Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors. (Q40773632)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11665562%20AND%20SRC:MED&resulttype=core&format=json

13 November 2019

title

Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11665562%20AND%20SRC:MED&resulttype=core&format=json

G protein-coupled receptor

13 November 2019

main subject

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1

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13 November 2019

Lei Shi

series ordinal

2

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13 November 2019

author name string

George Liapakis

series ordinal

3

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13 November 2019

language of work or name

English

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publication date

1 January 2002

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13 November 2019

published in

Methods in Enzymology

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13 November 2019

volume

343

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13 November 2019

page(s)

137-156

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Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation.

13 November 2019

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Use of site-directed fluorescence labeling to study proximity relationships in the lactose permease of Escherichia coli

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Substituted-cysteine accessibility method

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Multiple residues specify external tetraethylammonium blockade in voltage-gated potassium channels

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Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method

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The fourth transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle

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Structure and function of G protein-coupled receptors

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Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates

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Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate

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Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor

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Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11665562%20AND%20SRC:MED&resulttype=core&format=json

13 November 2019

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