A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle.

By D. Milan, J. Jeon, C. Looft, V. Amarger, A. Robic, Mattias Thelander, C. Rogel-Gaillard, S. Paul, N. Iannuccelli, L. Rask and 8 more. Science, 2000

768 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d8f7d89f1b9a3d7869f36d03792a4047408500d5

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In Molecular Biology

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Citations in the corpus

• Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. (2005, background): “…substi-tution (R200Q) in the PRKAG3 gene that causes high glycogen content in skeletal muscle resulting in detrimental effects on processing yield (Milan et al., 2000), other alleles within the same gene are associated with lower muscle glycogen content, and improved meat quality traits (Ciobanu…”
• AMP‐activated protein kinase: the energy charge hypothesis revisited (2001, background): “, another hypertrophic response.((49)) This mutation, R200Q, is in CBS1 of g3 and aligns perfectly with the R302Q and H383R mutations in CBS1 and CBS2 of g2.”
• Intrasteric control of AMPK via the γ1 subunit AMP allosteric regulatory site (2004, background): “The importance of AMPK in regulating glucose metabolism has been strongly highlighted by the discovery of a series of mutations in the AMPK subunit genes that cause glycogen storage disease in humans (Blair et al. 2001), pigs (Milan et al. 2000), and yeast (Cannon et al. 1994).”
• CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. (2004, background): “Thus, the R302Q, H383R, and R531G mutations in CBS1, CBS2, and CBS4 of γ2 all align (plus or minus one residue) with the D444N mutation in cystathionine β-synthase and with the R200Q mutation in CBS1 of the γ3 isoform of pig AMPK (13).”
• How Muscle Structure and Composition Influence Meat and Flesh Quality (2016, background): “Another pork quality defect is due to a mutation in the PRKAG3 gene that encodes a subunit of the AMP-activated protein kinase (AMPK) [69].”
• Glycogen and its metabolism: some new developments and old themes. (2012, background): “A rather different connection between AMPK and glycogen comes from study of Hampshire pigs [189] and PRKAG2 (AMPK γ2 non-catalytic subunit) mutations in humans [190] which cause massive overaccumulation of glycogen in muscle and heart respectively.”
• The AMP-activated protein kinase cascade--a unifying system for energy control. (2004, methodology): “mutation was identified as a missense mutation in AMPK g3, altering arginine at residue 225 (the numbering used here corresponds to the position of the residue within the predicted full-length sequence of pig g3 [33] )t o a glutamine (R225Q) [ 34 ].”
• AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. (2005, background): “If correct, this would help explain why the mutations are dominant and appear to act as gain-offunction mutations, as does a similar mutation in γ3 in pigs (R225Q, equivalent to R302Q in γ2) (Milan et al., 2000).”