Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling. - Wikidata - awgldk - TriplyDB

Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.

Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.

http://www.wikidata.org/entity/Q37267658

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Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility Scorpion venom components that affect ion-channels function 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.In vivo expression of G-protein beta1gamma2 dimer in adult mouse skeletal muscle alters L-type calcium current and excitation-contraction coupling.NALCN ion channels have alternative selectivity filters resembling calcium channels or sodium channels Properties of Na+ currents conducted by a skeletal muscle L-type Ca2+ channel pore mutant (SkEIIIK).Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca ( 2+) channel β1a subunit.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.Distinct Components of Retrograde Ca(V)1.1-RyR1 Coupling Revealed by a Lethal Mutation in RyR1.Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Structural insights into binding of STAC proteins to voltage-gated calcium channels.Distinct transcriptomic changes in E14.5 mouse skeletal muscle lacking RYR1 or Cav1.1 converge at E18.5.

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Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.

http://www.wikidata.org/entity/Q37267658

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on July 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Effects of inserting fluoresce ...... citation-contraction coupling.

@en

Effects of inserting fluoresce ...... citation-contraction coupling.

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type

label

Effects of inserting fluoresce ...... citation-contraction coupling.

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Effects of inserting fluoresce ...... citation-contraction coupling.

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prefLabel

Effects of inserting fluoresce ...... citation-contraction coupling.

@en

Effects of inserting fluoresce ...... citation-contraction coupling.

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The Journal of General Physiology

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Effects of inserting fluoresce ...... citation-contraction coupling.

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Claudia S Haarmann

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Kurt G Beam

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Roger A Bannister

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Symeon Papadopoulos

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P2860

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

A component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the dihydropyridine receptor alpha(1s) pore subunit.

Excitation-contraction coupling in skeletal muscle of a mouse lacking the dihydropyridine receptor subunit gamma1

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

A carboxyl-terminal region important for the expression and targeting of the skeletal muscle dihydropyridine receptor.

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.

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35-51

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scholarly article

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10.1085/JGP.200910241

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1

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134

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2009-07-01T00:00:00Z

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26328449

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19564426

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2712974

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