Multiple structural domains contribute to voltage-dependent inactivation of rat brain alpha(1E) calcium channels (Q48148450)

9 February 2018

title

Multiple structural domains contribute to voltage-dependent inactivation of rat brain alpha(1E) calcium channels (English)

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9 February 2018

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9 February 2018

author name string

Spaetgens RL

series ordinal

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9 February 2018

language of work or name

English

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publication date

1 August 1999

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Journal of Biological Chemistry

published in

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volume

274

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issue

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9 February 2018

page(s)

22428-22436

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Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype

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Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage

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The inactivation gate of the Shaker K+ channel behaves like an open-channel blocker.

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An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding

21 January 2018

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Structural parts involved in activation and inactivation of the sodium channel

21 January 2018

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Molecular determinants of voltage-dependent inactivation in calcium channels

21 January 2018

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Calcium channel β-subunit binds to a conserved motif in the I–II cytoplasmic linker of the α1-subunit

21 January 2018

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Playing Tetherball in the Nervous System

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Ca2+ channel block and inactivation: common molecular determinants

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Molecular determinants of high affinity phenylalkylamine block of L-type calcium channels in transmembrane segment IIIS6 and the pore region of the alpha1 subunit.

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.32.22428

1 reference

9 February 2018

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9 February 2018