Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite
binding affinity
inhibitor development
protein stability
protein structure
target activation
Journal
FASEB bioAdvances
ISSN: 2573-9832
Titre abrégé: FASEB Bioadv
Pays: United States
ID NLM: 101733210
Informations de publication
Date de publication:
Aug 2020
Aug 2020
Historique:
received:
24
03
2020
revised:
24
03
2020
accepted:
16
06
2020
entrez:
22
8
2020
pubmed:
22
8
2020
medline:
22
8
2020
Statut:
epublish
Résumé
Calmodulin (CaM), the key calcium sensor of eukaryotic cells regulating a great number of target proteins, belongs to the most conserved proteins. We compared function and properties of CaMs from two evolutionarily distant species, the human (
Identifiants
pubmed: 32821880
doi: 10.1096/fba.2020-00013
pii: FBA21150
pmc: PMC7429351
doi:
Types de publication
Journal Article
Langues
eng
Pagination
489-505Informations de copyright
© 2020 The Authors. FASEB BioAdvances published by The Federation of American Societies for Experimental Biology.
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