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

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

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

http://www.wikidata.org/entity/Q34144818

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Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy Defects of the Glycinergic Synapse in Zebrafish.3D Structure of the Dihydropyridine Receptor of Skeletal Muscle Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel CSF-contacting neurons regulate locomotion by relaying mechanical stimuli to spinal circuits.Selenoprotein N is required for ryanodine receptor calcium release channel activity in human and zebrafish muscle Triclosan impairs swimming behavior and alters expression of excitation-contraction coupling proteins in fathead minnow (Pimephales promelas).STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal muscle triads Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in skeletal muscle.The ß subunit of voltage-gated Ca2+ channels Defective glycinergic synaptic transmission in zebrafish motility mutants.Structural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle.Reciprocal interactions regulate targeting of calcium channel beta subunits and membrane expression of alpha1 subunits in cultured hippocampal neurons.Non-Ca2+-conducting Ca2+ channels in fish skeletal muscle excitation-contraction coupling.The Cavβ1a subunit regulates gene expression and suppresses myogenin in muscle progenitor cells.Looking for answers to EC coupling's persistent questions The β(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail Amino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptor Expression and function of ryanodine receptor related pathways in PCB tolerant Atlantic killifish (Fundulus heteroclitus) from New Bedford Harbor, MA, USA.The molecular architecture of dihydropyrindine receptor/L-type Ca2+ channel complex Gene splicing of an invertebrate beta subunit (LCavβ) in the N-terminal and HOOK domains and its regulation of LCav1 and LCav2 calcium channels.The evolution of the mitochondria-to-calcium release units relationship in vertebrate skeletal muscles.The alpha1 subunit EGL-19, the alpha2/delta subunit UNC-36, and the beta subunit CCB-1 underlie voltage-dependent calcium currents in Caenorhabditis elegans striated muscle.Bidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle.Intramolecular ex vivo Fluorescence Resonance Energy Transfer (FRET) of Dihydropyridine Receptor (DHPR) β1a Subunit Reveals Conformational Change Induced by RYR1 in Mouse Skeletal Myotubes Rem uncouples excitation-contraction coupling in adult skeletal muscle fibers.Evolving concepts on the age-related changes in "muscle quality".Touch responsiveness in zebrafish requires voltage-gated calcium channel 2.1b An electrically coupled network of skeletal muscle in zebrafish distributes synaptic current.Fluorescence resonance energy transfer (FRET) indicates that association with the type I ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) α(1S) subunit.Zebrafish and motor control over the last decade.Rem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels.Alpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubes Role of Active Contraction and Tropomodulins in Regulating Actin Filament Length and Sarcomere Structure in Developing Zebrafish Skeletal Muscle.Sequence differences in the IQ motifs of CaV1.1 and CaV1.2 strongly impact calmodulin binding and calcium-dependent inactivation.Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.Fatigue in Rapsyn-Deficient Zebrafish Reflects Defective Transmitter Release

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P2860

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

http://www.wikidata.org/entity/Q34144818

description

2005 nî lūn-bûn

@nan

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@ast

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@en

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@nl

type

label

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@ast

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@en

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@nl

prefLabel

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@ast

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@en

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

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PNAS.0508710102

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Proceedings of the National Academy of Sciences of the United States of America

P1476

The beta 1a subunit is essenti ...... tor arrays in skeletal muscle.

@en

P2093

Bernhard E Flucher

http://www.w3.org/2001/XMLSchema#string

E Tatiana Felder

http://www.w3.org/2001/XMLSchema#string

Gerald J Obermair

http://www.w3.org/2001/XMLSchema#string

Johann Schredelseker

http://www.w3.org/2001/XMLSchema#string

Manfred Grabner

http://www.w3.org/2001/XMLSchema#string

Valentina Di Biase

http://www.w3.org/2001/XMLSchema#string

P2860

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

Absence of the gamma subunit of the skeletal muscle dihydropyridine receptor increases L-type Ca2+ currents and alters channel inactivation properties

The Ca2+ channel alpha2delta-1 subunit determines Ca2+ current kinetics in skeletal muscle but not targeting of alpha1S or excitation-contraction coupling

The modulation contrast microscope.

The I-II loop of the Ca2+ channel alpha1 subunit contains an endoplasmic reticulum retention signal antagonized by the beta subunit.

Reduced Ca2+ current, charge movement, and absence of Ca2+ transients in skeletal muscle deficient in dihydropyridine receptor beta 1 subunit.

A small-molecule inhibitor of skeletal muscle myosin II.

Molecular origin of the L-type Ca2+ current of skeletal muscle myotubes selectively deficient in dihydropyridine receptor beta1a subunit

Differential regulation of skeletal muscle L-type Ca2+ current and excitation-contraction coupling by the dihydropyridine receptor beta subunit.

Truncation of the carboxyl terminus of the dihydropyridine receptor beta1a subunit promotes Ca2+ dependent excitation-contraction coupling in skeletal myotubes.

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17219-17224

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scholarly article

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10.1073/PNAS.0508710102

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47

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P478

102

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Clara Franzini-Armstrong

P577

2005-11-14T00:00:00Z

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P5875

7481099

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16286639

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1288016

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