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Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1
Ting Wang,
Ian Cook
,
Thomas S. Leyh
Microbiology & Immunology
Research output
:
Contribution to journal
›
Article
›
peer-review
17
Scopus citations
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Medicine & Life Sciences
human SULT1A1 protein
100%
Allosteric Regulation
75%
epigallocatechin gallate
65%
Isoenzymes
50%
Nucleotides
41%
Allosteric Site
36%
Sulfotransferases
35%
Catalytic Domain
22%
catechin gallate
22%
Phosphoadenosine Phosphosulfate
21%
Catechin
16%
Polyphenols
14%
Hydroxyl Radical
14%
Enzymes
13%
Amines
13%
Thyroid Hormones
12%
Epinephrine
11%
Serotonin
10%
Dopamine
10%
Protein Isoforms
10%
Binding Sites
9%
Steroids
9%
Anti-Inflammatory Agents
9%
Liver
6%
Pharmaceutical Preparations
5%
Chemical Compounds
(-)-Epigallocatechin
68%
Gallate
45%
Nucleotide
41%
Catechin
29%
Thyroid Hormone
17%
Steroid Hormone
16%
Signalling Molecule
16%
Nonsteroid Antiinflammatory Agent
14%
Serotonin
14%
Polyphenol
13%
Dopamine
11%
Conformational Isomer
11%
Hydroxyl
10%
Pharmacological Metabolism
9%
Binding Site
8%
Amine
8%
Molecule
4%