Structural basis of TRPC4 regulation by calmodulin and pharmacological agents.
Animals
Binding Sites
Calmodulin
/ chemistry
HEK293 Cells
Humans
Ligands
Membrane Potentials
Membrane Transport Modulators
/ chemistry
Models, Molecular
Protein Binding
Protein Conformation
Pyridazines
/ chemistry
Sf9 Cells
Structure-Activity Relationship
TRPC Cation Channels
/ chemistry
Xenopus
Zebrafish Proteins
/ chemistry
calmodulin
canonical transient receptor potential channel
cryo-EM
ion channel
modulation
molecular biophysics
none
regulation
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
25 11 2020
25 11 2020
Historique:
received:
01
07
2020
accepted:
23
11
2020
pubmed:
26
11
2020
medline:
17
3
2021
entrez:
25
11
2020
Statut:
epublish
Résumé
Canonical transient receptor potential channels (TRPC) are involved in receptor-operated and/or store-operated Ca
Identifiants
pubmed: 33236980
doi: 10.7554/eLife.60603
pii: 60603
pmc: PMC7735759
doi:
pii:
Substances chimiques
Calmodulin
0
Ligands
0
Membrane Transport Modulators
0
Pyridazines
0
TRPC Cation Channels
0
TRPC4 ion channel
0
Zebrafish Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : TR240
Pays : International
Informations de copyright
© 2020, Vinayagam et al.
Déclaration de conflit d'intérêts
DV, DQ, JY, OS, FM, MS, OH, GN, SR No competing interests declared, MY, ML, GM The author is or was a shareholder of Goldfinch Bio.
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