ArticleSynthetic and systems biotechnology2026
Malic enzyme-based system for transhydrogenation between nicotinamide cofactors.
Article in Synthetic and systems biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
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.
Who cites it
3 citing papers in PubMed.
- Reprogramming the Rossmann fold signature motif creates orthogonal redox biocatalysts.Nature communications · 2026Article
- Multi-omics analyses reveal cellular responses to biosynthesis of the non-natural cofactor nicotinamide cytosine dinucleotide.Frontiers in bioengineering and biotechnology · 2026Article
- Reprogramming the Rossmann Fold Signature Motif Creates Orthogonal Redox Biocatalysts.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nicotinamide cofactors including nicotinamide adenine dinucleotide (NAD) and its phosphate (NADP) play important roles in facilitating redox reactions for energy metabolism and biosynthesis. To expand the cofactor menu, a non-natural cofactor nicotinamide cytosine dinucleotide (NCD) has been introduced recently. The reduced forms of these cofactors carry reducing equivalents that are essential for cellular metabolism. However, there is a long standing challenge to rationally transfer reducing equivalent from one cofactor to another, albeit such process is highly demanding in metabolic engineering. This study develops a new approach based on malic enzyme (ME)-mediated transhydrogenation to enable reducing equivalents exchange among different cofactors. We used wild-type ME, MaeB and an engineered ME∗ that favors NAD, NADP and NCD, respectively, to demonstrate such conversions. When an
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.