Evidence map›Paper›PMID 39032346›Full record

ArticleJournal of inorganic biochemistry2024

A flexible linker of 8-amino acids between the membrane binding segment and the FMN domain of cytochrome P450 reductase is necessary for optimal activity.

Freeborn Rwere, Naw May P Cartee, Yuting Yang, Lucy Waskell

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Review
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

4 authors.

Freeborn RwereDepartment of Anesthesiology, University of Michigan and VAMC, 2215 Fuller Road, Ann Arbor, MI, USA; Department of Anesthesiology, Perioperative and Pain Medicine, School of Medicine, Stanford University, 3174 Porter Dr, Palo Alto, CA, USA. Electronic address: frwere@stanford.edu.
Naw May P CarteeDepartment of Anesthesiology, University of Michigan and VAMC, 2215 Fuller Road, Ann Arbor, MI, USA.
Yuting YangDepartment of Anesthesiology, University of Michigan and VAMC, 2215 Fuller Road, Ann Arbor, MI, USA.
Lucy WaskellDepartment of Anesthesiology, University of Michigan and VAMC, 2215 Fuller Road, Ann Arbor, MI, USA.

Funding

PARTICIPATION OF CYTOCHROME B5 IN ANESTHETIC METABOLISMR01GM035533 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 1985 to 2010
$2.7M
Microsomal Cytochromes P450 and their Interactions with their Redox PartnersR01GM094209 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 2011 to 2014
$1.5M
NIGMS NIH HHS R01 GM035533NIGMS NIH HHS R01 GM094209
6 · The paper itself

Abstract

The diflavin NADPH-cytochrome P450 reductase (CYPOR) plays a critical role in human cytochrome P450 (CYP) activity by sequentially delivering two electrons from NADPH to CYP enzymes during catalysis. Although electron transfer to forty-eight human CYP enzymes by the FMN hydroquinone of CYPOR is well-known, the role of the linker between the NH

Indexed as

Aryl Hydrocarbon HydroxylasesCytochrome P450 Family 2Flavin MononucleotideNADPH-Ferrihemoprotein ReductaseAnimalsHumansKineticsMutagenesis, Site-DirectedProtein DomainsAryl Hydrocarbon Hydroxylasescytochrome P-450 CYP2B4 (rabbit)Cytochrome P450 Family 2Flavin MononucleotideNADPH-Ferrihemoprotein ReductaseBenzphetamineCytochrome cCytochrome P450 2B4Cytochrome P450 reductaseEnzyme kineticsFlexible linker

Identifiers

PMID39032346
PMCPMC11298297

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.