Three-dimensional structure of CaV3.1: comparison with the cardiac L-type voltage-gated calcium channel monomer architecture.
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Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptorThe Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic PotentialGenetic disruption of voltage-gated calcium channels in psychiatric and neurological disordersProgress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.Looking for answers to EC coupling's persistent questionsCalcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.Oligomerization of Cavbeta subunits is an essential correlate of Ca2+ channel activity.The molecular architecture of dihydropyrindine receptor/L-type Ca2+ channel complexThree-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channel.Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The α2δ-1 subunit remodels CaV1.2 voltage sensors and allows Ca2+ influx at physiological membrane potentialsVoltage-gated calcium channels and their auxiliary subunits: physiology and pathophysiology and pharmacologyMechanosensitivity of ion channels based on protein-lipid interactions.NaChBac: the long lost sodium channel ancestorThe design and discovery of T-type calcium channel inhibitors for the treatment of central nervous system disorders.Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels.Site-specific biomolecule labeling with gold clusters.Negatively charged residues in the first extracellular loop of the L-type CaV1.2 channel anchor the interaction with the CaVα2δ1 auxiliary subunit.Physical interaction between calcineurin and Cav3.2 T-type Ca2+ channel modulates their functions.Calmodulin regulates Cav3 T-type channels at their gating brake.An Improved Method for Modeling Voltage-Gated Ion Channels at Atomic Accuracy Applied to Human Cav Channels.Voltage-gated calcium channels: their discovery, function and importance as drug targets
P2860
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P2860
Three-dimensional structure of CaV3.1: comparison with the cardiac L-type voltage-gated calcium channel monomer architecture.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Three-dimensional structure of ...... channel monomer architecture.
@en
type
label
Three-dimensional structure of ...... channel monomer architecture.
@en
prefLabel
Three-dimensional structure of ...... channel monomer architecture.
@en
P2093
P2860
P356
P1476
Three-dimensional structure of ...... channel monomer architecture.
@en
P2093
Adrian J Butcher
Anthony Davies
Ashraf Kitmitto
Conor P Walsh
P2860
P304
22310-22321
P356
10.1074/JBC.M109.017152
P407
P577
2009-06-11T00:00:00Z