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Michael R. Hansen

Fox Chase Cancer Center

4

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Amino Acid Substitution at Phe80 of Mammalian Phenylalanine Hydroxylase Destabilizes Both Resting‐State and Activated Conformations Increasing the Population of Intermediates.

2020 The FASEB Journal
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Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium

2019 Journal of Biological Chemistry
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Single-residue variants of phenylalanine hydroxylase help to observe multiple structural isoforms that comprise the structural equilibrium

2018 Acta Crystallographica Section A
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Simulations of the regulatory ACT domain of human phenylalanine hydroxylase (PAH) unveil its mechanism of phenylalanine binding

2018 Journal of Biological Chemistry
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