ArticleArchives of biochemistry and biophysics2007
CYP2E1 active site residues in substrate recognition sequence 5 identified by photoaffinity labeling and homology modeling.
Article in Archives of biochemistry and biophysics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- In vitro evaluation of structural analogs of diallyl sulfide as novel CYP2E1 inhibitors for their protective effect against xenobiotic-induced toxicity and HIV replication.Toxicology letters · 2018Article
- Altered metabolism of synthetic cannabinoid JWH-018 by human cytochrome P450 2C9 and variants.Biochemical and biophysical research communications · 2018Article
- Structural basis for cooperative binding of azoles to CYP2E1 as interpreted through guided molecular dynamics simulations.Journal of molecular graphics & modelling · 2015Article
- Article
- Cooperative effects for CYP2E1 differ between styrene and its metabolites.Xenobiotica; the fate of foreign compounds in biological systems · 2013Article
- Structure of pyrazole derivatives impact their affinity, stoichiometry, and cooperative interactions for CYP2E1 complexes.Archives of biochemistry and biophysics · 2013Article
- Application of MassSQUIRM for quantitative measurements of lysine demethylase activity.Journal of visualized experiments : JoVE · 2012Article
- Assessment of compound hepatotoxicity using human plateable cryopreserved hepatocytes in a 1536-well-plate format.Assay and drug development technologies · 2012Article
- Article
- Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners.Biochimica et biophysica acta · 2010Article
- Development and evaluation of a structural model for SF1B helicase Dda.Biochemistry · 2009Article
- Identification of hydroxywarfarin binding site in human UDP glucuronosyltransferase 1a10: phenylalanine90 is crucial for the glucuronidation of 6- and 7-hydroxywarfarin but not 8-hydroxywarfarin.Drug metabolism and disposition: the biological fate of chemicals · 2008Article
- Serum biomarker profile associated with high bone turnover and BMD in postmenopausal women.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2008Article
- CYP2E1 substrate inhibition. Mechanistic interpretation through an effector site for monocyclic compounds.The Journal of biological chemistry · 2008Article
- Article
- Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes.Biochemistry · 2007Article
- Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses.Dose-response : a publication of International Hormesis SocietyArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Despite its biological importance, our knowledge of active site structure and relevance of critical amino acids in CYP2E1 catalytic processes remain limited. In this study, we identified CYP2E1 active site residues using photoaffinity labeling with 7-azido-4-methylcoumarin (AzMC) coupled with a CYP2E1 homology model. In the absence of light, AzMC was an effective competitor against substrate p-nitrophenol oxidation by CYP2E1. Photoactivation of AzMC led to a concentration-dependent loss in CYP2E1 activity and structural integrity resulting from the modification of both heme and protein. The photo-labeling reaction degraded heme and produced a possible heme adduct. Probe incorporation into the protein occurred at multiple sites within substrate recognition sequence 5 (SRS-5). Based on a CYP2E1 homology model, we hypothesize AzMC labels SRS-5 residues, Leu363, Val364, and Leu368, in the active site. In addition, we propose a series of phenylalanines, especially Phe106, mediate contacts with the coumarin.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.