The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates
about
Structural and chemical profiling of the human cytosolic sulfotransferasesThe Regulation of Steroid Action by Sulfation and DesulfationThe structural biology of oestrogen metabolismSulfotransferase 1A1 Substrate Selectivity: A Molecular Clamp MechanismThe Molecular Basis for the Broad Substrate Specificity of Human Sulfotransferase 1A1The gate that governs sulfotransferase selectivity.Structure-Based Mutational Studies of Substrate Inhibition of Betaine Aldehyde Dehydrogenase BetB from Staphylococcus aureusIn silico mechanistic profiling to probe small molecule binding to sulfotransferasesSpecific estrogen sulfotransferase (SULT1E1) substrates and molecular imaging probe candidates.Paradigms of sulfotransferase catalysis: the mechanism of SULT2A1.Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexesThe allosteric binding sites of sulfotransferase 1A1.Potent inhibition of human sulfotransferase 1A1 by 17α-ethinylestradiol: role of 3'-phosphoadenosine 5'-phosphosulfate binding and structural rearrangements in regulating inhibition and activityHuman sulfotransferases and their role in chemical metabolism.Role for cytoplasmic nucleotide hydrolysis in hepatic function and protein synthesis.Design and Interpretation of Human Sulfotransferase 1A1 Assays.Controlling Sulfuryl-Transfer Biology.Inhibition of thyroid hormone sulfotransferase activity by brominated flame retardants and halogenated phenolics.Structure, dynamics and selectivity in the sulfotransferase family.From sequence and structure of sulfotransferases and dihydropyrimidinases to an understanding of their mechanisms of action and function.Substrate inhibition kinetics in drug metabolism reactions.Crystal structures of human sulfotransferases: insights into the mechanisms of action and substrate selectivity.Interactions of cytosolic sulfotransferases with xenobiotics.Mechanism of sulfotransferase pharmacogenetics in altered xenobiotic metabolism.Understanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism.Removal of substrate inhibition and increase in maximal velocity in the short chain dehydrogenase/reductase salutaridine reductase involved in morphine biosynthesis.Stochastic ensembles, conformationally adaptive teamwork, and enzymatic detoxification.Tetrahydrobiopterin regulates monoamine neurotransmitter sulfonation.The NSAID allosteric site of human cytosolic sulfotransferases.
P2860
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P2860
The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The structure of human SULT1A1 ...... ion with multi-ring substrates
@ast
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en-gb
The structure of human SULT1A1 ...... ion with multi-ring substrates
@nl
type
label
The structure of human SULT1A1 ...... ion with multi-ring substrates
@ast
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en-gb
The structure of human SULT1A1 ...... ion with multi-ring substrates
@nl
prefLabel
The structure of human SULT1A1 ...... ion with multi-ring substrates
@ast
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en-gb
The structure of human SULT1A1 ...... ion with multi-ring substrates
@nl
P2093
P2860
P356
P1476
The structure of human SULT1A1 ...... ion with multi-ring substrates
@en
P2093
Jennifer L Martin
Michael E McManus
Niranjali U Gamage
Ronald G Duggleby
Sergey Tsvetanov
P2860
P304
P356
10.1074/JBC.M508289200
P407
P577
2005-12-16T00:00:00Z