{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T10:12:38Z","timestamp":1760955158370},"reference-count":13,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2009,7,17]],"date-time":"2009-07-17T00:00:00Z","timestamp":1247788800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Hum Genet"],"published-print":{"date-parts":[[2009,8]]},"DOI":"10.1038\/jhg.2009.66","type":"journal-article","created":{"date-parts":[[2009,7,17]],"date-time":"2009-07-17T09:22:59Z","timestamp":1247822579000},"page":"493-496","source":"Crossref","is-referenced-by-count":16,"title":["Silent exonic mutation in the acid-\u03b1-glycosidase gene that causes glycogen storage disease type II by affecting mRNA splicing"],"prefix":"10.1038","volume":"54","author":[{"given":"Mireguli","family":"Maimaiti","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satoru","family":"Takahashi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kazuki","family":"Okajima","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nao","family":"Suzuki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junko","family":"Ohinata","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akiko","family":"Araki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hajime","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tokuo","family":"Mukai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenji","family":"Fujieda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2009,7,17]]},"reference":[{"key":"BFjhg200966_CR1","first-page":"3389","volume-title":"The metabolic and molecular bases of inherited disease","author":"R Hirschhorm","year":"2001","unstructured":"Hirschhorm, R. & Reuser, A. J. J. Glycogen storage disease type II. Acid alpha-glucosidase (acid maltase) deficiency In: Scriver CR, Beaudet AL, Sly WS, Valle D (eds) The metabolic and molecular bases of inherited disease, MacGraw-Hill: New York, pp 3389\u20133420 (2001)."},{"key":"BFjhg200966_CR2","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1007\/BF02185782","volume":"97","author":"WL Kuo","year":"1996","unstructured":"Kuo, W. L., Hirschhorn, R., Huie, M. L. & Hirschhorn, K. Localization and ordering of acid alpha-glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. Hum. Genet. 97, 404\u2013406 (1996).","journal-title":"Hum. Genet."},{"key":"BFjhg200966_CR3","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1042\/bj2720493","volume":"272","author":"LH Hoefsloot","year":"1990","unstructured":"Hoefsloot, L. H., Hoogeveen-Westerveld, M., Reuser, A. J. & Oostra, B. A. Characterization of the human lysosomal alpha-glucosidase gene. Biochem. J. 272, 493\u2013497 (1990).","journal-title":"Biochem. J."},{"key":"BFjhg200966_CR4","doi-asserted-by":"publisher","first-page":"6780","DOI":"10.1074\/jbc.M404008200","volume":"280","author":"RJ Moreland","year":"2005","unstructured":"Moreland, R. J., Jin, X., Zhang, X. K., Decker, R. W., Albee, K. L. & Lee, K. L. Lysosomal acid alpha-glucosidase consists of four different peptides processed from a single chain precursor. J. Biol. Chem. 280, 6780\u20136791 (2005).","journal-title":"J. Biol. Chem."},{"key":"BFjhg200966_CR5","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1042\/bj2890681","volume":"289","author":"MM Hermans","year":"1993","unstructured":"Hermans, M. M., Wisselaar, H. A., Kroos, M. A., Oostra, B. A. & Reuser, A. J. Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites. Biochem. J. 289, 681\u2013686 (1993).","journal-title":"Biochem. J."},{"key":"BFjhg200966_CR6","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1016\/S0021-9258(18)53985-5","volume":"268","author":"HA Wisselaar","year":"1993","unstructured":"Wisselaar, H. A., Kroos, M. A., Hermans, M. M., van Beeumen, J. & Reuser, A. J. Structural and functional changes of lysosomal acid alpha-glucosidase during intracellular transport and maturation. J. Biol. Chem. 268, 2223\u20132231 (1993).","journal-title":"J. Biol. Chem."},{"key":"BFjhg200966_CR7","doi-asserted-by":"publisher","first-page":"E13","DOI":"10.1002\/humu.20745","volume":"29","author":"M Kroos","year":"2008","unstructured":"Kroos, M., Pomponio, R. J., van Vliet, L., Palmer, R. E., Phipps, M., Van der Helm, R. et al. Update of the Pompe disease mutation database with 107 sequence variants and a format for severity rating. Hum. Mutat. 29, E13\u2013E26 (2008).","journal-title":"Hum. Mutat."},{"key":"BFjhg200966_CR8","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1016\/S0960-8966(00)00142-5","volume":"10","author":"S Tsujino","year":"2000","unstructured":"Tsujino, S., Huie, M., Kanazawa, N., Sugie, H., Goto, Y., Kawai, M. et al. Frequent mutations in Japanese patients with acid maltase deficiency. Neuromuscul. Disord. 10, 599\u2013603 (2000).","journal-title":"Neuromuscul. Disord."},{"key":"BFjhg200966_CR9","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.nurt.2008.08.009","volume":"5","author":"B Schoser","year":"2008","unstructured":"Schoser, B., Hill, V. & Raben, N. Therapeutic approaches in glycogen storage disease type II\/Pompe disease. Neurotherapeutics 5, 569\u2013578 (2008).","journal-title":"Neurotherapeutics"},{"key":"BFjhg200966_CR10","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/j.ymgme.2007.05.011","volume":"92","author":"L Gort","year":"2007","unstructured":"Gort, L., Coll, M. J. & Chab\u00e1s, A. Glycogen storage disease type II in Spanish patients: high frequency of c.1076-1G&gt;C mutation. Mol. Genet. Metab. 92, 183\u2013187 (2007).","journal-title":"Mol. Genet. Metab."},{"key":"BFjhg200966_CR11","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1002\/humu.10286","volume":"23","author":"MM Hermans","year":"2004","unstructured":"Hermans, M. M., van Leenen, D., Kroos, M. A., Beesley, C. E., Van Der Ploeg, A. T., Sakuraba, H. et al. Twenty-two novel mutations in the lysosomal alpha-glucosidase gene (GAA) underscore the genotype-phenotype correlation in glycogen storage disease type II. Hum. Mutat. 23, 47\u201356 (2004).","journal-title":"Hum. Mutat."},{"key":"BFjhg200966_CR12","doi-asserted-by":"publisher","first-page":"2231","DOI":"10.1093\/hmg\/3.7.1081","volume":"3","author":"ML Huie","year":"1994","unstructured":"Huie, M. L., Chen, A. S., Tsujino, S., Shanske, S., DiMauro, S., Engel, A. G. et al. Aberrant splicing in adult onset glycogen storage disease type II (GSDII): molecular identification of an IVS1 (-13T \u2192 G) mutation in a majority of patients and a novel IVS10 (+1GT \u2192 CT) mutation. Hum. Mol. Genet. 3, 2231\u20132236 (1994).","journal-title":"Hum. Mol. Genet."},{"key":"BFjhg200966_CR13","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1212\/01.wnl.0000299892.81127.8e","volume":"70","author":"AC Nascimbeni","year":"2008","unstructured":"Nascimbeni, A. C., Fanin, M., Tasca, E. & Angelini, C. Molecular pathology and enzyme processing in various phenotypes of acid maltase deficiency. Neurology 70, 617\u2013626 (2008).","journal-title":"Neurology"}],"container-title":["Journal of Human Genetics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/jhg200966.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/jhg200966","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/jhg200966.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T17:26:10Z","timestamp":1684430770000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/jhg200966"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,7,17]]},"references-count":13,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2009,8]]}},"alternative-id":["BFjhg200966"],"URL":"https:\/\/doi.org\/10.1038\/jhg.2009.66","relation":{},"ISSN":["1434-5161","1435-232X"],"issn-type":[{"value":"1434-5161","type":"print"},{"value":"1435-232X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,7,17]]}}}