Sandbox Reserved 1734: Difference between revisions

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== References ==
== References ==
<references/>
<references/>
1. Flydal, M. I.; Alcorlo-Pagés, M.; Johannessen, F. G.; Martínez-Caballero, S.; Skjærven, L.; Fernandez-Leiro, R.; Martinez, A.; Hermoso, J. A. Structure of Full-Length Human Phenylalanine Hydroxylase in Complex with Tetrahydrobiopterin. Proc. Natl. Acad. Sci. U.S.A. 2019, 116 (23), 11229–11234. https://doi.org/10.1073/pnas.1902639116.
1. Gjetting, T.; Petersen, M.; Guldberg, P.; Güttler, F. In Vitro Expression of 34 Naturally Occurring Mutant Variants of Phenylalanine Hydroxylase: Correlation with Metabolic Phenotypes and Susceptibility toward Protein Aggregation. Mol. Genet. Metab 2001, 72 (2), 132–143. https://doi.org/10.1006/mgme.2000.3118.


2. Matthews, D. E. An Overview of Phenylalanine and Tyrosine Kinetics in Humans. J Nutr. 2007 Jun; 137(6 Suppl 1): 1549S–1575S. doi: 10.1093/jn/137.6.1549S
2. Waters, P. J. HowPAH Gene Mutations Cause Hyper-Phenylalaninemia and Why Mechanism Matters: Insights from in Vitro Expression. Hum. Mutat 2003, 21 (4), 357–369. https://doi.org/10.1002/humu.10197.


3. Siltberg-Liberles, J.; Steen, I. H.; Svebak, R. M.; Martinez, A. The Phylogeny of the Aromatic Amino Acid Hydroxylases Revisited by Characterizing Phenylalanine Hydroxylase from Dictyostelium Discoideum. Gene 2008, 427 (1-2), 86–92. https://doi.org/10.1016/j.gene.2008.09.005.
3. Siltberg-Liberles, J.; Steen, I. H.; Svebak, R. M.; Martinez, A. The Phylogeny of the Aromatic Amino Acid Hydroxylases Revisited by Characterizing Phenylalanine Hydroxylase from Dictyostelium Discoideum. Gene 2008, 427 (1-2), 86–92. https://doi.org/10.1016/j.gene.2008.09.005.


4. Fusetti, F.; Erlandsen, H.; Flatmark, T.; Stevens, R. C. Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria. J. Biol. Chem 1998, 273 (27), 16962–16967. https://doi.org/10.1074/jbc.273.27.16962.
4. Flydal, M. I.; Martinez, A. Phenylalanine Hydroxylase: Function, Structure, and Regulation. IUBMB Life 2013, 65 (4), 341–349. https://doi.org/10.1002/iub.1150.


5. Carluccio, C.; Fraternali, F.; Salvatore, F.; Fornili, A.; Zagari, A. Structural Features of the Regulatory ACT Domain of Phenylalanine Hydroxylase. PLoS ONE 2013, 8 (11), e79482. https://doi.org/10.1371/journal.pone.0079482.
5. Carluccio, C.; Fraternali, F.; Salvatore, F.; Fornili, A.; Zagari, A. Structural Features of the Regulatory ACT Domain of Phenylalanine Hydroxylase. PLoS ONE 2013, 8 (11), e79482. https://doi.org/10.1371/journal.pone.0079482.


6. Flydal, M. I.; Martinez, A. Phenylalanine Hydroxylase: Function, Structure, and Regulation. IUBMB Life 2013, 65 (4), 341–349. https://doi.org/10.1002/iub.1150.
6. Flydal, M. I.; Alcorlo-Pagés, M.; Johannessen, F. G.; Martínez-Caballero, S.; Skjærven, L.; Fernandez-Leiro, R.; Martinez, A.; Hermoso, J. A. Structure of Full-Length Human Phenylalanine Hydroxylase in Complex with Tetrahydrobiopterin. Proc. Natl. Acad. Sci. U.S.A. 2019, 116 (23), 11229–11234. https://doi.org/10.1073/pnas.1902639116.


7. Gjetting, T.; Petersen, M.; Guldberg, P.; Güttler, F. In Vitro Expression of 34 Naturally Occurring Mutant Variants of Phenylalanine Hydroxylase: Correlation with Metabolic Phenotypes and Susceptibility toward Protein Aggregation. Mol. Genet. Metab 2001, 72 (2), 132–143. https://doi.org/10.1006/mgme.2000.3118.
7. Scriver, C. R. ThePAH Gene, Phenylketonuria, and a Paradigm Shift. Hum. Mutat 2007, 28 (9), 831–845. https://doi.org/10.1002/humu.20526.


8. Blau, N.; Erlandsen, H. The Metabolic and Molecular Bases of Tetrahydrobiopterin-Responsive Phenylalanine Hydroxylase Deficiency. Mol. Genet. Metab 2004, 82 (2), 101–111. https://doi.org/10.1016/j.ymgme.2004.03.006.
8. Shebl, G.; Ahmed, H.; Kato, A.; Dawoud, H.; Hamza, M.; Haider, A. Detection of Sequence Mutations in Phenylalanine Hydroxylase (PAH) Gene Isolated from Egyptian Phenylketonuria (PKU) Patients. Egypt. J. Exp. Biol. (Bot.) 2019, 15 (2), 295. https://doi.org/10.5455/egyjebb.20190804010102.


9. Scriver, C. R. ThePAH Gene, Phenylketonuria, and a Paradigm Shift. Hum. Mutat 2007, 28 (9), 831–845. https://doi.org/10.1002/humu.20526.
9. Matthews, D. E. An Overview of Phenylalanine and Tyrosine Kinetics in Humans. J Nutr. 2007 Jun; 137(6 Suppl 1): 1549S–1575S. doi: 10.1093/jn/137.6.1549S


10. Waters, P. J. HowPAH Gene Mutations Cause Hyper-Phenylalaninemia and Why Mechanism Matters: Insights from in Vitro Expression. Hum. Mutat 2003, 21 (4), 357–369. https://doi.org/10.1002/humu.10197.
10. Fusetti, F.; Erlandsen, H.; Flatmark, T.; Stevens, R. C. Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria. J. Biol. Chem 1998, 273 (27), 16962–16967. https://doi.org/10.1074/jbc.273.27.16962.


11. Shebl, G.; Ahmed, H.; Kato, A.; Dawoud, H.; Hamza, M.; Haider, A. Detection of Sequence Mutations in Phenylalanine Hydroxylase (PAH) Gene Isolated from Egyptian Phenylketonuria (PKU) Patients. Egypt. J. Exp. Biol. (Bot.) 2019, 15 (2), 295. https://doi.org/10.5455/egyjebb.20190804010102.
11. Blau, N.; Erlandsen, H. The Metabolic and Molecular Bases of Tetrahydrobiopterin-Responsive Phenylalanine Hydroxylase Deficiency. Mol. Genet. Metab 2004, 82 (2), 101–111. https://doi.org/10.1016/j.ymgme.2004.03.006.
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