type RHK1 channel

Outcome

Changes in channel properties at whole cell and single channel levels (decay of whole cell currents, burst durations, probability of reopening)surrogate

The inactivation mechanism of the mammalian RHK1 potassium channel relies on a positively charged NH2-terminal cytoplasmic domain, similar to the 'ball and chain' model in Shaker channels.

Cite This Study

Tseng-Crank et al. (1993) studied this question.

synapsesocial.com/papers/6a844a47cdf3a848bdbd8a60 https://doi.org/10.1085/jgp.102.6.1057

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

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