Roles of Residues F206 and V367 in Human CYP2B6: Effects of Mutations on Androgen Hydroxylation, Mechanism-Based Inactivation, and Reversible Inhibition.

about

Roles of Residues F206 and V367 in Human CYP2B6: Effects of Mutations on Androgen Hydroxylation, Mechanism-Based Inactivation, and Reversible Inhibition.

Item

http://www.wikidata.org/entity/Q42713267

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@en

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@nl

type

Item

label

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@en

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@nl

prefLabel

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@en

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@nl

P1476

Roles of Residues F206 and V36 ...... on, and Reversible Inhibition.

@en

P2093

Cesar Kenaan

http://www.w3.org/2001/XMLSchema#string

Haoming Zhang

http://www.w3.org/2001/XMLSchema#string

Hsia-Lien Lin

http://www.w3.org/2001/XMLSchema#string

Paul F Hollenberg

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-A resolution

Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity

Structural and Thermodynamic Consequences of 1-(4-Chlorophenyl)imidazole Binding to Cytochrome P450 2B4 † , ‡

Structural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic Activity

Structures of Cytochrome P450 2B6 Bound to 4-Benzylpyridine and 4-(4-Nitrobenzyl)pyridine: Insight into Inhibitor Binding and Rearrangement of Active Site Side Chains

Active site substitution A82W improves the regioselectivity of steroid hydroxylation by cytochrome P450 BM3 mutants as rationalized by spin relaxation nuclear magnetic resonance studies.

Analysis of mammalian cytochrome P450 structure and function by site-directed mutagenesis.

Mechanism-based inactivators as probes of cytochrome P450 structure and function.

Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes

CYP2B6: new insights into a historically overlooked cytochrome P450 isozyme

P304

1771-1779

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1124/DMD.116.071662

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2016-08-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27538916

http://www.w3.org/2001/XMLSchema#string

P932

5074475

http://www.w3.org/2001/XMLSchema#string