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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1996 1
1997 2
1998 6
1999 2
2000 2
2001 6
2002 2
2003 3
2005 5
2006 2
2007 3
2008 3
2009 1
2010 1
2012 4
2013 2
2014 3
2016 2
2017 1
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2021 1
2024 0

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Page 1
Syndromic craniosynostosis: from history to hydrogen bonds.
Cunningham ML, Seto ML, Ratisoontorn C, Heike CL, Hing AV. Cunningham ML, et al. Orthod Craniofac Res. 2007 May;10(2):67-81. doi: 10.1111/j.1601-6343.2007.00389.x. Orthod Craniofac Res. 2007. PMID: 17552943 Review.
The mutations in Pfeiffer (FGFR1), Muenke (FGFR3), and Apert syndrome (FGFR2) are caused by the same amino acid substitution in a highly conserved region of the Ig II-III linker region of these proteins, which suggests that these receptor tyrosine kinases hav …
The mutations in Pfeiffer (FGFR1), Muenke (FGFR3), and Apert syndrome (FGFR2) are caused by the same amino acid substitutio …
Craniosynostosis and related limb anomalies.
Wilkie AO, Oldridge M, Tang Z, Maxson RE Jr. Wilkie AO, et al. Novartis Found Symp. 2001;232:122-33; discussion 133-43. doi: 10.1002/0470846658.ch9. Novartis Found Symp. 2001. PMID: 11277076 Review.
Mouse models of Apert syndrome.
Holmes G. Holmes G. Childs Nerv Syst. 2012 Sep;28(9):1505-10. doi: 10.1007/s00381-012-1872-z. Epub 2012 Aug 8. Childs Nerv Syst. 2012. PMID: 22872267
It is caused by gain-of-function mutations in FGFR2, over 98% of which are the two amino acid substitution mutations S252W and P253R. FGFR2 is widely expressed throughout development, so that many tissues are adversely affected in Apert syndrome, particularly …
It is caused by gain-of-function mutations in FGFR2, over 98% of which are the two amino acid substitution mutations S2 …
Gain-of-function amino acid substitutions drive positive selection of FGFR2 mutations in human spermatogonia.
Goriely A, McVean GA, van Pelt AM, O'Rourke AW, Wall SA, de Rooij DG, Wilkie AO. Goriely A, et al. Proc Natl Acad Sci U S A. 2005 Apr 26;102(17):6051-6. doi: 10.1073/pnas.0500267102. Epub 2005 Apr 19. Proc Natl Acad Sci U S A. 2005. PMID: 15840724 Free PMC article.
C>G transversions at position 755 of FGF receptor 2 (FGFR2) cause Apert syndrome; this mutation, encoding the gain-of-function substitution Ser252Trp, occurs with a birth rate elevated 200- to 800-fold above background and originates exclusively from the unaffected fath …
C>G transversions at position 755 of FGF receptor 2 (FGFR2) cause Apert syndrome; this mutation, encoding the gain-of-function substit …
Biallelic mutations in CYP26B1: A differential diagnosis for Pfeiffer and Antley-Bixler syndromes.
Morton JE, Frentz S, Morgan T, Sutherland-Smith AJ, Robertson SP. Morton JE, et al. Am J Med Genet A. 2016 Oct;170(10):2706-10. doi: 10.1002/ajmg.a.37804. Epub 2016 Jul 13. Am J Med Genet A. 2016. PMID: 27410456 Review.
The disorder is caused by biallelic missense mutations in CYP26B1, which encodes for a cytochrome P450 enzyme responsible for the catabolism of retinoic acid in a temporally and spatially restricted fashion during embryonic development. ...
The disorder is caused by biallelic missense mutations in CYP26B1, which encodes for a cytochrome P450 enzyme responsible for the catabolism …
Clinical variability in patients with Apert's syndrome.
Lajeunie E, Cameron R, El Ghouzzi V, de Parseval N, Journeau P, Gonzales M, Delezoide AL, Bonaventure J, Le Merrer M, Renier D. Lajeunie E, et al. J Neurosurg. 1999 Mar;90(3):443-7. doi: 10.3171/jns.1999.90.3.0443. J Neurosurg. 1999. PMID: 10067911
The molecular basis for this syndrome appears remarkably specific: two adjacent amino acid substitutions (either S252W or P253R) occurring in the linking region between the second and third immunoglobulin domains of the fibroblast growth factor receptor (FGFR)2 gene …
The molecular basis for this syndrome appears remarkably specific: two adjacent amino acid substitutions (either S252W or P253 …
Monozygotic twins with Apert syndrome.
Breugem CC, Fitzpatrick DF, Verchere C. Breugem CC, et al. Cleft Palate Craniofac J. 2008 Jan;45(1):101-4. doi: 10.1597/06-149.1. Cleft Palate Craniofac J. 2008. PMID: 18215098
50 results