Noncovalent intermolecular interactions between dehydroepiandrosterone and the active site of human dehydroepiandrosterone sulphotransferase: A density functional theory based treatment
Author:
Funder
Tarbiat Modares University Research Council
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Reference19 articles.
1. Identification and Characterization of Two Amino Acids Critical for the Substrate Inhibition of Human Dehydroepiandrosterone Sulfotransferase (SULT2A1)
2. Structure and Function of Sulfotransferases
3. Bioactivation of mutagens via sulfation
4. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Theoretical investigation of the effects of diverse hydrogen-bonding characteristics on the 17O chemical shielding and electric field gradient tensors within the active sites of MraYAA bound to nucleoside antibiotics capuramycin, carbacaprazamycin, 3′-Hydroxymureidomycin A, and muraymycin D2;Solid State Nuclear Magnetic Resonance;2024-10
2. A new approach on diminutive effects for non-covalent interactions: fused bicyclic hydrogen-bonded complexes of hypohalous acids with fluoromethanol;Molecular Physics;2016-10-14
3. A study of hydrogen bond effects on the oxygen, nitrogen, and hydrogen electric field gradient tensors in the active site of human dehydroepiandrosterone sulphotransferase: A density-functional theory based treatment;Chemical Physics Letters;2016-06
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