{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T11:13:25Z","timestamp":1790680405913,"version":"4.1.0"},"reference-count":50,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2017,4,13]],"date-time":"2017-04-13T00:00:00Z","timestamp":1492041600000},"content-version":"am","delay-in-days":377,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100006151","name":"Basic Energy Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006151","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006132","name":"Office of Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006132","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-AC02-05CH11231"],"award-info":[{"award-number":["DE-AC02-05CH11231"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB-0918389"],"award-info":[{"award-number":["MCB-0918389"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2016,4]]},"DOI":"10.1016\/j.jmb.2016.02.032","type":"journal-article","created":{"date-parts":[[2016,3,10]],"date-time":"2016-03-10T20:46:28Z","timestamp":1457642788000},"page":"1493-1505","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"title":["Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency"],"prefix":"10.1016","volume":"428","author":[{"given":"Kyle M.","family":"Stiers","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bailee N.","family":"Kain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abigail C.","family":"Graham","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":"10.1016\/j.jmb.2016.02.032_bb0005","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":"10.1016\/j.jmb.2016.02.032_bb0010","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":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.jmb.2016.02.032_bb0015","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":"10.1016\/j.jmb.2016.02.032_bb0020","first-page":"87","article-title":"A case with rare type of congential-disorder of glycosylation: PGM1-CDG","volume":"26","author":"Kucukcongar","year":"2015","journal-title":"Genet. Couns."},{"key":"10.1016\/j.jmb.2016.02.032_bb0025","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":"10.1016\/j.jmb.2016.02.032_bb0030","unstructured":"S. Wong, L.J. Beamer, T. Gadomski, T. Honzik, M. Mohamed, S.B. Wortmann, et al., Defining the phenotype and assessing severity in Phosphoglucomutase-1 deficiency, J. Pediatr. Biochem. (in press)."},{"key":"10.1016\/j.jmb.2016.02.032_bb0035","doi-asserted-by":"crossref","first-page":"3139","DOI":"10.1002\/ajmg.a.37294","article-title":"Phosphoglucomutase-1 deficiency: intrafamilial clinical variability and common secondary adrenal insufficiency","volume":"167","author":"Loewenthal","year":"2015","journal-title":"Am. J. Med. Genet. Part A."},{"key":"10.1016\/j.jmb.2016.02.032_bb0040","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."},{"key":"10.1016\/j.jmb.2016.02.032_bb0045","doi-asserted-by":"crossref","first-page":"2130","DOI":"10.1110\/ps.04801104","article-title":"Evolutionary trace analysis of the alpha-d-phosphohexomutase superfamily","volume":"13","author":"Shackelford","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2016.02.032_bb0050","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":"10.1016\/j.jmb.2016.02.032_bb0055","doi-asserted-by":"crossref","first-page":"32010","DOI":"10.1074\/jbc.M114.597914","article-title":"Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency","volume":"289","author":"Lee","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.02.032_bb0060","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. Sect. D"},{"key":"10.1016\/j.jmb.2016.02.032_bb0065","doi-asserted-by":"crossref","first-page":"6322","DOI":"10.1016\/S0021-9258(18)42699-3","article-title":"The crystal structure of muscle phosphoglucomutase refined at 2.7\u00c5 resolution","volume":"267","author":"Dai","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.02.032_bb0070","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1093\/nar\/gkl282","article-title":"CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues","volume":"34","author":"Dundas","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2016.02.032_bb0075","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s10545-014-9757-9","article-title":"Mutations in hereditary phosphoglucomutase 1 deficiency map to key regions of enzyme structure and function","volume":"38","author":"Beamer","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.jmb.2016.02.032_bb0080","doi-asserted-by":"crossref","first-page":"2622","DOI":"10.1111\/febs.12249","article-title":"Identification of an essential active-site residue in the alpha-d-phosphohexomutase enzyme superfamily","volume":"280","author":"Lee","year":"2013","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2016.02.032_bb0085","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1002\/prot.22957","article-title":"Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens","volume":"79","author":"Mehra-Chaudhary","year":"2011","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2016.02.032_bb0090","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.str.2003.11.015","article-title":"Structural basis of diverse substrate recognition by the enzyme PMM\/PGM from P. aeruginosa","volume":"12","author":"Regni","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2016.02.032_bb0095","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1007\/s11095-007-9516-9","article-title":"Extrinsic fluorescent dyes as tools for protein characterization","volume":"25","author":"Hawe","year":"2008","journal-title":"Pharm. Res."},{"key":"10.1016\/j.jmb.2016.02.032_bb0100","doi-asserted-by":"crossref","first-page":"2778","DOI":"10.1021\/ci200227u","article-title":"LigPlot+: multiple ligand-protein interaction diagrams for drug discovery","volume":"51","author":"Laskowski","year":"2011","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.jmb.2016.02.032_bb0105","article-title":"The Human Gene Mutation Database (HGMD) and its exploitation in the study of mutational mechanisms.","author":"Cooper","year":"2006","journal-title":"Curr. Protoc. Bioinformatics"},{"key":"10.1016\/j.jmb.2016.02.032_bb0110","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.jmb.2005.08.020","article-title":"Loss of protein structure stability as a major causative factor in monogenic disease","volume":"353","author":"Yue","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0115","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.sbi.2009.08.003","article-title":"Stability effects of mutations and protein evolvability","volume":"19","author":"Tokuriki","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0120","doi-asserted-by":"crossref","first-page":"3919","DOI":"10.1016\/j.jmb.2013.07.014","article-title":"Molecular mechanisms of disease-causing missense mutations","volume":"425","author":"Stefl","year":"2013","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0125","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1002\/humu.22770","article-title":"On human disease-causing amino acid variants: statistical study of sequence and structural patterns","volume":"36","author":"Petukh","year":"2015","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.jmb.2016.02.032_bb0130","doi-asserted-by":"crossref","first-page":"4047","DOI":"10.1016\/j.jmb.2013.08.008","article-title":"Towards precision medicine: advances in computational approaches for the analysis of human variants","volume":"425","author":"Peterson","year":"2013","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0135","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nrm2144","article-title":"The folding and evolution of multidomain proteins","volume":"8","author":"Han","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0140","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1002\/pro.402","article-title":"Breaking the covalent connection: chain connectivity and the catalytic reaction of PMM\/PGM","volume":"19","author":"Schramm","year":"2010","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2016.02.032_bb0145","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/s12104-013-9511-5","article-title":"Chemical shift assignments of domain 4 from the phosphohexomutase from pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface","volume":"8","author":"Wei","year":"2014","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.jmb.2016.02.032_bb0150","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.jmb.2005.02.007","article-title":"Multi-domain proteins in the three kingdoms of life: orphan domains and other unassigned regions","volume":"348","author":"Ekman","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0155","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1086\/521879","article-title":"Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases","volume":"81","author":"Pey","year":"2007","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jmb.2016.02.032_bb0160","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1074\/jbc.M111.293795","article-title":"Crystal structure of human \u03b2-galactosidase: structural basis of G M1 gangliosidosis and morquio B diseases","volume":"287","author":"Ohto","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.02.032_bb0165","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.bbrc.2008.12.142","article-title":"Clustering of disease-causing mutations on the domain\u2013domain interfaces of ABCC6","volume":"379","author":"Fulop","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2016.02.032_bb0170","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0124277","article-title":"The structure of the T190M mutant of murine \u03b1-dystroglycan at high resolution: insight into the molecular basis of a primary dystroglycanopathy","volume":"10","author":"Bozzi","year":"2015","journal-title":"PLoS ONE"},{"key":"10.1016\/j.jmb.2016.02.032_bb0175","doi-asserted-by":"crossref","first-page":"4880","DOI":"10.1158\/0008-5472.CAN-09-4563","article-title":"Comprehensive analysis of missense variations in the BRCT domain of BRCA1 by structural and functional assays","volume":"70","author":"Lee","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.jmb.2016.02.032_bb0180","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1432-1327.1998.2570001.x","article-title":"Partial characterization and three-dimensional\u2013structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria","volume":"257","author":"Bj\u00f8rgo","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2016.02.032_bb0185","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":"10.1016\/j.jmb.2016.02.032_bb0190","doi-asserted-by":"crossref","first-page":"2551","DOI":"10.1021\/acs.biochem.5b00189","article-title":"Personalized biochemistry and biophysics","volume":"54","author":"Kroncke","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2016.02.032_bb0195","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/471836","article-title":"Advances in human biology: combining genetics and molecular biophysics to pave the way for personalized diagnostics and medicine","volume":"2014","author":"Alexov","year":"2014","journal-title":"Adv. Biol."},{"key":"10.1016\/j.jmb.2016.02.032_bb0200","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Software XDS for image rotation, recognition and crystal symmetry assignment","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0205","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0210","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444903008126","article-title":"A graphical user interface to the CCP 4 program suite","volume":"59","author":"Potterton","year":"2003","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0215","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1126\/science.1218231","article-title":"Linking crystallographic model and data quality","volume":"336","author":"Karplus","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.jmb.2016.02.032_bb0220","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1107\/S0021889800018227","article-title":"Global indicators of X-ray data quality","volume":"34","author":"Weiss","year":"2001","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0225","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0230","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: A comprehensive python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0235","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0240","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0245","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.02.032_bb0250","series-title":"The PyMOL Molecular Graphics System, Schr\u00f6dinger LLC Wwwpymolorg. Version 1","author":"DeLano","year":"2002"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283616001625?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283616001625?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:14:10Z","timestamp":1762668850000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283616001625"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4]]},"references-count":50,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2016,4]]}},"alternative-id":["S0022283616001625"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2016.02.032","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2016,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2016.02.032","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2016 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}