Evidence map›Paper›PMID 23057741›Full record

ReviewAnnual review of cell and developmental biology2012

Dynamic reorganization of metabolic enzymes into intracellular bodies.

Jeremy D O'Connell, Alice Zhao, Andrew D Ellington, Edward M Marcotte

Abstract readReview
In one paragraph

Review in Annual review of cell and developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

82 citing papers in PubMed, 150 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. The metabolic enzyme GYS1 condenses with NONO/p54Cell death and differentiation · 2025
    Article
  7. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.Protein science : a publication of the Protein Society · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Cellular quiescence in budding yeast.Yeast (Chichester, England) · 2021
    Review
  19. Quiescence Through the Prism of Evolution.Frontiers in cell and developmental biology · 2021
    Article
  20. Article

22 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

4 authors at 2 institutions in 2 countries.

Jeremy D O'ConnellCenter for Systems and Synthetic Biology, University of Texas, Austin, Texas 78712, USA.
Alice Zhao
Andrew D Ellington
Edward M Marcotte
The University of Texas at Austin · USInstitut de Biologie systémique et synthétique · FR

Funding

Proteomics of widespread, reversible protein assemblies in aging and aggregationR01GM076536 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2006 to 2014
$2.9M
NIGMS NIH HHS R01 GM076536
6 · The paper itself

Abstract

Both focused and large-scale cell biological and biochemical studies have revealed that hundreds of metabolic enzymes across diverse organisms form large intracellular bodies. These proteinaceous bodies range in form from fibers and intracellular foci--such as those formed by enzymes of nitrogen and carbon utilization and of nucleotide biosynthesis--to high-density packings inside bacterial microcompartments and eukaryotic microbodies. Although many enzymes clearly form functional mega-assemblies, it is not yet clear for many recently discovered cases whether they represent functional entities, storage bodies, or aggregates. In this article, we survey intracellular protein bodies formed by metabolic enzymes, asking when and why such bodies form and what their formation implies for the functionality--and dysfunctionality--of the enzymes that comprise them. The panoply of intracellular protein bodies also raises interesting questions regarding their evolution and maintenance within cells. We speculate on models for how such structures form in the first place and why they may be inevitable.

Indexed as

AnimalsCytoplasmic GranulesEscherichia coliEscherichia coli ProteinsFungal ProteinsHumansMetabolic Networks and PathwaysPeroxisomesProtein Structure, QuaternaryProtein TransportYeastsEscherichia coli ProteinsFungal Proteins

Identifiers

PMID23057741
PMCPMC4089986
OpenAlexW2101627628

What OpenQuestion holds

Textmetadata
LicenceTDM
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.