{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T01:44:38Z","timestamp":1789177478728,"version":"build-2803163510"},"reference-count":30,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2016,11,12]],"date-time":"2016-11-12T00:00:00Z","timestamp":1478908800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100005736","name":"Universit\u00e9 Paris Diderot","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005736","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004794","name":"Centre National de la Recherche Scientifique","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004794","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:p>Glycogen phosphorylase (<jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content>) is the key enzyme that regulates glycogen mobilization in cells. <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> is a complex allosteric enzyme that comprises a family of three isozymes: muscle <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> (<jats:styled-content style=\"fixed-case\">mGP<\/jats:styled-content>), liver <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> (<jats:styled-content style=\"fixed-case\">lGP<\/jats:styled-content>), and brain <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> (<jats:styled-content style=\"fixed-case\">bGP<\/jats:styled-content>). Although the three isozymes display high similarity and catalyze the same reaction, they differ in their sensitivity to the allosteric activator adenosine monophosphate (<jats:styled-content style=\"fixed-case\">AMP<\/jats:styled-content>). Moreover, inactivating mutations in <jats:styled-content style=\"fixed-case\">mGP<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">lGP<\/jats:styled-content> have been known to be associated with glycogen storage diseases (McArdle and Hers disease, respectively). The determination, decades ago, of the structure of <jats:styled-content style=\"fixed-case\">mGP<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">lGP<\/jats:styled-content> have allowed to better understand the allosteric regulation of these two isoforms and the development of specific inhibitors. Despite its important role in brain glycogen metabolism, the structure of the brain <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> had remained elusive. Here, we provide an overview of the human brain <jats:styled-content style=\"fixed-case\">GP<\/jats:styled-content> structure and its relationship with the two other members of this key family of the metabolic enzymes. We also summarize how this structure provides valuable information to understand the regulation of <jats:styled-content style=\"fixed-case\">bGP<\/jats:styled-content> and to design specific ligands of potential pharmacological interest.<\/jats:p>","DOI":"10.1111\/febs.13937","type":"journal-article","created":{"date-parts":[[2016,11,16]],"date-time":"2016-11-16T16:05:54Z","timestamp":1479312354000},"page":"546-554","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["The structure of brain glycogen phosphorylase\u2014from allosteric regulation mechanisms to clinical perspectives"],"prefix":"10.1111","volume":"284","author":[{"given":"C\u00e9cile","family":"Mathieu","sequence":"first","affiliation":[{"name":"Sorbonne Paris Cit\u00e9 Unit\u00e9 BFA, CNRS UMR 8251 Universit\u00e9 Paris Diderot 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