Evidence map›Paper›PMID 31871201›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Lessons from equilibrium statistical physics regarding the assembly of protein complexes.

Pablo Sartori, Stanislas Leibler

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Fuel-Driven Catalytic Molecular Templating.Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. Liquid Hopfield model: Retrieval and localization in multicomponent liquid mixtures.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Discovering optimal kinetic pathways for self-assembly using automatic differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Evolved interactions stabilize many coexisting phases in multicomponent liquids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Complex Portal 2022: new curation frontiers.Nucleic acids research · 2022
    Article
  14. Article
  15. Review
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

2 authors.

Pablo SartoriThe Simons Center for Systems Biology, Institute for Advanced Study, Princeton, NJ 08540; psartori@rockefeller.edu livingmatter@rockefeller.edu.
Stanislas LeiblerThe Simons Center for Systems Biology, Institute for Advanced Study, Princeton, NJ 08540; psartori@rockefeller.edu livingmatter@rockefeller.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular functions are established through biological evolution, but are constrained by the laws of physics. For instance, the physics of protein folding limits the lengths of cellular polypeptide chains. Consequently, many cellular functions are carried out not by long, isolated proteins, but rather by multiprotein complexes. Protein complexes themselves do not escape physical constraints, one of the most important being the difficulty of assembling reliably in the presence of cellular noise. In order to lay the foundation for a theory of reliable protein complex assembly, we study here an equilibrium thermodynamic model of self-assembly that exhibits 4 distinct assembly behaviors: diluted protein solution, liquid mixture, "chimeric assembly," and "multifarious assembly." In the latter regime, different protein complexes can coexist without forming erroneous chimeric structures. We show that 2 conditions have to be fulfilled to attain this regime: 1) The composition of the complexes needs to be sufficiently heterogeneous, and 2) the use of the set of components by the complexes has to be sparse. Our analysis of publicly available databases of protein complexes indicates that cellular protein systems might have indeed evolved so as to satisfy both of these conditions.

Indexed as

Chemical PhenomenaMechanical PhenomenaModels, StructuralMultiprotein ComplexesProtein FoldingProteinsThermodynamicsMultiprotein ComplexesProteinsprotein complexself-assembly

Identifiers

PMID31871201
PMCPMC6955335

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.