Log in to save to my catalogue

Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5886804

Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

About this item

Full title

Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2018-04, Vol.556 (7699), p.130-134

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Structures of the voltage-gated and phosphatidylinositol 3,5-bisphosphate-activated mouse two-pore channel TPC1 in apo and ligand-bound states provide insights into the selectivity and gating mechanisms of mammalian two-pore channels.
Structure of a mouse two-pore ion channel
Two-pore channels (TPCs) are organellar voltage-dependent ion chann...

Alternative Titles

Full title

Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5886804

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5886804

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature26139

How to access this item