BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
about
Membrane omega-3 fatty acids modulate the oligomerisation kinetics of adenosine A2A and dopamine D2 receptors.A G Protein-Coupled Receptor Dimerization Interface in Human Cone OpsinsProtease-activated receptors in hemostasis.Understanding the FRET Signatures of Interacting Membrane Proteins.Contribution of heteromerization to G protein-coupled receptor function.In vivo monitoring of the recruitment and activation of AP-1 by Arf1.ER/K linked GPCR-G protein fusions systematically modulate second messenger response in cellsThe Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists: Detection by Single-Molecule Tracking.Stoichiometric analysis of oligomeric states of three class-A GPCRs, chemokine-CXCR4, dopamine-D2, and prostaglandin-EP1 receptors, on living cells.Conformational biosensors reveal allosteric interactions between heterodimeric AT1 angiotensin and prostaglandin F2α receptors.
P2860
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P2860
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@ast
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@en
type
label
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@ast
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@en
prefLabel
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@ast
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@en
P2093
P2860
P356
P1433
P1476
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
@en
P2093
Chunman Li
Guangyu Wu
Nevin A Lambert
Tien-Hung Lan
P2860
P2888
P356
10.1038/SREP10166
P407
P50
P577
2015-05-08T00:00:00Z
P5875
P6179
1028444413