Evidence map›Paper›PMID 41427637›Full record

ArticleThe journal of physical chemistry. B2026

Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell.

Enguang Fu, Zane R Thornburg, Troy A Brier, Rong Wei, Bo Yuan, Benjamin R Gilbert, Shulei Wang, Zaida Luthey-Schulten

Abstract read
In one paragraph

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

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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

8 authors.

Enguang FuDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0009-0007-4631-3351
Zane R ThornburgBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Troy A BrierDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-9530-6517
Rong WeiNational Science Foundation Science and Technology Center for Quantitative Cell Biology, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Bo YuanNational Science Foundation Science and Technology Center for Quantitative Cell Biology, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Benjamin R GilbertDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-9344-5521
Shulei WangNational Science Foundation Science and Technology Center for Quantitative Cell Biology, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Zaida Luthey-SchultenDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0001-9749-8367

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macromolecular complexes in the genetically minimized bacterium, JCVI-syn3A, support gene expression (RNA polymerase, ribosome, degradosome), metabolism (ABC transporters, ATP synthase), and chromosome dynamics. In this work, we further incorporate the assembly of 21 unique macromolecular complexes into the existing whole-cell kinetic model of Syn3A. The synthesis and translocation of protein subunits in membrane complexes occur through distinct pathways. A range of 2D association rates for membrane complexes were considered to guarantee a high yield of assembly, given the existing time scales of gene expression. By alleviation of the undesired kinetically trapped intermediates in ATP synthase assembly, the efficiency was improved. The assembly of RNA polymerase, ribosome, and degradosome influences the speed and efficiency of protein synthesis. Collectively, this model predicted time-dependent cellular behaviors consistent with experiments. A machine learning analysis of the time-dependent metabolomics and metabolic fluxes highlighted the effect of introducing a complex assembly into our whole-cell model.

Indexed as

Macromolecular SubstancesModels, BiologicalKineticsMachine LearningRibosomesMacromolecular Substances

Identifiers

PMID41427637
PMCPMC12794154

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.