Evidence map›Paper›PMID 34668544›Full record

ReviewJournal of cell science2021

Compartmentalization and metabolic regulation of glycolysis.

Gregory G Fuller, John K Kim

Abstract readReview
In one paragraph

Review in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Article
  2. Retbindin Dynamically Redistributes to Preserve Retinal Flavin-Dependent Homeostasis in Response to Riboflavin Availability and Circadian Demand.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Direct energy consumption by inhibitory GABAFrontiers in neuroscience · 2026
    Article
  16. Loss ofLife science alliance · 2026
    Article
  17. Review
  18. Article
  19. Targeting the Glutaminolysis Pathway in Glaucoma-Associated Fibrosis.International journal of molecular sciences · 2025
    Review
  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

2 authors.

Gregory G FullerDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0003-2960-0256
John K KimDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0001-9838-3254

Funding

Formation and Function of Glycolytic Bodies in HypoxiaR01GM129301 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KIM, JOHN · 2018 to 2021
$1.9M
NIGMS NIH HHS R01 GM129301NIH HHS R01 GM129301
6 · The paper itself

Abstract

Hypoxia inhibits the tricarboxylic acid (TCA) cycle and leaves glycolysis as the primary metabolic pathway responsible for converting glucose into usable energy. However, the mechanisms that compensate for this loss in energy production due to TCA cycle inactivation remain poorly understood. Glycolysis enzymes are typically diffuse and soluble in the cytoplasm under normoxic conditions. In contrast, recent studies have revealed dynamic compartmentalization of glycolysis enzymes in response to hypoxic stress in yeast, C. elegans and mammalian cells. These messenger ribonucleoprotein (mRNP) structures, termed glycolytic (G) bodies in yeast, lack membrane enclosure and display properties of phase-separated biomolecular condensates. Disruption of condensate formation correlates with defects such as impaired synaptic function in C. elegans neurons and decreased glucose flux in yeast. Concentrating glycolysis enzymes into condensates may lead to their functioning as 'metabolons' that enhance rates of glucose utilization for increased energy production. Besides condensates, glycolysis enzymes functionally associate in other organisms and specific tissues through protein-protein interactions and membrane association. However, as discussed in this Review, the functional consequences of coalescing glycolytic machinery are only just beginning to be revealed. Through ongoing studies, we anticipate the physiological importance of metabolic regulation mediated by the compartmentalization of glycolysis enzymes will continue to emerge.

Indexed as

Caenorhabditis elegansGlycolysisAnimalsCitric Acid CycleGlucoseSaccharomyces cerevisiaeGlucoseCondensateG bodyGlycolysisHypoxia

Identifiers

PMID34668544
PMCPMC8572002

What OpenQuestion holds

Textmetadata
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.