Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle. - Test2 - elhamkhani - TriplyDB

Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle.

Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle.

http://www.wikidata.org/entity/Q37657281

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3D Structure of the Dihydropyridine Receptor of Skeletal Muscle Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel 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.A malignant hyperthermia-inducing mutation in RYR1 (R163C): consequent alterations in the functional properties of DHPR channels Looking for answers to EC coupling's persistent questions Ryanodine modification of RyR1 retrogradely affects L-type Ca(2+) channel gating in skeletal muscle.The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.Interaction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling Multiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle.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 Bidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Computer modeling of siRNA knockdown effects indicates an essential role of the Ca2+ channel alpha2delta-1 subunit in cardiac excitation-contraction coupling.Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunit Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca ( 2+) channel β1a subunit.Evolution of skeletal type e-c coupling: a novel means of controlling calcium delivery.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.Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Core skeletal muscle ryanodine receptor calcium release complex.The proximal C-terminus of α(1C) subunits is necessary for junctional membrane targeting of cardiac L-type calcium channels.Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit.The alpha(1S) III-IV loop influences 1,4-dihydropyridine receptor gating but is not directly involved in excitation-contraction coupling interactions with the type 1 ryanodine receptor.Skeletal muscle excitation-contraction coupling is independent of a conserved heptad repeat motif in the C-terminus of the DHPRbeta(1a) subunit.Stable incorporation versus dynamic exchange of β subunits in a native Ca2+ channel complex.Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion.Junctional trafficking and restoration of retrograde signaling by the cytoplasmic RyR1 domain.De novo reconstitution reveals the proteins required for skeletal muscle voltage-induced Ca2+ release.Transport of the alpha subunit of the voltage gated L-type calcium channel through the sarcoplasmic reticulum occurs prior to localization to triads and requires the beta subunit but not Stac3 in skeletal muscles.

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Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle.

http://www.wikidata.org/entity/Q37657281

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 22 September 2004

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Differential contribution of s ...... tor arrays in skeletal muscle.

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Differential contribution of s ...... tor arrays in skeletal muscle.

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type

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Differential contribution of s ...... tor arrays in skeletal muscle.

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Differential contribution of s ...... tor arrays in skeletal muscle.

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Differential contribution of s ...... tor arrays in skeletal muscle.

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Differential contribution of s ...... tor arrays in skeletal muscle.

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MBC.E04-05-0414

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Molecular Biology of the Cell

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Differential contribution of s ...... tor arrays in skeletal muscle.

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Bernhard E Flucher

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Cecilia Paolini

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Gerlinde Kugler

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Hiroaki Takekura

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Manfred Grabner

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P2860

Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscle

Malignant-hyperthermia susceptibility is associated with a mutation of the alpha 1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscle

Identification of a region of RyR1 that participates in allosteric coupling with the alpha(1S) (Ca(V)1.1) II-III loop

Primary structure of the receptor for calcium channel blockers from skeletal muscle

Tagging with green fluorescent protein reveals a distinct subcellular distribution of L-type and non-L-type Ca2+ channels expressed in dysgenic myotubes.

Cooperation of two-domain Ca(2+) channel fragments in triad targeting and restoration of excitation- contraction coupling in skeletal muscle.

Involvement of the carboxy-terminus region of the dihydropyridine receptor beta1a subunit in excitation-contraction coupling of skeletal muscle

RYR1 and RYR3 have different roles in the assembly of calcium release units of skeletal muscle.

The structure of Ca(2+) release units in arthropod body muscle indicates an indirect mechanism for excitation-contraction coupling

Cardiac-type EC-coupling in dysgenic myotubes restored with Ca2+ channel subunit isoforms alpha1C and alpha1D does not correlate with current density

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5408-5419

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scholarly article

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10.1091/MBC.E04-05-0414

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12

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15

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Clara Franzini-Armstrong

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2004-09-22T00:00:00Z

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15385628

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532020

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