X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity
about
Structural and chemical profiling of the human cytosolic sulfotransferasesCrystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reactionStructure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibitionPhylogenomic approaches to common problems encountered in the analysis of low copy repeats: the sulfotransferase 1A gene family exampleCrystal structure of SULT2A3, human hydroxysteroid sulfotransferaseCrystal structure of StaL, a glycopeptide antibiotic sulfotransferase from Streptomyces toyocaensisThe Molecular Basis for the Broad Substrate Specificity of Human Sulfotransferase 1A1Identification of a new subfamily of sulphotransferases: cloning and characterization of canine SULT1D1Cytosolic sulfotransferase 1A3 is induced by dopamine and protects neuronal cells from dopamine toxicity: role of D1 receptor-N-methyl-D-aspartate receptor couplingGenetic diversity and function in the human cytosolic sulfotransferases.The dimerization motif of cytosolic sulfotransferases.Predicting Mouse Liver Microsomal Stability with "Pruned" Machine Learning Models and Public Data.Dopamine receptors in human adipocytes: expression and functionsCrystal structure-based studies of cytosolic sulfotransferase.Mechanistic studies of beta-arylsulfotransferase IVEnzymatic aspects of the phenol (aryl) sulfotransferases.Sulfation through the looking glass--recent advances in sulfotransferase research for the curious.Arginine residues in the active site of human phenol sulfotransferase (SULT1A1).In silico pharmacology for drug discovery: applications to targets and beyondSULT1A3-mediated regiospecific 7-O-sulfation of flavonoids in Caco-2 cells can be explained by the relevant molecular docking studies.Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases.Computational prediction of human drug metabolism.Concerted actions of the catechol O-methyltransferase and the cytosolic sulfotransferase SULT1A3 in the metabolism of catecholic drugs.Plasma-free vs deconjugated metanephrines for diagnosis of phaeochromocytomaCrystal structures of human sulfotransferases: insights into the mechanisms of action and substrate selectivity.The use of zebrafish as a model system for investigating the role of the SULTs in the metabolism of endogenous compounds and xenobiotics.Interactions of cytosolic sulfotransferases with xenobiotics.The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions.Kinetic and affinity predictions of a protein-protein interaction using multivariate experimental design.Mechanism of sulfotransferase pharmacogenetics in altered xenobiotic metabolism.Expression and therapeutic targeting of dopamine receptor-1 (D1R) in breast cancer.Conformation and interactions of dopamine hydrochloride in solution.Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity.Study of human dopamine sulfotransferases based on gene expression programming.Inhibition of bovine phenol sulfotransferase (bSULT1A1) by CoA thioesters. Evidence for positive cooperativity and inhibition by interaction with both the nucleotide and phenol binding sites.Manganese stimulation and stereospecificity of the Dopa (3,4-dihydroxyphenylalanine)/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase. Kinetic studies of the mechanism using wild-type and mutant enzymes.Structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase, SULT1A3.Sulfation of apomorphine by human sulfotransferases: evidence of a major role for the polymorphic phenol sulfotransferase, SULT1A1.Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay.Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3.
P2860
Q21145886-6863EADB-9770-4DA6-A342-BDFDA6BA4403Q24292419-F30128F5-5163-4332-8C2F-212F0726B128Q24324237-ED7909F8-EB30-4B5B-8AC1-AEE8F3FBEDA6Q24804582-23B1B9CC-4780-4D60-859A-B6D1D7D74F9CQ27624929-022361EC-4278-4D3F-8C20-33F671E952A9Q27643934-D829D822-6D70-4837-A093-411662D55761Q27675466-CAC2837F-C9C5-46CB-827A-E660947FB79CQ28366304-2739BA33-152E-49D7-B22A-18969FAFF656Q28910380-92272279-6B0E-411C-A15B-6CC95AE7C276Q30355169-5AFF9D56-5129-4298-BDE8-F107F7ABDC72Q30979229-5745254A-79ED-4460-A053-A44D7C5E64F6Q30998741-B1423B5B-F594-4A93-B4E1-95ABBD6E87CDQ34038390-21DE0815-09BC-4F2F-BB3B-049DED77D369Q34205759-F59B138B-0EE6-4DB5-B5FD-53BDF0D6F119Q34328069-0CA7956C-0DCA-4E5C-9B2F-30092E5ACBC7Q34479020-111D92BD-5432-40D4-A885-CCA0268F5174Q35002556-6D65F865-BE81-404D-ACF5-035A4B321934Q35054996-F5925395-95EF-483E-A54A-27761506F461Q35995265-06CBC296-A9E5-4351-8489-BC84F1DA3FE5Q36115778-35109319-250D-424F-9FA5-E75A2261A732Q36486711-5A19AE5C-586D-40EF-ABCC-F998F89767ECQ36572605-1DF60FC4-5566-497A-AE89-64390E34FAADQ36755200-3AB022D8-4131-4405-83A5-F0A1CC839B90Q37146776-CECA451C-68F7-4C4C-B002-BB48D04EDD16Q38003482-30B9723E-7900-448B-92E8-BE235D321513Q38136700-835E495E-2D30-418E-B7F7-F9D2CABF06DAQ38159767-081A31CD-D786-43B0-9A9C-1E7CCC87C85FQ38264122-13509F47-7252-4EB3-A154-C06C8B1C8EF5Q38288616-A3E2398D-167F-4B59-8ABF-84F36C0C1EC2Q38527536-736D7B8B-E2D0-44F2-A979-CF1DD89ED78FQ41225554-9716860C-0BB0-4A11-BC93-383A1DE035C4Q41602058-B9B7B751-1313-4D93-BF5A-624A545A180AQ43003533-58C5FBD3-AD3C-44B1-A48A-40E882EC35B1Q43974588-FBFD1E33-43FC-4DF3-93CE-ED628E2A3CEBQ44094492-C0AE42A2-117F-4C50-835D-3C30D08C359CQ44135109-CE78265C-A5B8-4CA0-A1D8-157EB55AC3CEQ44211082-0E5D6A9C-0FC7-481E-AD87-E622D0C8A6BDQ44683306-5C709094-F7C8-4277-B090-EAD0EB309288Q44758118-BE46B4F1-9227-485E-A718-DE8B0E122B7AQ44761851-BBF30C02-58BA-44F0-9998-63395E7EE409
P2860
X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
X-ray crystal structure of hum ...... nsferase substrate specificity
@ast
X-ray crystal structure of hum ...... nsferase substrate specificity
@en
X-ray crystal structure of hum ...... nsferase substrate specificity
@nl
type
label
X-ray crystal structure of hum ...... nsferase substrate specificity
@ast
X-ray crystal structure of hum ...... nsferase substrate specificity
@en
X-ray crystal structure of hum ...... nsferase substrate specificity
@nl
prefLabel
X-ray crystal structure of hum ...... nsferase substrate specificity
@ast
X-ray crystal structure of hum ...... nsferase substrate specificity
@en
X-ray crystal structure of hum ...... nsferase substrate specificity
@nl
P2093
P2860
P921
P356
P1476
X-ray crystal structure of hum ...... nsferase substrate specificity
@en
P2093
A J Wonacott
G R Manchee
J Taskinen
P2860
P304
37862-37868
P356
10.1074/JBC.274.53.37862
P407
P577
1999-12-01T00:00:00Z