Evidence map›Paper›PMID 31483745›Full record

ArticleMolecular biology of the cell2019

A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network.

Chalongrat Noree, Kyle Begovich, Dane Samilo, Risa Broyer, Elena Monfort, James E Wilhelm

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.3field-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

56 citing papers in PubMed, 91 citations in OpenAlex.

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  6. Structural basis of secreted acid phosphatase polymerization in the Leishmania parasite.Protein science : a publication of the Protein Society · 2026
    Article
  7. Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026
    Review
  8. Review
  9. Article
  10. Beyond contacts: The important role of the support region in protein complex assembly.Protein science : a publication of the Protein Society · 2026
    Article
  11. Review
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  18. Cytoophidium complexes resonate with cell fates.Cellular and molecular life sciences : CMLS · 2025
    Article
  19. Article
  20. Article
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

6 authors at 2 institutions in 2 countries.

Chalongrat NoreeHoward Hughes Medical Institute Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543.
Kyle BegovichHoward Hughes Medical Institute Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543.
Dane SamiloDivision of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Risa BroyerDivision of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Elena MonfortDivision of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
James E WilhelmHoward Hughes Medical Institute Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543.
Marine Biological Laboratory · USUniversity of California San Diego · US

Funding

GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
NIGMS NIH HHS T32 GM007240
6 · The paper itself

Abstract

Despite the proliferation of proteins that can form filaments or phase-separated condensates, it remains unclear how this behavior is distributed over biological networks. We have found that 60 of the 440 yeast metabolic enzymes robustly form structures, including 10 that assemble within mitochondria. Additionally, the ability to assemble is enriched at branch points on several metabolic pathways. The assembly of enzymes at the first branch point in de novo purine biosynthesis is coordinated, hierarchical, and based on their position within the pathway, while the enzymes at the second branch point are recruited to RNA stress granules. Consistent with distinct classes of structures being deployed at different control points in a pathway, we find that the first enzyme in the pathway, PRPP synthetase, forms evolutionarily conserved filaments that are sequestered in the nucleus in higher eukaryotes. These findings provide a roadmap for identifying additional conserved features of metabolic regulation by condensates/filaments.

Indexed as

Metabolic Networks and PathwaysGene Expression Regulation, EnzymologicGene Expression Regulation, FungalLuminescent ProteinsMicroscopy, FluorescenceMitochondrial ProteinsRibose-Phosphate PyrophosphokinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLuminescent ProteinsMitochondrial ProteinsRibose-Phosphate PyrophosphokinaseSaccharomyces cerevisiae Proteins

Identifiers

PMID31483745
PMCPMC6761767
OpenAlexW2971839298

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.