Structural and electrostatic properties of the 5-HT3 receptor pore revealed by substituted cysteine accessibility mutagenesis. (Q42659707)

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11 November 2019

title

Structural and electrostatic properties of the 5-HT3 receptor pore revealed by substituted cysteine accessibility mutagenesis (English)

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11 November 2019

3

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11 November 2019

author name string

Reeves DC

series ordinal

1

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11 November 2019

Goren EN

series ordinal

2

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Lummis SC

series ordinal

4

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11 November 2019

language of work or name

English

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publication date

13 September 2001

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Journal of Biological Chemistry

11 November 2019

published in

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11 November 2019

volume

276

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11 November 2019

issue

45

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11 November 2019

page(s)

42035-42042

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Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel

11 November 2019

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State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor. Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the alpha subunit

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Antibodies against the extracellular domain of the 5-HT3 receptor label both native and recombinant receptors.

21 January 2018

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

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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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Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit.

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Conversion of the ion selectivity of the 5-HT(3a) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M106066200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11557761%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

1 reference