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Volumn 12, Issue 22, 2012, Pages 2534-2545

Phenylalanine hydroxylase misfolding and pharmacological chaperones

Author keywords

Folding aids; High throughput screening; Pharmachaperones; Pharmacophore modeling; Phenylalanine hydroxylase

Indexed keywords

CHAPERONE; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN; TRYPTOPHAN HYDROXYLASE; TYROSINE 3 MONOOXYGENASE; UBIQUITIN;

EID: 84874929066     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026611212220008     Document Type: Article
Times cited : (55)

References (108)
  • 3
    • 77955887072 scopus 로고    scopus 로고
    • Phenylketonuria: A 21st century perspective
    • van Spronsen, F. J., Phenylketonuria: a 21st century perspective. Nat. Rev. Endocrinol., 2010, 6, 509-514.
    • (2010) Nat. Rev. Endocrinol , vol.6 , pp. 509-514
    • van Spronsen, F.J.1
  • 4
    • 72249106379 scopus 로고    scopus 로고
    • Pathogenesis of cognitive dysfunction in phenylketonuria: Review of hypotheses
    • de Groot, M. J.; Hoeksma, M.; Blau, N.; Reijngoud, D. J.; van Spronsen, F. J., Pathogenesis of cognitive dysfunction in phenylketonuria: review of hypotheses. Mol. Genet. Metab., 2010, 99 Suppl 1, S86-S89.
    • (2010) Mol. Genet. Metab , vol.99 , Issue.SUPPL. 1
    • de Groot, M.J.1    Hoeksma, M.2    Blau, N.3    Reijngoud, D.J.4    van Spronsen, F.J.5
  • 5
    • 34848850451 scopus 로고    scopus 로고
    • The PAH gene, phenylketonuria, and a paradigm shift
    • Scriver, C. R., The PAH gene, phenylketonuria, and a paradigm shift. Hum. Mutat., 2007, 28, 831-845.
    • (2007) Hum. Mutat , vol.28 , pp. 831-845
    • Scriver, C.R.1
  • 7
    • 75449123150 scopus 로고
    • A Simple Phenylalanine Method for Detecting Phenylketonuria in Large Populations of Newborn Infants
    • Guthrie, R.; Susi, A., A Simple Phenylalanine Method for Detecting Phenylketonuria in Large Populations of Newborn Infants. Pediatrics, 1963, 32, 338-343.
    • (1963) Pediatrics , vol.32 , pp. 338-343
    • Guthrie, R.1    Susi, A.2
  • 9
    • 77957237994 scopus 로고    scopus 로고
    • Suboptimal outcomes in patients with PKU treated early with diet alone: Revisiting the evidence
    • Enns, G. M.; Koch, R.; Brumm, V.; Blakely, E.; Suter, R.; Jurecki, E., Suboptimal outcomes in patients with PKU treated early with diet alone: revisiting the evidence. Mol. Genet. Metab., 2010, 101, 99-109.
    • (2010) Mol. Genet. Metab , vol.101 , pp. 99-109
    • Enns, G.M.1    Koch, R.2    Brumm, V.3    Blakely, E.4    Suter, R.5    Jurecki, E.6
  • 10
    • 0000134296 scopus 로고    scopus 로고
    • Hyperphenylalaninemia:Phenylalanine hydroxylase defciency
    • 8th ed.; Scriver, C. R.; Beaudet, A. L.; Valle, D.; Sly, W. S., Eds. McGraw-Hill: New York
    • Scriver, C. R.; Kaufman, S., Hyperphenylalaninemia:phenylalanine hydroxylase defciency. In: The Metabolic and Molecular bases of Inherited Disease, 8th ed.; Scriver, C. R.; Beaudet, A. L.; Valle, D.; Sly, W. S., Eds. McGraw-Hill: New York, 2001; pp 1667-1724.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 1667-1724
    • Scriver, C.R.1    Kaufman, S.2
  • 11
    • 80051675515 scopus 로고    scopus 로고
    • Tetrahydrobiopterin: Biochemistry and pathophysiology
    • Werner, E. R.; Blau, N.; Thony, B., Tetrahydrobiopterin: biochemistry and pathophysiology. Biochem. J., 2011, 438, 397-414.
    • (2011) Biochem. J , vol.438 , pp. 397-414
    • Werner, E.R.1    Blau, N.2    Thony, B.3
  • 13
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F., Mechanism of aromatic amino acid hydroxylation. Biochemistry, 2003, 42, 14083-14091.
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 14
    • 0001749787 scopus 로고    scopus 로고
    • Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • Flatmark, T.; Stevens, R. C., Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms. Chem. Rev., 1999, 99, 2137-2160.
    • (1999) Chem. Rev , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 15
    • 33847222673 scopus 로고    scopus 로고
    • Selectivity and affinity determinants for ligand binding to the aromatic amino Acid hydroxylases
    • Teigen, K.; McKinney, J. A.; Haavik, J.; Martinez, A., Selectivity and affinity determinants for ligand binding to the aromatic amino Acid hydroxylases. Curr. Med. Chem., 2007, 14, 455-467.
    • (2007) Curr. Med. Chem , vol.14 , pp. 455-467
    • Teigen, K.1    McKinney, J.A.2    Haavik, J.3    Martinez, A.4
  • 16
    • 75549091083 scopus 로고    scopus 로고
    • Tryptophan hydroxylase as novel target for the treatment of depressive disorders
    • Matthes, S.; Mosienko, V.; Bashammakh, S.; Alenina, N.; Bader, M., Tryptophan hydroxylase as novel target for the treatment of depressive disorders. Pharmacology, 2010, 85, 95-109.
    • (2010) Pharmacology , vol.85 , pp. 95-109
    • Matthes, S.1    Mosienko, V.2    Bashammakh, S.3    Alenina, N.4    Bader, M.5
  • 18
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • Koehntop, K. D.; Emerson, J. P.; Que, L., Jr., The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J.Biol. Inorg. Chem., 2005, 10, 87-93.
    • (2005) J.Biol. Inorg. Chem , vol.10 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 19
    • 0032479302 scopus 로고    scopus 로고
    • Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria
    • 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, 16962-16967.
    • (1998) J. Biol. Chem , vol.273 , pp. 16962-16967
    • Fusetti, F.1    Erlandsen, H.2    Flatmark, T.3    Stevens, R.C.4
  • 20
    • 0031010420 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases
    • Goodwill, K. E.; Sabatier, C.; Marks, C.; Raag, R.; Fitzpatrick, P. F.; Stevens, R. C., Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases. Nat. Struct. Biol., 1997, 4, 578-585.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 578-585
    • Goodwill, K.E.1    Sabatier, C.2    Marks, C.3    Raag, R.4    Fitzpatrick, P.F.5    Stevens, R.C.6
  • 21
    • 0031303781 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria
    • Erlandsen, H.; Fusetti, F.; Martínez, A.; Hough, E.; Flatmark, T.; Stevens, R. C., Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat. Struct. Biol., 1997, 4, 995-1000.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 995-1000
    • Erlandsen, H.1    Fusetti, F.2    Martínez, A.3    Hough, E.4    Flatmark, T.5    Stevens, R.C.6
  • 23
    • 0033521234 scopus 로고    scopus 로고
    • The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: Implications for the catalytic mechanism
    • Teigen, K.; Frøystein, N. Å.; Martínez, A., The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism. J. Mol. Biol., 1999, 294, 807-823.
    • (1999) J. Mol. Biol , vol.294 , pp. 807-823
    • Teigen, K.1    Frøystein, N.Å.2    Martínez, A.3
  • 25
    • 0034093759 scopus 로고    scopus 로고
    • Crystal Structure and Site-Specific Mutagenesis of Pterin-Bound Human Phenylalanine Hydroxylase
    • Erlandsen, H.; Bjørgo, E.; Flatmark, T.; Stevens, R. C., Crystal Structure and Site-Specific Mutagenesis of Pterin-Bound Human Phenylalanine Hydroxylase. Biochemistry, 2000, 39, 2208-2217.
    • (2000) Biochemistry , vol.39 , pp. 2208-2217
    • Erlandsen, H.1    Bjørgo, E.2    Flatmark, T.3    Stevens, R.C.4
  • 26
    • 0142106379 scopus 로고    scopus 로고
    • 2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: Substrate specificity and molecular motions related to substrate binding
    • Andersen, O. A.; Stokka, A. J.; Flatmark, T.; Hough, E., 2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding. J. Mol. Biol., 2003, 333, 747-757.
    • (2003) J. Mol. Biol , vol.333 , pp. 747-757
    • Andersen, O.A.1    Stokka, A.J.2    Flatmark, T.3    Hough, E.4
  • 27
    • 0032711431 scopus 로고    scopus 로고
    • The structural basis of phenylketonuria
    • Erlandsen, H.; Stevens, R. C., The structural basis of phenylketonuria. Mol. Genet. Metab., 1999, 68, 103-125.
    • (1999) Mol. Genet. Metab , vol.68 , pp. 103-125
    • Erlandsen, H.1    Stevens, R.C.2
  • 28
    • 35348876038 scopus 로고    scopus 로고
    • Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases
    • Pey, A. L.; Stricher, F.; Serrano, L.; Martinez, A., Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases. Am. J. Hum. Genet., 2007, 81, 1006-1024.
    • (2007) Am. J. Hum. Genet , vol.81 , pp. 1006-1024
    • Pey, A.L.1    Stricher, F.2    Serrano, L.3    Martinez, A.4
  • 29
    • 77957375684 scopus 로고    scopus 로고
    • The Aromatic Amino Acid Hydroxylase Mechanism: A Perspective from Computational Chemistry
    • Olsson, E.; Teigen, K.; Martinez, A.; Jensen, V. R., The Aromatic Amino Acid Hydroxylase Mechanism: A Perspective from Computational Chemistry. Adv. Inorg. Chem., 2010, 62, 437-500.
    • (2010) Adv. Inorg. Chem , vol.62 , pp. 437-500
    • Olsson, E.1    Teigen, K.2    Martinez, A.3    Jensen, V.R.4
  • 32
    • 84857812487 scopus 로고    scopus 로고
    • Allosteric regulation of phenylalanine hydroxylase
    • Fitzpatrick, P. F., Allosteric regulation of phenylalanine hydroxylase. Arch. Biochem. Biophys., 2012, 519, 194-201.
    • (2012) Arch. Biochem. Biophys , vol.519 , pp. 194-201
    • Fitzpatrick, P.F.1
  • 33
    • 0028853230 scopus 로고
    • Coordinate regulation of tetrahydrobiopterin turnover and phenylalanine hydroxylase activity in rat liver cells
    • Mitnaul, L. J.; Shiman, R., Coordinate regulation of tetrahydrobiopterin turnover and phenylalanine hydroxylase activity in rat liver cells. Proc. Natl. Acad. Sci. U S A, 1995, 92, 885-889.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 885-889
    • Mitnaul, L.J.1    Shiman, R.2
  • 34
    • 6444235533 scopus 로고    scopus 로고
    • Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase
    • Pey, A. L.; Thórólfsson, M.; Teigen, K.; Ugarte, M.; Martínez, A., Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase. J. Am. Chem. Soc., 2004, 126, 13670-13678.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 13670-13678
    • Pey, A.L.1    Thórólfsson, M.2    Teigen, K.3    Ugarte, M.4    Martínez, A.5
  • 37
    • 0037240146 scopus 로고    scopus 로고
    • How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: Insights from in vitro expression
    • Waters, P. J., How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: insights from in vitro expression. Hum. Mutat., 2003, 21, 357-369.
    • (2003) Hum. Mutat , vol.21 , pp. 357-369
    • Waters, P.J.1
  • 38
    • 78650281988 scopus 로고
    • Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation
    • Leandro, J.; Simonsen, N.; Saraste, J.; Leandro, P.; Flatmark, T., Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation. Biochim. Biophys. Acta, 2011, 1812, 106-120.
    • (1812) Biochim. Biophys. Acta , vol.2011 , pp. 106-120
    • Leandro, J.1    Simonsen, N.2    Saraste, J.3    Leandro, P.4    Flatmark, T.5
  • 39
    • 84866276492 scopus 로고    scopus 로고
    • The mechanism of BH(4) -responsive hyperphenylalaninemia - as it occurs in the ENU1/2 genetic mouse model
    • Sarkissian, C. N.; Ying, M.; Scherer, T.; Thony, B.; Martinez, A., The mechanism of BH(4) -responsive hyperphenylalaninemia - as it occurs in the ENU1/2 genetic mouse model. Hum. Mutat., 2012, 33(10): 1464-1473.
    • (2012) Hum. Mutat , vol.33 , Issue.10 , pp. 1464-1473
    • Sarkissian, C.N.1    Ying, M.2    Scherer, T.3    Thony, B.4    Martinez, A.5
  • 40
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitin-mediated recognition and beyond
    • Kraft, C.; Peter, M.; Hofmann, K., Selective autophagy: ubiquitin-mediated recognition and beyond. Nat. Cell. Biol., 2010, 12, 836-841.
    • (2010) Nat. Cell. Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 41
    • 33645098770 scopus 로고    scopus 로고
    • Administration-route and gender-independent long-term therapeutic correction of phenylketonuria (PKU) in a mouse model by recombinant adeno-associated virus 8 pseudotyped vector-mediated gene transfer
    • Ding, Z.; Georgiev, P.; Thony, B., Administration-route and gender-independent long-term therapeutic correction of phenylketonuria (PKU) in a mouse model by recombinant adeno-associated virus 8 pseudotyped vector-mediated gene transfer. Gene Ther., 2006, 13, 587-593.
    • (2006) Gene Ther , vol.13 , pp. 587-593
    • Ding, Z.1    Georgiev, P.2    Thony, B.3
  • 42
    • 41149168735 scopus 로고    scopus 로고
    • Correction of murine PKU following AAV-mediated intramuscular expression of a complete phenylalanine hydroxylating system
    • Ding, Z.; Harding, C. O.; Rebuffat, A.; Elzaouk, L.; Wolff, J. A.; Thony, B., Correction of murine PKU following AAV-mediated intramuscular expression of a complete phenylalanine hydroxylating system. Mol. Therapy, 2008, 16, 673-681.
    • (2008) Mol. Therapy , vol.16 , pp. 673-681
    • Ding, Z.1    Harding, C.O.2    Rebuffat, A.3    Elzaouk, L.4    Wolff, J.A.5    Thony, B.6
  • 45
    • 82455199281 scopus 로고    scopus 로고
    • Evaluation of orally administered PEGylated phenylalanine ammonia lyase in mice for the treatment of Phenylketonuria
    • Sarkissian, C. N.; Kang, T. S.; Gamez, A.; Scriver, C. R.; Stevens, R. C., Evaluation of orally administered PEGylated phenylalanine ammonia lyase in mice for the treatment of Phenylketonuria. Mol. Genet. Metab., 2011, 104, 249-254.
    • (2011) Mol. Genet. Metab , vol.104 , pp. 249-254
    • Sarkissian, C.N.1    Kang, T.S.2    Gamez, A.3    Scriver, C.R.4    Stevens, R.C.5
  • 47
    • 72249098974 scopus 로고    scopus 로고
    • Future treatment strategies in phenylketonuria
    • van Spronsen, F. J.; Enns, G. M., Future treatment strategies in phenylketonuria. Mol. Genet. Metab., 2010, 99 Suppl 1, S90-S95.
    • (2010) Mol. Genet. Metab , vol.99 , Issue.SUPPL. 1
    • van Spronsen, F.J.1    Enns, G.M.2
  • 49
    • 79960348053 scopus 로고    scopus 로고
    • Pseudoexon exclusion by antisense therapy in 6-pyruvoyl-tetrahydropterin synthase deficiency
    • Epub a head of print
    • Brasil, S.; Viecelli, H. M.; Meili, D.; Rassi, A.; Desviat, L. R.; Perez, B.; Ugarte, M.; Thony, B., Pseudoexon exclusion by antisense therapy in 6-pyruvoyl-tetrahydropterin synthase deficiency. Hum. Mutat., 2011, [Epub a head of print].
    • (2011) Hum. Mutat
    • Brasil, S.1    Viecelli, H.M.2    Meili, D.3    Rassi, A.4    Desviat, L.R.5    Perez, B.6    Ugarte, M.7    Thony, B.8
  • 52
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B.; Weissman, J.; Horwich, A., Molecular chaperones and protein quality control. Cell, 2006, 125, 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 53
    • 84856323688 scopus 로고    scopus 로고
    • Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    • Kriegenburg, F.; Ellgaard, L.; Hartmann-Petersen, R., Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. The FEBS journal, 2012, 279, 532-542.
    • (2012) The FEBS Journal , vol.279 , pp. 532-542
    • Kriegenburg, F.1    Ellgaard, L.2    Hartmann-Petersen, R.3
  • 54
  • 55
    • 74249108175 scopus 로고    scopus 로고
    • Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases
    • Brandt, G. E.; Blagg, B. S., Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases. Curr. Top. Med. Chem., 2009, 9, 1447-1461.
    • (2009) Curr. Top. Med. Chem , vol.9 , pp. 1447-1461
    • Brandt, G.E.1    Blagg, B.S.2
  • 56
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen, F. E.; Kelly, J. W., Therapeutic approaches to protein-misfolding diseases. Nature, 2003, 426, 905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 58
    • 0034978522 scopus 로고    scopus 로고
    • Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system
    • Leandro, P.; Lechner, M. C.; Tavares de Almeida, I.; Konecki, D., Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system. Mol. Genet. Metab., 2001, 73, 173-178.
    • (2001) Mol. Genet. Metab , vol.73 , pp. 173-178
    • Leandro, P.1    Lechner, M.C.2    de Tavares, A.I.3    Konecki, D.4
  • 59
    • 55949106049 scopus 로고    scopus 로고
    • Modulation of the activity of newly synthesized human phenylalanine hydroxylase mutant proteins by low-molecular-weight compounds
    • Nascimento, C.; Leandro, J.; Tavares de Almeida, I.; Leandro, P., Modulation of the activity of newly synthesized human phenylalanine hydroxylase mutant proteins by low-molecular-weight compounds. Protein J., 2008, 27, 392-400.
    • (2008) Protein J , vol.27 , pp. 392-400
    • Nascimento, C.1    Leandro, J.2    de Tavares, A.I.3    Leandro, P.4
  • 60
    • 85047683541 scopus 로고    scopus 로고
    • Chemical chaperones: A pharmacological strategy for disorders of protein folding and trafficking
    • Perlmutter, D. H., Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking. Pediatr. Res., 2002, 52, 832-836.
    • (2002) Pediatr. Res , vol.52 , pp. 832-836
    • Perlmutter, D.H.1
  • 61
    • 3042540232 scopus 로고    scopus 로고
    • Pharmacological chaperones: Potential treatment for conformational diseases
    • Bernier, V.; Lagace, M.; Bichet, D. G.; Bouvier, M., Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocrinol. Metab., 2004, 15, 222-228.
    • (2004) Trends Endocrinol. Metab , vol.15 , pp. 222-228
    • Bernier, V.1    Lagace, M.2    Bichet, D.G.3    Bouvier, M.4
  • 62
    • 34547105186 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones as new therapeutic agents
    • Loo, T. W.; Clarke, D. M., Chemical and pharmacological chaperones as new therapeutic agents. Expert Rev. Mol. Med., 2007, 9, 1-18.
    • (2007) Expert Rev. Mol. Med , vol.9 , pp. 1-18
    • Loo, T.W.1    Clarke, D.M.2
  • 64
    • 37349013379 scopus 로고    scopus 로고
    • A counterintuitive approach to treat enzyme deficiencies: Use of enzyme inhibitors for restoring mutant enzyme activity
    • Fan, J. Q., A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity. Biol. Chem., 2008, 389, 1-11.
    • (2008) Biol. Chem , vol.389 , pp. 1-11
    • Fan, J.Q.1
  • 67
    • 82755189438 scopus 로고    scopus 로고
    • Diagnosis, classification, and genetics of phenylketonuria and tetrahydrobiopterin (BH4) deficiencies
    • Blau, N.; Hennermann, J. B.; Langenbeck, U.; Lichter-Konecki, U., Diagnosis, classification, and genetics of phenylketonuria and tetrahydrobiopterin (BH4) deficiencies. Mol. Genet. Metab., 2011, 104 Suppl: S2-S9.
    • (2011) Mol. Genet. Metab , vol.104 , Issue.SUPPL.
    • Blau, N.1    Hennermann, J.B.2    Langenbeck, U.3    Lichter-Konecki, U.4
  • 68
    • 34547697475 scopus 로고    scopus 로고
    • Efficacy of sapropterin dihydrochloride (tetrahydrobiopterin, 6R-BH4) for reduction of phenylalanine concentration in patients with phenylketonuria: A phase III randomised placebo-controlled study
    • Levy, H. L.; Milanowski, A.; Chakrapani, A.; Cleary, M.; Lee, P.; Trefz, F. K.; Whitley, C. B.; Feillet, F.; Feigenbaum, A. S.; Bebchuk, J. D.; Christ-Schmidt, H.; Dorenbaum, A., Efficacy of sapropterin dihydrochloride (tetrahydrobiopterin, 6R-BH4) for reduction of phenylalanine concentration in patients with phenylketonuria: a phase III randomised placebo-controlled study. Lancet, 2007, 370, 504-510.
    • (2007) Lancet , vol.370 , pp. 504-510
    • Levy, H.L.1    Milanowski, A.2    Chakrapani, A.3    Cleary, M.4    Lee, P.5    Trefz, F.K.6    Whitley, C.B.7    Feillet, F.8    Feigenbaum, A.S.9    Bebchuk, J.D.10    Christ-Schmidt, H.11    Dorenbaum, A.12
  • 70
    • 4744342508 scopus 로고    scopus 로고
    • Wild-type phenylalanine hydroxylase activity is enhanced by tetrahydrobiopterin supplementation in vivo: An implication for therapeutic basis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency
    • Kure, S.; Sato, K.; Fujii, K.; Aoki, Y.; Suzuki, Y.; Kato, S.; Matsubara, Y., Wild-type phenylalanine hydroxylase activity is enhanced by tetrahydrobiopterin supplementation in vivo: an implication for therapeutic basis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Mol. Genet. Metab.urano, 2004, 83, 150-156.
    • (2004) Mol. Genet. Metab.urano , vol.83 , pp. 150-156
    • Kure, S.1    Sato, K.2    Fujii, K.3    Aoki, Y.4    Suzuki, Y.5    Kato, S.6    Matsubara, Y.7
  • 71
    • 0028158628 scopus 로고
    • PHD, an automatic mail server for protein structure prediction
    • Rost, B.; Sander, C.; Schneider, R., PHD, an automatic mail server for protein structure prediction. Comput. Appl. Biosci., 1994, 10, 53-60.
    • (1994) Comput. Appl. Biosci , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 72
    • 33745653140 scopus 로고    scopus 로고
    • Molecular mechanism for pterin-mediated inactivation of tyrosine hydroxylase: Formation of insoluble aggregates of tyrosine hydroxylase
    • Urano, F.; Hayashi, N.; Arisaka, F.; Kurita, H.; Murata, S.; Ichinose, H., Molecular mechanism for pterin-mediated inactivation of tyrosine hydroxylase: formation of insoluble aggregates of tyrosine hydroxylase. J. Biochem. (Tokyo), 2006, 139, 625-635.
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 625-635
    • Urano, F.1    Hayashi, N.2    Arisaka, F.3    Kurita, H.4    Murata, S.5    Ichinose, H.6
  • 74
    • 33846622066 scopus 로고    scopus 로고
    • Ligand effects on protein thermodynamic stability
    • Sanchez-Ruiz, J. M., Ligand effects on protein thermodynamic stability. Biophys. Chem., 2007, 126, 43-49.
    • (2007) Biophys. Chem , vol.126 , pp. 43-49
    • Sanchez-Ruiz, J.M.1
  • 75
    • 33847032037 scopus 로고    scopus 로고
    • High-throughput screening for human lysosomal beta-N-Acetyl hexosaminidase inhibitors acting as pharmacological chaperones
    • Tropak, M. B.; Blanchard, J. E.; Withers, S. G.; Brown, E. D.; Mahuran, D., High-throughput screening for human lysosomal beta-N-Acetyl hexosaminidase inhibitors acting as pharmacological chaperones. Chem. Biol., 2007, 14, 153-164.
    • (2007) Chem. Biol , vol.14 , pp. 153-164
    • Tropak, M.B.1    Blanchard, J.E.2    Withers, S.G.3    Brown, E.D.4    Mahuran, D.5
  • 76
    • 70350347721 scopus 로고    scopus 로고
    • What are pharmacological chaperones and why are they interesting
    • Ringe, D.; Petsko, G. A., What are pharmacological chaperones and why are they interesting? J. Biol., 2009, 8, 80.
    • (2009) J. Biol , vol.8 , pp. 80
    • Ringe, D.1    Petsko, G.A.2
  • 77
    • 77449098166 scopus 로고    scopus 로고
    • Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics
    • Parenti, G., Treating lysosomal storage diseases with pharmacological chaperones: from concept to clinics. EMBO Mol. Med., 2009, 1, 268-279.
    • (2009) EMBO Mol. Med , vol.1 , pp. 268-279
    • Parenti, G.1
  • 78
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • Valenzano, K. J.; Khanna, R.; Powe, A. C.; Boyd, R.; Lee, G.; Flanagan, J. J.; Benjamin, E. R., Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders. Assay Drug. Dev. Technol., 2011, 9, 213-235.
    • (2011) Assay Drug. Dev. Technol , vol.9 , pp. 213-235
    • Valenzano, K.J.1    Khanna, R.2    Powe, A.C.3    Boyd, R.4    Lee, G.5    Flanagan, J.J.6    Benjamin, E.R.7
  • 79
    • 79951829938 scopus 로고    scopus 로고
    • Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR
    • Sampson, H. M.; Robert, R.; Liao, J.; Matthes, E.; Carlile, G. W.; Hanrahan, J. W.; Thomas, D. Y., Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR. Chem. Biol., 2011, 18, 231-242.
    • (2011) Chem. Biol , vol.18 , pp. 231-242
    • Sampson, H.M.1    Robert, R.2    Liao, J.3    Matthes, E.4    Carlile, G.W.5    Hanrahan, J.W.6    Thomas, D.Y.7
  • 80
    • 84856816223 scopus 로고    scopus 로고
    • Effects of cellular, chemical, and pharmacological chaperones on the rescue of a trafficking-defective mutant of the ATP-binding cassette transporter proteins ABCB1/ABCB4
    • Gautherot, J.; Durand-Schneider, A. M.; Delautier, D.; Delaunay, J. L.; Rada, A.; Gabillet, J.; Housset, C.; Maurice, M.; Ait-Slimane, T., Effects of cellular, chemical, and pharmacological chaperones on the rescue of a trafficking-defective mutant of the ATP-binding cassette transporter proteins ABCB1/ABCB4. J. Biol. Chem., 2012, 287, 5070-5078.
    • (2012) J. Biol. Chem , vol.287 , pp. 5070-5078
    • Gautherot, J.1    Durand-Schneider, A.M.2    Delautier, D.3    Delaunay, J.L.4    Rada, A.5    Gabillet, J.6    Housset, C.7    Maurice, M.8    Ait-Slimane, T.9
  • 81
    • 84859907268 scopus 로고    scopus 로고
    • Discovery and structural development of small molecules that enhance transport activity of bile salt export pump mutant associated with progressive familial intrahepatic cholestasis type 2
    • Misawa, T.; Hayashi, H.; Sugiyama, Y.; Hashimoto, Y., Discovery and structural development of small molecules that enhance transport activity of bile salt export pump mutant associated with progressive familial intrahepatic cholestasis type 2. Bioorg. Med. Chem., 2012, 20(9): 2940-2949.
    • (2012) Bioorg. Med. Chem , vol.20 , Issue.9 , pp. 2940-2949
    • Misawa, T.1    Hayashi, H.2    Sugiyama, Y.3    Hashimoto, Y.4
  • 82
    • 77953390645 scopus 로고    scopus 로고
    • Overview of computational methods employed in early-stage drug discovery
    • Skjevik, A. A.; Teigen, K.; Martinez, A., Overview of computational methods employed in early-stage drug discovery. Fut. Med. Chem., 2009, 1, 49-63.
    • (2009) Fut. Med. Chem , vol.1 , pp. 49-63
    • Skjevik, A.A.1    Teigen, K.2    Martinez, A.3
  • 84
    • 77954818699 scopus 로고    scopus 로고
    • Pharmacophore modeling and applications in drug discovery: Challenges and recent advances
    • Yang, S. Y., Pharmacophore modeling and applications in drug discovery: challenges and recent advances. Drug Discov. Today, 2010, 15, 444-450.
    • (2010) Drug Discov. Today , vol.15 , pp. 444-450
    • Yang, S.Y.1
  • 85
    • 48249108690 scopus 로고    scopus 로고
    • A high-throughput screening method for small-molecule pharmacologic chaperones of misfolded rhodopsin. Invest
    • Noorwez, S. M.; Ostrov, D. A.; McDowell, J. H.; Krebs, M. P.; Kaushal, S., A high-throughput screening method for small-molecule pharmacologic chaperones of misfolded rhodopsin. Invest. Ophthalmol. Vis. Sci., 2008, 49, 3224-3230.
    • (2008) Ophthalmol. Vis. Sci , vol.49 , pp. 3224-3230
    • Noorwez, S.M.1    Ostrov, D.A.2    McDowell, J.H.3    Krebs, M.P.4    Kaushal, S.5
  • 88
    • 0001008140 scopus 로고    scopus 로고
    • Glossary of Terms Used in Medicinal Chemistry (IUPAC Recommendations 1997)
    • Wermuth, C.-G.; Ganellin, C. R.; Lindberg, P.; Mitscher, L. A., Glossary of Terms Used in Medicinal Chemistry (IUPAC Recommendations 1997). Annu. Rep. Med. Chem., 1998, 33, 385-395.
    • (1998) Annu. Rep. Med. Chem , vol.33 , pp. 385-395
    • Wermuth, C.-G.1    Ganellin, C.R.2    Lindberg, P.3    Mitscher, L.A.4
  • 89
    • 44349144497 scopus 로고    scopus 로고
    • Pharmacophore-based virtual screening
    • Sun, H., Pharmacophore-based virtual screening. Curr. Med. Chem., 2008, 15, 1018-1024.
    • (2008) Curr. Med. Chem , vol.15 , pp. 1018-1024
    • Sun, H.1
  • 90
    • 70349482953 scopus 로고    scopus 로고
    • Novel trends in high-throughput screening
    • Mayr, L. M.; Bojanic, D., Novel trends in high-throughput screening. Curr Opin Pharmacol, 2009, 9, 580-588.
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 580-588
    • Mayr, L.M.1    Bojanic, D.2
  • 92
    • 33745809902 scopus 로고    scopus 로고
    • Hit discovery and hit-to-lead approaches
    • Keseru, G. M.; Makara, G. M., Hit discovery and hit-to-lead approaches. Drug Discov. Today, 2006, 11, 741-748.
    • (2006) Drug Discov. Today , vol.11 , pp. 741-748
    • Keseru, G.M.1    Makara, G.M.2
  • 94
    • 84855845987 scopus 로고    scopus 로고
    • High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase
    • Goldin, E.; Zheng, W.; Motabar, O.; Southall, N.; Choi, J. H.; Marugan, J.; Austin, C. P.; Sidransky, E., High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase. PLoS ONE, 2012, 7, e29861.
    • (2012) PLoS ONE , vol.7
    • Goldin, E.1    Zheng, W.2    Motabar, O.3    Southall, N.4    Choi, J.H.5    Marugan, J.6    Austin, C.P.7    Sidransky, E.8
  • 95
    • 79954415602 scopus 로고    scopus 로고
    • Inhibitor screening of pharmacological chaperones for lysosomal b-glucocerebrosidase by capillary electrophoresis
    • Shanmuganathan, M.; Britz-McKibbin, P., Inhibitor screening of pharmacological chaperones for lysosomal b-glucocerebrosidase by capillary electrophoresis. Anal. Bioanal. Chem., 2011, 399, 2843-2853.
    • (2011) Anal. Bioanal. Chem , vol.399 , pp. 2843-2853
    • Shanmuganathan, M.1    Britz-McKibbin, P.2
  • 97
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H.; Berglund, H.; Vedadi, M., The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc., 2007, 2, 2212-2221.
    • (2007) Nat. Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 98
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo, M.-C.; Aulabaugh, A.; Jin, G.; Cowling, R.; Bard, J.; Malamas, M.; Ellestad, G., Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem., 2004, 332, 153-159.
    • (2004) Anal. Biochem , vol.332 , pp. 153-159
    • Lo, M.-C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 99
    • 79952035065 scopus 로고    scopus 로고
    • Rescue of misfolded proteins and stabilization by small molecules
    • Stevens, R. C.; Sancho, J.; Martinez, A., Rescue of misfolded proteins and stabilization by small molecules. Methods Mol. Biol., 2010, 648, 313-324.
    • (2010) Methods Mol. Biol , vol.648 , pp. 313-324
    • Stevens, R.C.1    Sancho, J.2    Martinez, A.3
  • 101
    • 0035879403 scopus 로고    scopus 로고
    • Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation
    • Flatmark, T.; Stokka, A. J.; Berge, S. V., Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation. Anal. Biochem., 2001, 294, 95-101.
    • (2001) Anal. Biochem , vol.294 , pp. 95-101
    • Flatmark, T.1    Stokka, A.J.2    Berge, S.V.3
  • 102
    • 0037330268 scopus 로고    scopus 로고
    • Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: The effect of terminal deletions, substrate analogues and phosphorylation
    • Stokka, A. J.; Flatmark, T., Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation. Biochem. J., 2003, 369, 509-518.
    • (2003) Biochem. J , vol.369 , pp. 509-518
    • Stokka, A.J.1    Flatmark, T.2
  • 103
    • 0001623810 scopus 로고    scopus 로고
    • Tyrosine hydroxylase binds tetrahydrobiopterin cofactor with negative cooperativity, as shown by kinetic analyses and surface plasmon resonance detection
    • Flatmark, T.; Almås, B.; Knappskog, P. M.; Berge, S. V.; Svebak, R. M.; Chehin, R.; Muga, A.; Martínez, A., Tyrosine hydroxylase binds tetrahydrobiopterin cofactor with negative cooperativity, as shown by kinetic analyses and surface plasmon resonance detection. Eur. J. Biochem., 1999, 262, 840-849.
    • (1999) Eur. J. Biochem , vol.262 , pp. 840-849
    • Flatmark, T.1    Almås, B.2    Knappskog, P.M.3    Berge, S.V.4    Svebak, R.M.5    Chehin, R.6    Muga, A.7    Martínez, A.8
  • 104
    • 84862304996 scopus 로고    scopus 로고
    • Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase
    • Torreblanca, R.; Lira-Navarrete, E.; Sancho, J.; Hurtado-Guerrero, R., Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase. Chembiochem., 2012, 13 1266-1269.
    • (2012) Chembiochem , vol.13 , pp. 1266-1269
    • Torreblanca, R.1    Lira-Navarrete, E.2    Sancho, J.3    Hurtado-Guerrero, R.4
  • 105
    • 0030849458 scopus 로고    scopus 로고
    • Analysis of phenylalanine hydroxylase genotypes and hyperphenylalaninemia phenotypes using L-[1-13C]phenylalanine oxidation rates in vivo: A pilot study
    • Treacy, E. P.; Delente, J. J.; Elkas, G.; Carter, K.; Lambert, M.; Waters, P. J.; Scriver, C. R., Analysis of phenylalanine hydroxylase genotypes and hyperphenylalaninemia phenotypes using L-[1-13C]phenylalanine oxidation rates in vivo: a pilot study. Pediatr. Res., 1997, 42, 430-435.
    • (1997) Pediatr. Res , vol.42 , pp. 430-435
    • Treacy, E.P.1    Delente, J.J.2    Elkas, G.3    Carter, K.4    Lambert, M.5    Waters, P.J.6    Scriver, C.R.7
  • 107
    • 79952449396 scopus 로고    scopus 로고
    • Tyrosine hydroxylase and regulation of dopamine synthesis
    • Daubner, S. C.; Le, T.; Wang, S., Tyrosine hydroxylase and regulation of dopamine synthesis. Arch. Biochem. Biophys., 2011, 508, 1-12.
    • (2011) Arch. Biochem. Biophys , vol.508 , pp. 1-12
    • Daubner, S.C.1    Le, T.2    Wang, S.3


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