{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T08:08:33Z","timestamp":1791446913130,"version":"4.3.3"},"reference-count":27,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Physiological Genomics"],"published-print":{"date-parts":[[2000,1,24]]},"abstract":"<jats:p>Winterpacht, Andreas, Katja Hilbert, Christiane Stelzer, Thorsten Schweikardt, Heinz Decker, Hugo Segerer, J\u00fcrgen Spranger, and Bernhard Zabel. A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia. Physiol. Genomics 2: 9\u201312, 2000.\u2014Fibroblast growth factor receptor 3 (FGFR3) is a glycoprotein that belongs to the family of tyrosine kinase receptors. Specific mutations in the FGFR3 gene are associated with autosomal dominant human skeletal disorders such as hypochondroplasia, achondroplasia, and thanatophoric dysplasia. Hypochondroplasia (HCH), the mildest form of this group of short-limbed dwarfism disorders, results in \u223c60% of cases from a mutation in the intracellular FGFR3-tyrosine kinase domain. The remaining cases may either be caused by defects in other FGFR gene regions or other yet unidentified genes. We describe a novel HCH mutation, the first found outside the common mutation hot spot of this condition. This point mutation, an N328I exchange in the extracellular Ig domain III of the receptor, seems to be unique as it affects a putative N-glycosylation site that is conserved between different FGFRs and species. The amino acid exchange itself most probably has no impact on the three-dimensional structure of the receptor domain, suggesting that the phenotype is the result of altered receptor glycosylation and its pathophysiological consequences.<\/jats:p>","DOI":"10.1152\/physiolgenomics.2000.2.1.9","type":"journal-article","created":{"date-parts":[[2017,12,23]],"date-time":"2017-12-23T18:01:41Z","timestamp":1514052101000},"page":"9-12","source":"Crossref","is-referenced-by-count":60,"title":["A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia"],"prefix":"10.1152","volume":"2","author":[{"given":"ANDREAS","family":"WINTERPACHT","sequence":"first","affiliation":[{"name":"Children's Hospital, University of Mainz, D-55101 Mainz"},{"name":"Institute of Human Genetics, University of Hamburg, D-22529 Hamburg"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"KATJA","family":"HILBERT","sequence":"additional","affiliation":[{"name":"Children's Hospital, University of Mainz, D-55101 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"CHRISTIANE","family":"STELZER","sequence":"additional","affiliation":[{"name":"Children's Hospital, University of Mainz, D-55101 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"THORSTEN","family":"SCHWEIKARDT","sequence":"additional","affiliation":[{"name":"Institute for Molecular Biophysics, University of Mainz, D-55128 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"HEINZ","family":"DECKER","sequence":"additional","affiliation":[{"name":"Institute for Molecular Biophysics, University of Mainz, D-55128 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"HUGO","family":"SEGERER","sequence":"additional","affiliation":[{"name":"St. Hedwig Hospital, D-93006 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00dcRGEN","family":"SPRANGER","sequence":"additional","affiliation":[{"name":"Children's Hospital, University of Mainz, D-55101 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"BERNHARD","family":"ZABEL","sequence":"additional","affiliation":[{"name":"Children's Hospital, University of Mainz, D-55101 Mainz"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","reference":[{"key":"R1","doi-asserted-by":"publisher","DOI":"10.1038\/ng0795-357"},{"key":"R2","unstructured":"Bhatia, P. K., and A. Mukhopadhyay.\n                      Protein glycosylation: implications for in vivo functions and therapeutic applications.\n                      Adv. Biochem. Eng. Biotechnol.\n                      64\n                      : 155\u2013201, 1998."},{"key":"R3","doi-asserted-by":"publisher","DOI":"10.1021\/bi00033a002"},{"key":"R4","doi-asserted-by":"crossref","unstructured":"Grigeliognien\u00e9, G., L. Hagen\u00e4s, O. Ekl\u00f6f, L. Neumeyer, P. E. Haereid, and M. Anvret.\n                      A novel missense mutation Ile538Val in the fibroblast growth factor receptor 3 in hypochondroplasia.\n                      Human Mutation, Mutation in Brief, 122 Online,\n                      1997.","DOI":"10.1002\/(SICI)1098-1004(1998)11:4<333::AID-HUMU17>3.3.CO;2-A"},{"key":"R5","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.1312"},{"key":"R6","doi-asserted-by":"publisher","DOI":"10.1007\/s001120050312"},{"key":"R7","doi-asserted-by":"crossref","unstructured":"Johnson, D. E., and L. T. Williams.\n                      Structural and functional diversity in the FGF receptor multigene family.\n                      Adv. Cancer Res.\n                      60\n                      : 1\u201340, 1993.","DOI":"10.1016\/S0065-230X(08)60821-0"},{"key":"R8","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.10.6621"},{"key":"R9","doi-asserted-by":"crossref","unstructured":"Keegan, K., D. E. Johnson, L. T. Williams, and M. Hayman.\n                      Isolation of an additional member of the fibroblast growth factor receptor family, FGFR3.\n                      Proc. Natl. Acad. Sci. USA\n                      88: 1095\u20131099. 1991.","DOI":"10.1073\/pnas.88.4.1095"},{"key":"R10","unstructured":"Keegan, K., S. Meyer, and M. J. Hayman.\n                      Structural and biosynthetic characterization of fibroblast growth factor receptor 3 (FGFR-3) protein.\n                      Oncogene\n                      2\n                      : 2229\u20132236, 1991."},{"key":"R11","doi-asserted-by":"publisher","DOI":"10.1006\/geno.1996.0492"},{"key":"R12","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4652(199707)172:1<117::AID-JCP13>3.0.CO;2-9"},{"key":"R13","doi-asserted-by":"publisher","DOI":"10.1016\/S0079-6603(08)61031-4"},{"key":"R14","unstructured":"Murgue, B., S. Tsunekawa, I. Rosenberg, M. deBeaumont, and D. K. Podolsky.\n                      Identification of a novel variant form of fibroblast growth factor receptor 3 (FGFR3 IIIb) in human colonic epithelium.\n                      Cancer Res.\n                      54\n                      : 5206\u20135211, 1994."},{"key":"R15","doi-asserted-by":"publisher","DOI":"10.1038\/ng0696-233"},{"key":"R16","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(96)01134-9"},{"key":"R17","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80051-3"},{"key":"R18","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/4.11.2097"},{"key":"R19","doi-asserted-by":"crossref","unstructured":"Raffioni, S., Y.Z. Zhu, R. A. Bradshaw, and L. M. Thompson.\n                      Effect of transmembrane and kinase domain mutations on fibroblast growth factor receptor 3 chimera signaling in PC12 cells.\n                      J. Biol. Chem.\n                      52\n                      : 35250\u201335259, 1998.","DOI":"10.1074\/jbc.273.52.35250"},{"key":"R20","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1096-8628(19960726)67:4<387::AID-AJMG12>3.0.CO;2-F"},{"key":"R21","doi-asserted-by":"publisher","DOI":"10.1136\/jmg.33.9.749"},{"key":"R22","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1626"},{"key":"R23","doi-asserted-by":"crossref","unstructured":"Su, W.C. S., M. Kitagawa, N. Xue, B. Xie, S. Garofalo, J. Cho, C. Deng, et al.\n                      Activation of Stat1 by mutant fibroblast growth-factor receptor in thanatophoric dysplasia type II dwarfism.\n                      Nature\n                      386\n                      : 287\u2013292, 1997.","DOI":"10.1038\/386288a0"},{"key":"R24","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1996.tb00384.x"},{"key":"R25","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-9525(97)01131-1"},{"key":"R26","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(95)00102-3"},{"key":"R27","doi-asserted-by":"publisher","DOI":"10.1007\/s004390050493"}],"container-title":["Physiological Genomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.physiology.org\/doi\/pdf\/10.1152\/physiolgenomics.2000.2.1.9","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,8]],"date-time":"2019-09-08T18:09:40Z","timestamp":1567966180000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.physiology.org\/doi\/10.1152\/physiolgenomics.2000.2.1.9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,1,24]]},"references-count":27,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2000,1,24]]}},"alternative-id":["10.1152\/physiolgenomics.2000.2.1.9"],"URL":"https:\/\/doi.org\/10.1152\/physiolgenomics.2000.2.1.9","relation":{},"ISSN":["1094-8341","1531-2267"],"issn-type":[{"value":"1094-8341","type":"print"},{"value":"1531-2267","type":"electronic"}],"subject":[],"published":{"date-parts":[[2000,1,24]]}}}