Evidence map›Paper›PMID 27801646›Full record

ArticleeLife2016

Biomolecular interactions modulate macromolecular structure and dynamics in atomistic model of a bacterial cytoplasm.

Isseki Yu, Takaharu Mori, Tadashi Ando, Ryuhei Harada, Jaewoon Jung, Yuji Sugita, Michael Feig

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
20.9field-weighted citation impact, top 1% of its field
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

147 citing papers in PubMed, 310 citations in OpenAlex.

  1. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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  3. Article
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  5. Compartment-guided assembly of large-scale molecular models with Bentopy.Protein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  15. Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

87 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Isseki YuiTHES Research Group, RIKEN, Saitama, Japan.
Takaharu MoriiTHES Research Group, RIKEN, Saitama, Japan.
Tadashi AndoLaboratory for Biomolecular Function Simulation, RIKEN Quantitative Biology Center, Kobe, Japan.
Ryuhei HaradaComputational Biophysics Research Team, RIKEN Advanced Institute for Computational Science, Kobe, Japan.
Jaewoon JungComputational Biophysics Research Team, RIKEN Advanced Institute for Computational Science, Kobe, Japan.
Yuji SugitaiTHES Research Group, RIKEN, Saitama, Japan.
Michael FeigLaboratory for Biomolecular Function Simulation, RIKEN Quantitative Biology Center, Kobe, Japan.ORCID 0000-0001-9380-6422
RIKEN Center for Computational Science · JPRIKEN · JP

Funding

Protein structure refinement through effective sampling and scoringR01GM084953 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FEIG, MICHAEL · 2008 to 2017
$2.5M
Multiscale modeling of supramolecular protein-DNA assembliesR01GM092949 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FEIG, MICHAEL · 2010 to 2013
$1.1M
NIGMS NIH HHS R01 GM084953NIGMS NIH HHS R01 GM092949
6 · The paper itself

Abstract

Biological macromolecules function in highly crowded cellular environments. The structure and dynamics of proteins and nucleic acids are well characterized in vitro, but in vivo crowding effects remain unclear. Using molecular dynamics simulations of a comprehensive atomistic model cytoplasm we found that protein-protein interactions may destabilize native protein structures, whereas metabolite interactions may induce more compact states due to electrostatic screening. Protein-protein interactions also resulted in significant variations in reduced macromolecular diffusion under crowded conditions, while metabolites exhibited significant two-dimensional surface diffusion and altered protein-ligand binding that may reduce the effective concentration of metabolites and ligands in vivo. Metabolic enzymes showed weak non-specific association in cellular environments attributed to solvation and entropic effects. These effects are expected to have broad implications for the in vivo functioning of biomolecules. This work is a first step towards physically realistic in silico whole-cell models that connect molecular with cellular biology.

Indexed as

CytoplasmMacromolecular SubstancesMolecular Dynamics SimulationMycoplasma genitaliumSpatio-Temporal AnalysisMacromolecular Substancesbiophysicscomputational biologycrowding effectsdiffusionmetabolite dynamicsnative state stabilitynonequinary interactionsstructural biologysystems biologywhole-cell modeling

Identifiers

PMID27801646
PMCPMC5089862
OpenAlexW2542660070

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.