Evidence map›Paper›PMID 33924466›Full record

ReviewCells2021

Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease.

Marta Migocka-Patrzałek, Magdalena Elias

Abstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Trial
  2. Protein phosphatase 2A impairs cardiac uptake of glucose in the mammalian heart.Naunyn-Schmiedeberg's archives of pharmacology · 2026
    Article
  3. Article
  4. Phenotype-specific muscle proteomic profiling in titinopathies.Acta neuropathologica communications · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Astrocytic PYGM attenuates tau pathology by promoting lactate-mediated neuroprotection.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Steaming duration-dependent effects on theFrontiers in pharmacology · 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

2 authors.

Marta Migocka-PatrzałekDepartment of Animal Developmental Biology, Faculty of Biological Sciences, University of Wroclaw, 50-335 Wroclaw, Poland.ORCID 0000-0003-0077-7779
Magdalena EliasDepartment of Animal Developmental Biology, Faculty of Biological Sciences, University of Wroclaw, 50-335 Wroclaw, Poland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycogen phosphorylase (PG) is a key enzyme taking part in the first step of glycogenolysis. Muscle glycogen phosphorylase (PYGM) differs from other PG isoforms in expression pattern and biochemical properties. The main role of PYGM is providing sufficient energy for muscle contraction. However, it is expressed in tissues other than muscle, such as the brain, lymphoid tissues, and blood. PYGM is important not only in glycogen metabolism, but also in such diverse processes as the insulin and glucagon signaling pathway, insulin resistance, necroptosis, immune response, and phototransduction. PYGM is implicated in several pathological states, such as muscle glycogen phosphorylase deficiency (McArdle disease), schizophrenia, and cancer. Here we attempt to analyze the available data regarding the protein partners of PYGM to shed light on its possible interactions and functions. We also underline the potential for zebrafish to become a convenient and applicable model to study PYGM functions, especially because of its unique features that can complement data obtained from other approaches.

Indexed as

AnimalsDisease Models, AnimalGene Expression RegulationGlycogenGlycogen PhosphorylaseGlycogen Storage Disease Type VHumansInsulin ResistanceLight Signal TransductionMuscle ContractionMuscle, SkeletalNecroptosisNeoplasmsProtein Interaction MappingRetinal Pigment EpitheliumSchizophreniaGlycogenGlycogen Phosphorylasecancerfunctional protein partnersglycogenolysisMcArdle diseasemuscle glycogen phosphorylasePYGMschizophrenia

Identifiers

PMID33924466
PMCPMC8070155

What OpenQuestion holds

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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.