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“Replacement of this tyrosine by phenylalanine (Y616F) disabled the auto-phosphorylation activity of Fer and abolished its ability to phosphorylate Stat3.”
“Preferential utilization of glucose-1-phosphate, d-mannitol and l-phenylalanine ; production of 2-hydroxycaproic acid and termination of dimethyl sulphide production were major Fnn response-factors to iron limitation.”
“Exchange of tyrosine residues 421, 466, and 482 for phenylalanine prevented cortactin phosphorylation by hypertonicity and strongly decreased it upon FER overexpression, suggesting that FER targets primarily the same osmo-sensitive tyrosines.”
The Journal of Biological Chemistry • 2000 | View Paper
“Thus, the large benzyl side chain of phenylalanine at position 68 inhibits the rate of ligand movement up to and away from the iron atom but not the final bound state.”
The Journal of biological chemistry • 1975 | View Paper
“The alteration of the environment of the iron atom of cytochrome c by movement of the swinging phenylalanine ring can be described as variable space-filling.”