Evidence map›Paper›PMID 42107642›Full record

ArticleThe Journal of biological chemistry2026

A high-sensitivity strategy to screen NAD(P)H-dependent reductase activity by coupled enzyme cascade.

Trisha Ghosh, Jacob Sicheri, David H Kwan

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Trisha GhoshDepartment of Biology, Concordia University, Montreal, Quebec, Canada.
Jacob SicheriDepartment of Biology, Concordia University, Montreal, Quebec, Canada.
David H KwanDepartment of Biology, Concordia University, Montreal, Quebec, Canada; Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada. Electronic address: david.kwan@concordia.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes play a pivotal role in "green chemistry" as tools for biocatalysis. Oxidoreductase enzymes are especially useful for carrying out key electron transfer (redox) steps toward a wide range of chemical transformations (e.g., asymmetric hydrogenation, oxygenation, hydroxylation, epoxidation, or Baeyer-Villiger oxidation) that might not otherwise be available to chemists through conventional (nonbiological) synthetic approaches. The ability to screen oxidoreductase activity is important in identifying useful biocatalysts from nature, and also toward engineering novel ones through directed evolution. Many valuable redox enzymes are dependent upon NAD(P)H as an electron-donating co-substrate (or conversely, upon NAD(P)

Indexed as

NADPOxidoreductasesBiocatalysisOxidation-ReductionNADPOxidoreductasesBiocatalysisEnzyme cascadeFluorescence-based assayGreen chemistryhigh throughput screeningNAD(P)HOxidoreductase

Identifiers

PMID42107642
PMCPMC13264166

What OpenQuestion holds

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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.