Evidence map›Paper›PMID 34272697›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Enzyme Kinetics of Oxidative Metabolism-Cytochromes P450.

Ken Korzekwa

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Noninvasive Evaluation of Prolonged-Release Pirfenidone in Compensated Liver Cirrhosis. ODISEA Study, a Randomised Trial.Liver international : official journal of the International Association for the Study of the Liver · 2025
    Trial
  2. Enzyme-substrate-inactivator complex formation can impact time-dependent inhibition kinetics.Drug metabolism and disposition: the biological fate of chemicals · 2026
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Ken KorzekwaDepartment of Pharmaceutical Sciences, Temple University School of Pharmacy, Philadelphia, PA, USA. korzekwa@temple.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytochrome P450 enzymes (CYPs) are the most important enzymes in the oxidative metabolism of hydrophobic drugs and other foreign compounds (xenobiotics). The versatility of these enzymes results in some unusual kinetic properties, stemming from the simultaneous interaction of multiple substrates with the CYP active site. Often, the CYPs display kinetics that deviate from standard hyperbolic saturation or inhibition kinetics. Non-Michaelis-Menten or "atypical" saturation kinetics include sigmoidal, biphasic, and substrate inhibition kinetics (see Chapter 2 ). Interactions between substrates include competitive inhibition, noncompetitive inhibition, mixed inhibition, partial inhibition, activation, and activation followed by inhibition (see Chapters 4 and 6 ). Models and equations that can result in these kinetic profiles will be presented and discussed.

Indexed as

Activation, MetabolicAlgorithmsCatalytic DomainCytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemHumansHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularOxidative StressSubstrate SpecificityXenobioticsCytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemXenobioticsBiphasic kineticsCatalytic cycleCytochrome P450Non-Michaelis-Menten kineticsSubstrate binding

Identifiers

What OpenQuestion holds

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Registered trials

None linked

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.