The DOI matches its Crossref record; 501 of the 501 references it cites were found in a registry or an index.
Inhibition of Cytochrome P450 Enzymes
Open accessAbstract
Cytochrome P450s (P450s) are subject to inhibition/inactivation by various chemically diverse agents, which may interact directly or indirectly with either the P450 prosthetic heme or the protein moiety or with both moieties. This inhibition is clinically relevant, as it can block physiological pathways as well as result in therapeutically significant beneficial or adverse effects and clinically relevant drug–drug interactions. Herein, we discuss the various chemical agents and their chemical mechanisms that lead to such reversible, quasi-irreversible, or irreversible inhibition of these enzymes. We note that such inhibition targeted at P450-dependent physiological and/or pathological processes has been ingeniously and effectively harnessed not only in the design and development of clinically relevant therapeutic agents but also of fungicides, insecticides, and herbicides.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Carbon Monoxide-binding Pigment of Liver Microsomes
Omura, T., & Sato, R. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82244-3 · Cited by 11,781
Cytochrome P-450: Structure, Mechanism, and Biochemistry
de Montellano, O., & Paul, R. (1986) · Medical Entomology and Zoology · Cited by 2,663
Wink, D. A., & Mitchell, J. B. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00092-6 · Cited by 1,606
High-resolution crystal structure of cytochrome P450cam
Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90190-2 · Cited by 1,411
P-450 Metabolites of Arachidonic Acid in the Control of Cardiovascular Function
Roman, R. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00021.2001 · Cited by 1,309
Gotoh, O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48462-1 · Cited by 1,194
Spectral Studies of Drug Interaction with Hepatic Microsomal Cytochrome
SCHENKMAN, J. B., REMMER, H., & ESTABROOK, R. W. (1967) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)14748-2 · Cited by 1,190
The P450 Superfamily: Update on New Sequences, Gene Mapping, and Recommended Nomenclature
NEBERT, D. W., NELSON, D. R., COON, M. J., ESTABROOK, R. W., FEYEREISEN, R., FUJII-KURIYAMA, Y., GONZALEZ, F. J., GUENGERICH, F. P., GUNSALUS, I. C., JOHNSON, E. F., et al. (1991) · DNA and Cell Biology · doi:10.1089/dna.1991.10.1 · Cited by 1,094
Thiazolidinediones in the Treatment of Insulin Resistance and Type II Diabetes
Saltiel, A. R., & Olefsky, J. M. (1996) · Diabetes · doi:10.2337/diab.45.12.1661 · Cited by 1,053
Guengerich, F. P., Dannan, G. A., Wright, S. T., Martin, M. V., & Kaminsky, L. S. (1982) · Biochemistry · doi:10.1021/bi00266a045 · Cited by 1,012
Cited by
Human Pharmacology of MDMA: Pharmacokinetics, Metabolism, and Disposition
de la Torre, R., Farré, M., Roset, P. N., Pizarro, N., Abanades, S., Segura, M., Segura, J., & Camí, J. (2004) · Therapeutic Drug Monitoring · doi:10.1097/00007691-200404000-00009 · Cited by 444
Feyereisen, R. (2005) · Comprehensive Molecular Insect Science · doi:10.1016/b0-44-451924-6/00049-1 · Cited by 420
Shafiei, M., Peyton, L., Hashemzadeh, M., & Foroumadi, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104240 · Cited by 295
Chatterjee, P., & Franklin, M. R. (2003) · Drug Metabolism and Disposition · doi:10.1124/dmd.31.11.1391 · Cited by 146
Hamamura, N., Page, C., Long, T., Semprini, L., & Arp, D. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.9.3607-3613.1997 · Cited by 80
Metadata
- Authors
- Correia, M. A., & Hollenberg, P. F.
- Venue
- Cytochrome P450
- Publisher
- Springer International Publishing
- Published
- 2015
- Pages
- 177-259
- OpenAlex
- W2155231169
- Cited by
- 257
- References
- 501
- FWCI
- 69.64
- Type
- book chapter
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Inhibition of Cytochrome P450 Enzymes. https://app.cochat.ai/papers/10.1007/978-3-319-12108-6_5
- The paper
- Correia, M. A., & Hollenberg, P. F. (2015). Inhibition of Cytochrome P450 Enzymes. Cytochrome P450. https://doi.org/10.1007/978-3-319-12108-6_5
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.