Ca
Amino Acid Sequence
/ genetics
Binding Sites
/ genetics
Calcium
/ metabolism
Calmodulin
/ metabolism
EF Hand Motifs
/ genetics
Fibroblast Growth Factors
/ genetics
Humans
Models, Molecular
NAV1.2 Voltage-Gated Sodium Channel
/ metabolism
Nuclear Magnetic Resonance, Biomolecular
/ methods
Protein Binding
Protein Interaction Domains and Motifs
/ genetics
Voltage-Gated Sodium Channels
/ metabolism
Ca(2+)-dependent interaction
FHF
FRET
NMR
affinity
allostery
biosensor
molecular recognition
protein–protein interaction
thermodynamics
voltage-gated sodium channel
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Historique:
received:
17
12
2020
revised:
15
02
2021
accepted:
23
02
2021
pubmed:
28
2
2021
medline:
31
8
2021
entrez:
27
2
2021
Statut:
ppublish
Résumé
Voltage-gated sodium channels (Na
Identifiants
pubmed: 33639159
pii: S0021-9258(21)00231-3
doi: 10.1016/j.jbc.2021.100458
pmc: PMC8059062
pii:
doi:
Substances chimiques
Calmodulin
0
FGF12 protein, human
0
NAV1.2 Voltage-Gated Sodium Channel
0
Voltage-Gated Sodium Channels
0
Fibroblast Growth Factors
62031-54-3
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100458Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM057001
Pays : United States
Organisme : NINDS NIH HHS
ID : T32 NS045549
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflicts of interest The authors declare that they have no conflicts of interest with the contents of this article.
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