Förster resonance energy transfer (FRET) correlates of altered subunit stoichiometry in cys-loop receptors, exemplified by nicotinic α4β2. (Q36202419)

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English	Förster resonance energy transfer (FRET) correlates of altered subunit stoichiometry in cys-loop receptors, exemplified by nicotinic α4β2.	scientific article

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Europe PubMed Central

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12 August 2017

Förster resonance energy transfer (FRET) correlates of altered subunit stoichiometry in cys-loop receptors, exemplified by nicotinic α4β2. (English)

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Europe PubMed Central

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12 August 2017

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Fraser J Moss

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Rahul Srinivasan

1

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Europe PubMed Central

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12 August 2017

Christopher I Richards

2

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12 August 2017

Crystal Dilworth

3

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Europe PubMed Central

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12 August 2017

Dennis A Dougherty

5

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12 August 2017

Henry A Lester

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12 August 2017

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10 August 2012

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Europe PubMed Central

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12 August 2017

International Journal of Molecular Sciences

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12 August 2017

13

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12 August 2017

8

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Europe PubMed Central

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12 August 2017

10022-10040

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Europe PubMed Central

PMC publication ID

12 August 2017

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Creative Commons Attribution 4.0 International

10 August 2012

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Live-cell imaging of single receptor composition using zero-mode waveguide nanostructures.

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Pharmacological chaperoning of nicotinic acetylcholine receptors reduces the endoplasmic reticulum stress response.

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1 October 2017

Trafficking of alpha4* nicotinic receptors revealed by superecliptic phluorin: effects of a beta4 amyotrophic lateral sclerosis-associated mutation and chronic exposure to nicotine

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1 October 2017

Principles of activation and permeation in an anion-selective Cys-loop receptor

1 reference

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1 October 2017

Neural systems governed by nicotinic acetylcholine receptors: emerging hypotheses

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1 October 2017

Nicotine up-regulates alpha4beta2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning

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Strength in numbers: effects of acceptor abundance on FRET efficiency

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Comparison between whole distribution- and average-based approaches to the determination of fluorescence resonance energy transfer efficiency in ensembles of proteins in living cells

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Förster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins

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GABA transporter function, oligomerization state, and anchoring: correlates with subcellularly resolved FRET

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Nicotine is a selective pharmacological chaperone of acetylcholine receptor number and stoichiometry. Implications for drug discovery.

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Nicotine binding to brain receptors requires a strong cation-pi interaction

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Robust approaches to quantitative ratiometric FRET imaging of CFP/YFP fluorophores under confocal microscopy

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Single-molecule imaging of a fluorescent unnatural amino acid incorporated into nicotinic receptors

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Alpha4 containing nicotinic receptors are positioned to mediate postsynaptic effects on 5-HT neurons in the rat dorsal raphe nucleus.

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Roles of accessory subunits in alpha4beta2(*) nicotinic receptors

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Role of the agonist binding site in up-regulation of neuronal nicotinic alpha4beta2 receptors

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A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries

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Nicotine acts as a pharmacological chaperone to up-regulate human alpha4beta2 acetylcholine receptors

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Nicotine upregulates its own receptors through enhanced intracellular maturation

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Refined structure of the nicotinic acetylcholine receptor at 4A resolution

1 reference

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Alternate stoichiometries of alpha4beta2 nicotinic acetylcholine receptors

1 reference

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Fluorescence resonance energy transfer-based stoichiometry in living cells

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Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes

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Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

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Agonist-induced up-regulation of alpha4beta2 nicotinic acetylcholine receptors in M10 cells: pharmacological and spatial definition

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Human alpha4beta2 acetylcholine receptors formed from linked subunits.

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Ca2+ permeability of the (alpha4)3(beta2)2 stoichiometry greatly exceeds that of (alpha4)2(beta2)3 human acetylcholine receptors.

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Analysis of FRET signals in the presence of free donors and acceptors

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12 December 2020

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Substance P and somatostatin inhibit calcium channels in rat sympathetic neurons via different G protein pathwavs

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10.3390/IJMS130810022

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Europe PubMed Central

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12 August 2017

PMC publication ID

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Europe PubMed Central

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12 August 2017

PubMed publication ID

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Europe PubMed Central

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12 August 2017

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