Evidence map›Paper›PMID 22343815›Full record

ArticleClinical pharmacology and therapeutics2012

Heterotropic effects on drug-metabolizing enzyme activities: in vitro curiosity emerges as a clinically meaningful phenomenon (perhaps?).

R S Obach

Abstract readComment
PubMed Publisher
In one paragraph

Article in Clinical pharmacology and therapeutics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

R S ObachPfizer, Inc., Groton, Connecticut, USA. r.scott.obach@pfizer.com

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alterations in cytochrome P4503A4 are the most frequent underlying cause of drug-drug interactions (DDIs). This enzyme exhibits some unusual behaviors; for example, it has been observed that certain inhibitors can affect some CYP3A4-catalyzed reactions more than others, even for the same substrate. This has been proposed to be due to the simultaneous binding of more than one ligand to the enzyme. This behavior has been frequently observed in vitro, but seldom are analogous effects evident in vivo.

Indexed as

Cytochrome P-450 CYP3AFluconazoleHumansMidazolamCYP3A4 protein, humanCYP3A5 protein, humanCytochrome P-450 CYP3AFluconazoleMidazolam

Identifiers

PMID22343815

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.