{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:48:43Z","timestamp":1790254123161,"version":"4.1.0"},"reference-count":97,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2021,4,13]],"date-time":"2021-04-13T00:00:00Z","timestamp":1618272000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.3390\/cells10040883","type":"journal-article","created":{"date-parts":[[2021,4,13]],"date-time":"2021-04-13T10:58:07Z","timestamp":1618311487000},"page":"883","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":72,"title":["Muscle Glycogen Phosphorylase and Its Functional Partners in Health and Disease"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0077-7779","authenticated-orcid":false,"given":"Marta","family":"Migocka-Patrza\u0142ek","sequence":"first","affiliation":[{"name":"Department of Animal Developmental Biology, Faculty of Biological Sciences, University of Wroclaw, 50-335 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magdalena","family":"Elias","sequence":"additional","affiliation":[{"name":"Department of Animal Developmental Biology, Faculty of Biological Sciences, University of Wroclaw, 50-335 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,4,13]]},"reference":[{"key":"ref_1","first-page":"35","article-title":"Muscle glycogenoses: An overview","volume":"26","year":"2007","journal-title":"Acta Myol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s10545-014-9743-2","article-title":"The pathogenomics of McArdle disease\u2014Genes, enzymes, models, and therapeutic implications","volume":"38","author":"Santalla","year":"2015","journal-title":"J. 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