Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca ( 2+) channel β1a subunit.
about
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 receptorRem uncouples excitation-contraction coupling in adult skeletal muscle fibers.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.Three-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channel.
P2860
Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca ( 2+) channel β1a subunit.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年论文
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name
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@ast
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@en
type
label
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@ast
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@en
prefLabel
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@ast
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@en
P2093
P2860
P356
P1433
P1476
Bimolecular fluorescence compl ...... Ca ( 2+) channel β1a subunit.
@en
P2093
David C Sheridan
Kurt G Beam
Nancy M Lorenzon
P2860
P356
10.4161/CHAN.18916
P577
2012-01-01T00:00:00Z