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Structural principles of distinct assemblies of the human α4β2 nicotinic receptor

Structural principles of distinct assemblies of the human α4β2 nicotinic receptor

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6132059

Structural principles of distinct assemblies of the human α4β2 nicotinic receptor

About this item

Full title

Structural principles of distinct assemblies of the human α4β2 nicotinic receptor

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2018-05, Vol.557 (7704), p.261-265

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Fast chemical communication in the nervous system is mediated by neurotransmitter-gated ion channels. The prototypical member of this class of cell surface receptors is the cation-selective nicotinic acetylcholine receptor. As with most ligand-gated ion channels, nicotinic receptors assemble as oligomers of subunits, usually as hetero-oligomers and...

Alternative Titles

Full title

Structural principles of distinct assemblies of the human α4β2 nicotinic receptor

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6132059

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6132059

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/s41586-018-0081-7

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