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Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated...

Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bdd0f03d3f00427785931b54c7c5ab48

Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer

About this item

Full title

Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2024-10, Vol.15 (1), p.9223-12, Article 9223

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Connexin 36 (Cx36) forms interneuronal gap junctions, establishing electrical synapses for rapid synaptic transmission. In disease conditions, inhibiting Cx36 gap junction channels (GJCs) is beneficial, as it prevents abnormal synchronous neuronal firing and apoptotic signal propagation, mitigating seizures and progressive cell death. Here, we pres...

Alternative Titles

Full title

Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_bdd0f03d3f00427785931b54c7c5ab48

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bdd0f03d3f00427785931b54c7c5ab48

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-024-53587-6

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