Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.
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Structural basis for endothelial nitric oxide synthase binding to calmodulinThe importance of intrinsic disorder for protein phosphorylationSite-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor.Calcium in red blood cells-a perilous balance.
P2860
Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.
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2001 nî lūn-bûn
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name
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@en
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@nl
type
label
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@en
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@nl
prefLabel
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@en
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@nl
P2860
P1433
P1476
Phosphorylation of serine resi ...... g domain of human protein 4.1.
@en
P2093
P2860
P304
P356
10.1046/J.1432-1327.2001.02347.X
P407
P577
2001-08-01T00:00:00Z