Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution
about
Tyrosine hydroxylase and regulation of dopamine synthesisStructural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylaseCatecholamine biosynthesis and physiological regulation in neuroendocrine cells.Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active siteEffects of phosphorylation by protein kinase A on binding of catecholamines to the human tyrosine hydroxylase isoforms.Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.The interplay of catechol ligands with nanoparticulate iron oxides.Conformation and interactions of dopamine hydrochloride in solution.Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation.The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase.Modeled ligand-protein complexes elucidate the origin of substrate specificity and provide insight into catalytic mechanisms of phenylalanine hydroxylase and tyrosine hydroxylase.A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Rotational Spectrum and Conformational Analysis of N-Methyl-2-Aminoethanol: Insights into the Shape of Adrenergic Neurotransmitters.
P2860
Q21710723-9908F9F6-85E8-4949-97C8-E6F172E00F8EQ27678855-374C7FE6-4313-4F78-879F-258D3425309EQ33848376-0A71BA62-E87B-4006-AF5C-319C66AF7AA6Q34731673-E91DFEFC-5756-4A2C-B5DE-310B1333EC19Q35724388-D516B8B1-44F6-40CD-B736-1AE4FF14B954Q37695699-B1FF0CEA-670F-4B81-BB12-BC186162772AQ37975445-463420FC-B000-4B90-9D3D-C3A39BD4C302Q41602058-D5508C63-7FF6-497B-A7E3-729FDCDF699AQ42036836-06660D1F-1846-4938-BA10-8AD059BF3F6BQ43066150-03C7AF3E-8E30-487C-B125-DF1E708BAB55Q43574533-56B4482A-A720-4252-9971-A65A4ADFB934Q44358666-7D1CC004-A632-4ED0-9359-3B11C1A2F79FQ52571058-F32E445F-1D91-4BCB-A9F1-0804AD4F380EQ55412811-118D1D73-A95C-44C0-A944-3C0CB1354A7B
P2860
Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@ast
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@en
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@nl
type
label
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@ast
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@en
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@nl
prefLabel
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@ast
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@en
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@nl
P2093
P356
P1433
P1476
Crystallographic analysis of t ...... inhibitors at 2.0 A resolution
@en
P2093
H Erlandsen
R C Stevens
T Flatmark
P304
P356
10.1021/BI9815290
P407
P577
1998-11-10T00:00:00Z