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1 ving, in most cases, a deficient activity of phenylalanine hydroxylase.
2 that of the core of the regulatory domain of phenylalanine hydroxylase.
3 tor of the tetrahydropterin-dependent enzyme phenylalanine hydroxylase.
4 ss-react with either tyrosine hydroxylase or phenylalanine hydroxylase.
5 ormality in the function of the liver enzyme phenylalanine hydroxylase.
6 ading to competitive inhibition of epidermal phenylalanine hydroxylase.
7 h(enu2) mice have a mutation in the gene for phenylalanine hydroxylase.
8 droxylase and the 122 N-terminal residues of phenylalanine hydroxylase.
9                                              Phenylalanine hydroxylase, a mononuclear non-heme iron e
10 th high levels of 6BH4, and the induction of phenylalanine hydroxylase activities during the telogen/
11 phenylalanine concentrations and we measured phenylalanine hydroxylase activity and phenylalanine int
12                                              Phenylalanine hydroxylase and 4a-hydroxy-6BH4-dehydratas
13 kinetic properties of pure recombinant human phenylalanine hydroxylase and on estimates of the in viv
14 mutations were incorporated into full-length phenylalanine hydroxylase and the complementary mutation
15                              Both the copper-phenylalanine hydroxylase and the copper-depleted hydrox
16  1 containing the C-terminal 331 residues of phenylalanine hydroxylase and the N-terminal 168 residue
17 ytic domains of the pterin-dependent enzymes phenylalanine hydroxylase and tyrosine hydroxylase are h
18 ordinates of two highly homologous proteins, phenylalanine hydroxylase and tyrosine hydroxylase, were
19 id hydroxylase family--tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase--r
20  tyrosine hydroxylase and of tyrosine 325 of phenylalanine hydroxylase are 5 and 4.5 A, respectively,
21 romatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, ut
22 ional changes accompanying activation of rat phenylalanine hydroxylase by phenylalanine.
23                                              Phenylalanine hydroxylase catalyzes the first step in th
24 very pronounced asymmetry is observed in the phenylalanine hydroxylase, caused by the occurrence of t
25  hydroxylase locus using a full-length human phenylalanine hydroxylase cDNA clone as a hybridization
26 e site-specific genome integration of murine phenylalanine hydroxylase cDNA in the livers of phenylke
27 phage integration system, we delivered mouse phenylalanine hydroxylase cDNA to the livers of PKU mice
28                                 Tyrosine and phenylalanine hydroxylases contain homologous catalytic
29                                 The purified phenylalanine hydroxylase contains copper, which does no
30 e of the divergent Chromobacterium violaceum phenylalanine hydroxylase (CvPheOH) ( approximately 24%
31                        Phenylketonuria (PKU, phenylalanine hydroxylase deficiency), an inborn error o
32 H, the C-terminal 336 amino acid residues of phenylalanine hydroxylase; Delta155TYH, the C-terminal 3
33  induced by the inclusion of an inhibitor of phenylalanine hydroxylase, DL-p-chlorophenylalanine, and
34                       The model identifies a phenylalanine hydroxylase enzyme with 2.5x catalytic act
35        Previous studies of ferrous wild-type phenylalanine hydroxylase, [Fe(2+)]PAH(T)[], have shown
36                    To study this hypothesis, phenylalanine hydroxylase from a bacterial source has be
37                     The non-heme iron enzyme phenylalanine hydroxylase from Chromobacterium violaceum
38                                              Phenylalanine hydroxylase from Chromobacterium violaceum
39                       Because defects in the phenylalanine hydroxylase gene (PAH) cause phenylketonur
40   The c.1222C>T (p.Arg408Trp) variant in the phenylalanine hydroxylase gene (PAH) is the most frequen
41 ive genetic disease caused by defects in the phenylalanine hydroxylase gene.
42 ed within the protein coding sequence of the phenylalanine hydroxylase gene.
43                              A gene encoding phenylalanine hydroxylase has been cloned from Chromobac
44 he mouse liver by targeting it via the human phenylalanine hydroxylase (hPAH) gene promoter.
45                                        Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylal
46 ne such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen
47                         Dysfunction of human phenylalanine hydroxylase (hPAH, EC 1.14.16.1) is the pr
48 utations on the isolated catalytic domain of phenylalanine hydroxylase identified three residues that
49 undantly produced in nonneuronal tissues via phenylalanine hydroxylase, in addition to canonical bios
50                                 In addition, phenylalanine hydroxylase is allosterically regulated by
51 he position corresponding to position 379 of phenylalanine hydroxylase is critical for dihydroxypheny
52                              In this context phenylalanine hydroxylase is subject to phosphorylation/
53  restriction site polymorphisms at the human phenylalanine hydroxylase locus among Caucasians are suc
54 ymorphisms have been identified at the human phenylalanine hydroxylase locus using a full-length huma
55  D4S1625 and D4S1629; and LOD = 2.56 at PAH (phenylalanine hydroxylase) on chromosome 12).
56  for the phenylalanine-degrading enzyme PAH (phenylalanine hydroxylase), or restricted dietary phenyl
57 cture, dynamics, and function for the enzyme phenylalanine hydroxylase (PAH) can lead to needed new t
58                      The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylat
59          MC-DNA vectors expressed the murine phenylalanine hydroxylase (Pah) complementary DNA (cDNA)
60 ave previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordi
61          Phenylketonuria (PKU; also known as phenylalanine hydroxylase (PAH) deficiency) is an autoso
62 ylketonuria (PKU), caused by variants in the phenylalanine hydroxylase (PAH) gene, is the most common
63 isorder caused by pathogenic variants in the phenylalanine hydroxylase (PAH) gene, results in the acc
64 ylketonuria (PKU) is a genetic deficiency of phenylalanine hydroxylase (PAH) in liver resulting in bl
65                                              Phenylalanine hydroxylase (PAH) is a key enzyme in the c
66                                              Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin
67 KU) patients, a genetic defect in the enzyme phenylalanine hydroxylase (PAH) leads to elevated system
68 enylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently
69 -chain amino-acid transaminase 1 (BCAT1) and phenylalanine hydroxylase (PAH) with development of IFG.
70 th HPA harbor mutations in the gene encoding phenylalanine hydroxylase (PAH), and a small proportion
71 , inducible nitric oxide synthase (iNOS) and phenylalanine hydroxylase (PAH), and competition for BH4
72     Activated phenylalanine 4-monooxygenase, phenylalanine hydroxylase (PAH), is known to be involved
73 umans that arises from deficient activity of phenylalanine hydroxylase (PAH), which catalyzes the con
74 partial or complete deficiency of the enzyme phenylalanine hydroxylase (PAH), which is necessary for
75                                              Phenylalanine hydroxylase (Pah)-deficient "PKU mice" hav
76 ic defect caused by lack of the liver enzyme phenylalanine hydroxylase (PAH).
77 her PHS/DCoH could enhance the expression of phenylalanine hydroxylase (PAH).
78 se lncRNA Pair and human HULC associate with phenylalanine hydroxylase (PAH).
79                     The regulatory domain of phenylalanine hydroxylase (PAH, EC ) consists of more th
80                    The activity of rat liver phenylalanine hydroxylase (PAH; phenylalanine 4-monooxyg
81 enase, the neural cell adhesion molecule L1, phenylalanine hydroxylase, paired box 6, the X-linked re
82                                              Phenylalanine hydroxylase (PheH) and tryptophan hydroxyl
83                                              Phenylalanine hydroxylase (PheH) catalyzes the key step
84 The naturally occurring R68S substitution of phenylalanine hydroxylase (PheH) causes phenylketonuria
85                                        Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme
86                                    Mammalian phenylalanine hydroxylase (PheH) is an allosteric enzyme
87                                              Phenylalanine hydroxylase (PheH) is an iron(II)-dependen
88 tyrosine hydroxylase (TyrH) whose homolog in phenylalanine hydroxylase (PheH) takes on a different co
89                                              Phenylalanine hydroxylase (PheOH) catalyzes the conversi
90                                   The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxyl
91 ry dehydratase, together with genes encoding phenylalanine hydroxylase (PhhA) and aromatic aminotrans
92 i and is hypothesized to be the cofactor for phenylalanine hydroxylase (PhhA) in Pseudomonas aerugino
93 ssess a cluster of structural genes encoding phenylalanine hydroxylase (PhhA), carbinolamine dehydrat
94 with Delta117PheH, the catalytic core of rat phenylalanine hydroxylase, ranging from 1.12-1.41.
95                               Only wild-type phenylalanine hydroxylase required pretreatment with phe
96                             This sequence in phenylalanine hydroxylase (residues 19 to 33) has previo
97                                              Phenylalanine hydroxylase stimulator (PHS) is a componen
98 catalyst, we identified a copper-substituted phenylalanine hydroxylase that facilitates enantioconver
99 rited disease caused by impaired activity of phenylalanine hydroxylase, the enzyme that converts phen
100  mutation of the corresponding valine 379 of phenylalanine hydroxylase to aspartate was not sufficien
101 ase to aspartate was not sufficient to allow phenylalanine hydroxylase to form dihydroxyphenylalanine
102                      The nonheme iron enzyme phenylalanine hydroxylase, tyrosine hydroxylase, and try
103                                              Phenylalanine hydroxylase, tyrosine hydroxylase, and try
104 the family of pterin-dependent hydroxylases, phenylalanine hydroxylase, tyrosine hydroxylase, and try
105 uncated and chimeric mutants of tyrosine and phenylalanine hydroxylase were constructed: Delta117PAH,
106  proteins containing the catalytic domain of phenylalanine hydroxylase were unable to hydroxylate tyr
107 ficity, seven residues in the active site of phenylalanine hydroxylase whose side chains are dissimil
108 f a recombinant adeno-associated virus-mouse phenylalanine hydroxylase-woodchuck hepatitis virus post

 
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