Active Site Topology of Human Cytochrome P450 2E1

1996 ◽  
Vol 9 (1) ◽  
pp. 223-226 ◽  
Author(s):  
Richard Mackman ◽  
Zuyu Guo ◽  
F. Peter Guengerich ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Cytochrome P450 ◽  
Active Site ◽  
Cytochrome P450 2E1 ◽  
Human Cytochrome

scholarly journals Inhibition of Human Cytochrome P450 2E1 by Halogenated Anilines, Phenols, and Thiophenols

2005 ◽  
Vol 28 (7) ◽  
pp. 1221-1223 ◽  
Author(s):  
Yohei Ohashi ◽  
Katsuya Yamada ◽  
Ikuyo Takemoto ◽  
Takaharu Mizutani ◽  
Ken-ichi Saeki
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 2E1 ◽  
Human Cytochrome

scholarly journals Inhibition of human cytochrome P450 2E1 and 2A6 by aldehydes: Structure and activity relationships

2014 ◽  
Vol 219 ◽  
pp. 195-202 ◽  
Author(s):  
Suneel K. Kandagatla ◽  
Todd Mack ◽  
Sean Simpson ◽  
Jill Sollenberger ◽  
Eric Helton ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 2E1 ◽  
Human Cytochrome ◽  
Structure And Activity

Control of Human Cytochrome P450 2E1 Electrocatalytic Response as a Result of Unique Orientation on Gold Electrodes

2010 ◽  
Vol 82 (12) ◽  
pp. 5357-5362 ◽  
Author(s):  
Lok Hang Mak ◽  
Sheila J. Sadeghi ◽  
Andrea Fantuzzi ◽  
Gianfranco Gilardi
Keyword(s):  
Cytochrome P450 ◽  
Gold Electrodes ◽  
Cytochrome P450 2E1 ◽  
Human Cytochrome

Stable expression of human cytochrome P450 2E1 in V79 Chinese hamster cells

1995 ◽  
Vol 293 (2) ◽  
pp. 123-131 ◽  
Author(s):  
Wolfgang A. Schmalix ◽  
Martina Barrenscheen ◽  
Robert Landsiedel ◽  
Christine Janzowski ◽  
Gerhard Eisenbrand ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Chinese Hamster ◽  
Stable Expression ◽  
Cytochrome P450 2E1 ◽  
Chinese Hamster Cells ◽  
Human Cytochrome

scholarly journals The screening of the inhibitors of the human cytochrome P450(51) (CYP51A1): the plant and animal structural lanosterol's analogs

2014 ◽  
Vol 60 (5) ◽  
pp. 528-537 ◽  
Author(s):  
L.A. Kaluzhskiy ◽  
O.V. Gnedenko ◽  
A.A. Gilep ◽  
N.V. Strushkevich ◽  
T.V. Shkel ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Surface Plasmon Resonance ◽  
Active Site ◽  
Cholesterol Biosynthesis ◽  
High Affinity ◽  
Human Cytochrome ◽  
Low Weight ◽  
Biosynthesis Regulation ◽  
Spectral Titration ◽  
Specific Inhibitors

The cholesterol biosynthesis regulation is the important part of the hypercholesterolemia diseases therapy. The inhibition of the post-squalene cholesterol biosynthesis steps provide the alternative to classic statin therapy. Sterol-14a-demethylase (CYP51) is one of the hypothetical targets for it. In this work the screening of the ability to interact with human CYP51 (CYP51A1) for the nature low-weight compounds with steroid-like scaffold were performed by integration of the surface plasmon resonance biosensor and spectral titration methods. The results of the selection were 4 compounds (betulafolientriol, holothurin A, teasaponin, capsicoside A) witch had high affinity to the CYP51A1 active site. These data extend the range of compounds which may be used as specific inhibitors of CYP51 and give the permission to suggest the dynamic of the enzyme.

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