{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T04:49:12Z","timestamp":1790743752972,"version":"4.1.0"},"reference-count":32,"publisher":"Elsevier BV","issue":"46","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":2136,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2014,11]]},"DOI":"10.1074\/jbc.m114.597914","type":"journal-article","created":{"date-parts":[[2014,10,7]],"date-time":"2014-10-07T07:04:59Z","timestamp":1412665499000},"page":"32010-32019","source":"Crossref","is-referenced-by-count":49,"title":["Compromised Catalysis and Potential Folding Defects in in Vitro Studies of Missense Mutants Associated with Hereditary Phosphoglucomutase 1 Deficiency"],"prefix":"10.1016","volume":"289","author":[{"given":"Yingying","family":"Lee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyle M.","family":"Stiers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bailee N.","family":"Kain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lesa J.","family":"Beamer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M114.597914_bib1","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1007\/s10545-012-9525-7","article-title":"A novel congenital disorder of glycosylation type without central nervous system involvement caused by mutations in the phosphoglucomutase 1 gene","volume":"36","author":"P\u00e9rez","year":"2013","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.597914_bib2","doi-asserted-by":"crossref","first-page":"4151","DOI":"10.1093\/hmg\/dds123","article-title":"Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing","volume":"21","author":"Timal","year":"2012","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.597914_bib3","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1056\/NEJMoa1206605","article-title":"Multiple phenotypes in phosphoglucomutase 1 deficiency","volume":"370","author":"Tegtmeyer","year":"2014","journal-title":"N. Engl. J. Med"},{"key":"10.1074\/jbc.M114.597914_bib4","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1056\/NEJMc0901158","article-title":"Muscle glycogenosis due to phosphoglucomutase 1 deficiency","volume":"361","author":"Stojkovic","year":"2009","journal-title":"N. Engl. J. Med"},{"key":"10.1074\/jbc.M114.597914_bib5","first-page":"137","article-title":"Glycogen storage disease-like phenotype with central nervous system involvement in a PGM1-CDG patient","volume":"35","author":"Ondruskova","year":"2014","journal-title":"Neuro. Endocrinol. Lett"},{"key":"10.1074\/jbc.M114.597914_bib6","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1007\/s10545-006-0301-4","article-title":"Protein misfolding disorders: pathogenesis and intervention","volume":"29","author":"Gregersen","year":"2006","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.597914_bib7","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1007\/s10545-014-9701-z","article-title":"Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators","volume":"37","author":"Muntau","year":"2014","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.597914_bib8","doi-asserted-by":"crossref","first-page":"3680","DOI":"10.1093\/hmg\/ddt217","article-title":"Pharmacological chaperones as a potential therapeutic option in methylmalonic aciduria cblB type","volume":"22","author":"Jorge-Finnigan","year":"2013","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.597914_bib9","doi-asserted-by":"crossref","first-page":"11","DOI":"10.3892\/ijmm.2012.1187","article-title":"New strategies for the treatment of lysosomal storage diseases (review)","volume":"31","author":"Parenti","year":"2013","journal-title":"Int. J. Mol. Med"},{"key":"10.1074\/jbc.M114.597914_bib10","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/j.1432-1033.1974.tb03366.x","article-title":"A kinetic study of the isozymes determined by the three human phosphoglucomutase loci PGM1, PGM2 and PGM3","volume":"42","author":"Quick","year":"1974","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M114.597914_bib11","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1107\/S0907444997000875","article-title":"Structure of rabbit muscle phosphoglucomutase refined at 2.4-\u00c5 resolution","volume":"53","author":"Liu","year":"1997","journal-title":"Acta Crystallogr. D"},{"key":"10.1074\/jbc.M114.597914_bib12","doi-asserted-by":"crossref","first-page":"2130","DOI":"10.1110\/ps.04801104","article-title":"Evolutionary trace analysis of the \u03b1-d-phosphohexomutase superfamily","volume":"13","author":"Shackelford","year":"2004","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M114.597914_bib13","article-title":"Mutations in hereditary phosphoglucomutase 1 deficiency map to key regions of enzyme structure and function","author":"Beamer","year":"2014","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.597914_bib14","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1093\/oxfordjournals.molbev.a025942","article-title":"A phylogenetic approach to the identification of phosphoglucomutase genes","volume":"15","author":"Whitehouse","year":"1998","journal-title":"Mol. Biol. Evol"},{"key":"10.1074\/jbc.M114.597914_bib15","doi-asserted-by":"crossref","first-page":"10725","DOI":"10.1073\/pnas.90.22.10725","article-title":"Intragenic recombination at the human phosphoglucomutase 1 locus: predictions fulfilled","volume":"90","author":"Takahashi","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.597914_bib16","doi-asserted-by":"crossref","first-page":"10730","DOI":"10.1073\/pnas.90.22.10730","article-title":"The classical human phosphoglucomutase (PGM1) isozyme polymorphism is generated by intragenic recombination","volume":"90","author":"March","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.597914_bib17","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/j.1469-1809.1970.tb00230.x","article-title":"The relative activities attributable to the three phosphoglucomutase loci (PGM1, PGM2, PGM3) in human tissues","volume":"34","author":"McAlpine","year":"1970","journal-title":"Ann. Hum. Genet"},{"key":"10.1074\/jbc.M114.597914_bib18","doi-asserted-by":"crossref","first-page":"2770","DOI":"10.1021\/bi00463a021","article-title":"Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques","volume":"29","author":"Ray","year":"1990","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M114.597914_bib19","doi-asserted-by":"crossref","first-page":"2705","DOI":"10.1021\/jm301557k","article-title":"Pharmacological chaperones as therapeutics for lysosomal storage diseases","volume":"56","author":"Boyd","year":"2013","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M114.597914_bib20","doi-asserted-by":"crossref","first-page":"4674","DOI":"10.1074\/jbc.M113.532226","article-title":"Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase","volume":"289","author":"Lee","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597914_bib21","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1046\/j.1432-1327.1999.00373.x","article-title":"Reaction mechanism of phosphoglucosamine mutase from Escherichia coli","volume":"262","author":"Jolly","year":"1999","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M114.597914_bib22","doi-asserted-by":"crossref","first-page":"8118","DOI":"10.1038\/sj.onc.1207969","article-title":"Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase","volume":"23","author":"Gururaj","year":"2004","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M114.597914_bib23","doi-asserted-by":"crossref","first-page":"15866","DOI":"10.1074\/jbc.M110.107722","article-title":"Rescue of cystathionine-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight cbs mutant enzymes","volume":"285","author":"Majtan","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597914_bib24","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1002\/humu.1380060305","article-title":"Comparison between medium-chain acyl-CoA dehydrogenase mutant proteins overexpressed in bacterial and mammalian cells","volume":"6","author":"Jensen","year":"1995","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.M114.597914_bib25","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1093\/hmg\/ddp079","article-title":"Protein misfolding is the molecular mechanism underlying MCADD identified in newborn screening","volume":"18","author":"Maier","year":"2009","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.597914_bib26","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1007\/s10545-011-9328-2","article-title":"Expression analysis revealing destabilizing mutations in phosphomannomutase 2 deficiency (PMM2-CDG)","volume":"34","author":"Vega","year":"2011","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.597914_bib27","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.bbadis.2010.09.015","article-title":"Phenylketonuria as a protein misfolding disease: the mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation","volume":"1812","author":"Leandro","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M114.597914_bib28","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1006\/mgme.2000.2965","article-title":"Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype","volume":"69","author":"Waters","year":"2000","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.597914_bib29","doi-asserted-by":"crossref","first-page":"29737","DOI":"10.1074\/jbc.M003231200","article-title":"Expression analysis of phenylketonuria mutations: effect on folding and stability of the phenylalanine hydroxylase protein","volume":"275","author":"G\u00e1mez","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597914_bib30","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1097\/MAJ.0b013e3180a5e934","article-title":"Phosphoglucomutase genetic polymorphism and body mass","volume":"334","author":"Gloria-Bottini","year":"2007","journal-title":"Am. J. Med. Sci"},{"key":"10.1074\/jbc.M114.597914_bib31","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1002\/ajhb.1066","article-title":"Birth weight and parental PGM1 alleles","volume":"13","author":"Gloria-Bottini","year":"2001","journal-title":"Am. J. Hum. Biol"},{"key":"10.1074\/jbc.M114.597914_bib32","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.ymgme.2014.06.002","article-title":"Galactose supplementation in phosphoglucomutase-1 deficiency: review and outlook for a novel treatable CDG","volume":"112","author":"Morava","year":"2014","journal-title":"Mol. Genet. Metab"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820332889?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820332889?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M114.597914","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T05:35:42Z","timestamp":1641274542000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820332889"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11]]},"references-count":32,"journal-issue":{"issue":"46","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["S0021925820332889"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m114.597914","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2014,11]]}}}