Evidence map›Paper›PMID 41011624›Full record

ReviewMolecules (Basel, Switzerland)2025

Recent Advances in Elucidating the Mechanism of the NADPH-Cytochrome P450 Reductase-Mediated Electron Transfer Cycle: Experimental and Computational Perspectives.

Songyan Xia, Hajime Hirao

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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

2 authors.

Songyan XiaWarshel Institute for Computational Biology, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.ORCID 0009-0004-7289-1823
Hajime HiraoWarshel Institute for Computational Biology, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.

Funding

Guangdong Natural Science Foundation Grant (General) 2023A1515010317Warshel Institute for Computational Biology (Longgang) LGKCSDPT2024001Warshel Institute for Computational Biology (Shenzhen) C10120180043
6 · The paper itself

Abstract

NADPH-cytochrome P450 reductase (CPR) is an essential redox partner for a wide range of metal-containing proteins, mediating the stepwise transfer of two electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to the redox centers of its partner proteins. This Perspective summarizes recent advances in understanding the mechanisms underlying the CPR-mediated electron transfer (ET) cycle. Emphasis is placed on human and other mammalian CPRs, which provide critical insights into human biology and drug metabolism. Recent experimental and computational approaches that have deepened our mechanistic understanding of CPR function are highlighted. Selected studies are reviewed to illustrate progress in elucidating the interflavin ET within CPR, the interplay between its redox states and structural dynamics, and its protein-protein interactions with redox partners, along with the associated ET pathways. Finally, the remaining challenges and future research directions are outlined.

Indexed as

NADPH-Ferrihemoprotein ReductaseAnimalsElectron TransportHumansModels, MolecularNADPOxidation-ReductionNADPNADPH-Ferrihemoprotein Reductaseconformational dynamicselectron transfer mechanismflavin adenine dinucleotide (FAD)flavin mononucleotide (FMN)NADPH–cytochrome P450 reductase (CPR)nicotinamide adenine dinucleotide phosphate (NADPH)protein–protein interaction

Identifiers

PMID41011624
PMCPMC12472590

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.