Evidence map›Paper›PMID 41755815›Full record

ArticleJACS Au2026

Conserved-Potential-Driven Molecular Dynamics Deciphers Formose Reaction Mechanisms.

Hei Wun Kan, Xiao-Tian Li, Tong Zhu, Yuzhi Xu, John Zeng Hui Zhang

Abstract read
In one paragraph

Article in JACS Au, 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

5 authors.

Hei Wun KanFaculty of Synthetic Biology, Shenzhen University of Advanced Technology, Shenzhen 518107, China.ORCID https://orcid.org/0000-0003-4566-5746
Xiao-Tian LiFaculty of Synthetic Biology, Shenzhen University of Advanced Technology, Shenzhen 518107, China.ORCID https://orcid.org/0009-0003-2526-0722
Tong ZhuShanghai Engineering Research Center of Molecular Therapeutics and New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China.ORCID https://orcid.org/0000-0001-7472-3736
Yuzhi XuNYU-ECNU Center for Computational Chemistry, NYU Shanghai, Shanghai 200126, China.ORCID https://orcid.org/0000-0002-3325-5427
John Zeng Hui ZhangFaculty of Synthetic Biology, Shenzhen University of Advanced Technology, Shenzhen 518107, China.ORCID https://orcid.org/0000-0003-4612-1863

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formose reaction, in which formaldehyde reacts to form sugars under alkaline conditions, is a leading candidate for prebiotic sugar synthesis, with ribose as a particularly significant though minor product. Despite the simplicity of its starting material (formaldehyde), the reaction involves intricate mechanistic steps and generates a complex product mixture, hindering full mechanistic elucidation even after decades of study. Here, we develop an efficient, mechanism-free molecular dynamics (MD) approach to simulate the formose reaction, using our recently proposed roto-translationally invariant potential (RTIP) to drive the molecular system toward reactive configurations for potential reactions. High-resolution RTIP-MD trajectories reveal a comprehensive reaction network, elucidating previously elusive mechanistic details for formaldehyde self-condensation, aldose-ketose tautomerization, and ribose synthesis. Based on the Gibbs free energy landscape, the microkinetic simulation conclusively settles the autocatalytic cycle debate, demonstrating that autocatalysis occurs predominantly at low glycolaldehyde concentrations, as evidenced by the reverse aldotetrose retroaldol cleavage. This proof-of-concept study demonstrates RTIP-MD's capability to simulate complex, multistep reactions, suggesting potential applicability to challenging systems such as enzyme catalysis.

Indexed as

autocatalytic cycleformaldehyde self-condensationformose reactionribose synthesisRTIP-MD

Identifiers

PMID41755815
PMCPMC12933356

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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.