P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance. (Q41526271)

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18 January 2020

title

P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance (English)

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18 January 2020

1

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18 January 2020

author name string

Lishuang Cao

2

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18 January 2020

Helen E Broomhead

3

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18 January 2020

Laricia Bragg

4

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18 January 2020

William J Wilkinson

5

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18 January 2020

R Alan North

6

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18 January 2020

language of work or name

English

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publication date

19 December 2010

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18 January 2020

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18 January 2020

volume

14

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18 January 2020

issue

1

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18 January 2020

page(s)

17-18

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New structure enlivens interest in P2X receptors.

18 January 2020

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Crystal structure of the ATP-gated P2X(4) ion channel in the closed state

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Gating the pore of P2X receptor channels

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308.

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Ivermectin Interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

A single P-loop glutamate point mutation to either lysine or arginine switches the cation-anion selectivity of the CNGA2 channel

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Pharmacological and biophysical properties of the human P2X5 receptor

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Molecular physiology of P2X receptors

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Two mechanisms for inward rectification of current flow through the purinoceptor P2X2 class of ATP‐gated channels

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Identification of amino acid residues contributing to the pore of a P2X receptor

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3012030

A Domain Contributing to the Ion Channel of ATP-Gated P2X2Receptors Identified by the Substituted Cysteine Accessibility Method

6 June 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21170052

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NN.2705

1 reference

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Dimensions Publication ID

18 January 2020

0 references

1 reference

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18 January 2020

PubMed publication ID

21170052

1 reference