3D Structure of the Dihydropyridine Receptor of Skeletal Muscle - sprookjes - yvandenbroek - TriplyDB

3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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2015 nî lūn-bûn

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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2015 թվականի հունվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年學術文章

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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European Journal of Translational Myology

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle

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Montserrat Samsó

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Absence of the beta subunit (cchb1) of the skeletal muscle dihydropyridine receptor alters expression of the alpha 1 subunit and eliminates excitation-contraction coupling

The crystal structure of a voltage-gated sodium channel

EMAN: semiautomated software for high-resolution single-particle reconstructions

International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels

Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution.

Do's and don'ts of cryo-electron microscopy: a primer on sample preparation and high quality data collection for macromolecular 3D reconstruction.

Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle

The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.

Malignant hyperthermia susceptibility arising from altered resting coupling between the skeletal muscle L-type Ca2+ channel and the type 1 ryanodine receptor

Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.

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2015-01-07T00:00:00Z

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