Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer ; volume:15 ; number:1 ; day:25 ; month:10 ; year:2024 ; pages:1-12 ; date:12.2024
Nature Communications ; 15, Heft 1 (25.10.2024), 1-12, 12.2024
- Creator
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Cho, Hwa-Jin
Chung, Dong Kyu
Lee, Hyung Ho
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-024-53587-6
- URN
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urn:nbn:de:101:1-2501152116490.536116841094
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:20 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Cho, Hwa-Jin
- Chung, Dong Kyu
- Lee, Hyung Ho
- SpringerLink (Online service)
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Structural study of UFL1‐UFC1 interaction uncovers the role of UFL1 N‐terminal helix in ufmylation
Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies
Helix-Helix-Wechselwirkungen in Tyrosinkinaserezeptoren
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Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
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Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy
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Bergschnecke (Helix cricetorum). Steinpicker (Helix lapicida).
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Cas12a is governed in its Activity and Conformational Transitions by the Two Interplaying Key Elements Helix 1 and Bridge Helix
Photoresponsive Helical Foldamers: Conformational Control Through Double Helix Formation and Light‐Induced Protonation
Structural study of UFL1‐UFC1 interaction uncovers the role of UFL1 N‐terminal helix in ufmylation
Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies
Helix-Helix-Wechselwirkungen in Tyrosinkinaserezeptoren
Helix
Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
Conformational flexibility of the protein insertase BamA in the native asymmetric bilayer elucidated by ESR spectroscopy
Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy
Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy