Novel mutation in the ?-sterol reductase gene in three Lebanese sibs with Smith-Lemli-Opitz (RSH) syndrome

2002 ◽  
Vol 110 (2) ◽  
pp. 103-108 ◽  
Author(s):  
Marjan M. Nezarati ◽  
Judith Loeffler ◽  
Grace Yoon ◽  
Linda MacLaren ◽  
Ernest Fung ◽  
...  
Keyword(s):  
Novel Mutation ◽  
Reductase Gene

Novel mutation in the ?7-dehydrocholesterol reductase gene in an Australian patient with Smith-Lemli-Opitz syndrome

2001 ◽  
Vol 103 (4) ◽  
pp. 344-347 ◽  
Author(s):  
Timothy Evans ◽  
Alisa Poh ◽  
Charlotte Webb ◽  
Brandon Wainwright ◽  
Carol Wicking ◽  
...  
Keyword(s):  
Novel Mutation ◽  
Reductase Gene ◽  
Opitz Syndrome

A novel mutation of the human 7-dehydrocholesterol reductase gene reduces enzyme activity in patients with holoprosencephaly

2004 ◽  
Vol 315 (1) ◽  
pp. 219-223 ◽  
Author(s):  
Yhong-Hee Shim ◽  
Soo-Han Bae ◽  
Jai-Hyun Kim ◽  
Kyu-Rae Kim ◽  
Chong Jai Kim ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Novel Mutation ◽  
Reductase Gene

Clinical and genetic studies in a family with a novel mutation in the sepiapterin reductase gene

2014 ◽  
Vol 129 ◽  
pp. 7-12 ◽  
Author(s):  
J. Koht ◽  
A. Rengmark ◽  
T. Opladen ◽  
K. A. Bjørnarå ◽  
T. Selberg ◽  
...  
Keyword(s):  
Novel Mutation ◽  
Genetic Studies ◽  
Sepiapterin Reductase ◽  
Reductase Gene

Characterization of a Novel Mutation in the NADH-Cytochrome b5 Reductase Gene Responsible for Rare Hereditary Methaemoglobinaemia Type I

2013 ◽  
Vol 130 (2) ◽  
pp. 122-125 ◽  
Author(s):  
Katarzyna Rawa ◽  
Liliana Chelmecka-Hanusiewicz ◽  
Danuta Plochocka ◽  
Katarzyna Pawinska-Wasikowska ◽  
Walentyna Balwierz ◽  
...  
Keyword(s):  
Novel Mutation ◽  
Cytochrome B5 ◽  
Type I ◽  
Cytochrome B5 Reductase ◽  
Reductase Gene ◽  
Nadh Cytochrome

scholarly journals Genetic study in a family with dopa-responsive dystonia revealed a novel mutation in sepiapterin reductase gene

2019 ◽  
Vol 35 (6) ◽  
Author(s):  
Tawfiq Froukh
Keyword(s):  
Genetic Study ◽  
Clinical Symptoms ◽  
Novel Mutation ◽  
Gene Encoding ◽  
Early Management ◽  
Reductase Deficiency ◽  
Creative Commons ◽  
Sepiapterin Reductase ◽  
Recessive Mutations ◽  
Reductase Gene

Dopa-responsive dystonia due to sepiapterin reductase deficiency (OMIM#612716) is caused by recessive mutations in the gene encoding sepiapterin reductase (SPR), which plays an important role in the biosynthesis of tetrahydrobiopterin (BH4). One Jordanian patient to first cousin parents is reported in this study. The parents of the proband have recognized the symptoms of their daughter at six months old with motor developmental delay. The symptoms were progressed after-then to include speech delay, seizure, ataxia, oculomotor apraxia, dysarthia and choreoathetosis. Despite of these symptoms, the clinicians in Jordan were unable to diagnose the case. In August 2018, the proband (8 years old) was presented to the department of biotechnology and genetic engineering at Philadelphia University in Jordan for the purposes of performing whole exome sequencing (WES). Analysis of WES data has revealed novel homozygous frameshift variant in the gene SPR (NM_003124.4:c.40delG,p.Ala15Profs*100). The variant is heterozygous in the parents and in the healthy male siblings. Therefore, the studied case was diagnosed with sepiapterin reductase deficiency. Because this disease is likely to be treated recommendations were given to the family immediately to start treatments trials. The case in this study illustrates the difficulties of diagnosing sepiapterin reductase deficiency based on clinical symptoms only and thus renders the possibilities of early management. Also, this study reinforces the importance of running WES to undiagnosed neurodevelopmental cases. doi: https://doi.org/10.12669/pjms.35.6.1181 How to cite this:Froukh T. Genetic study in a family with dopa-responsive dystonia revealed a novel mutation in sepiapterin reductase gene. Pak J Med Sci. 2019;35(6):1736-1739. doi: https://doi.org/10.12669/pjms.35.6.1181 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Congenital mirror movements in a family with a novel mutation in the DCC gene

2011 ◽  
Vol 42 (S 01) ◽  
Author(s):  
GC Korenke ◽  
M Wagner ◽  
A Maak ◽  
G Rosenberger ◽  
K Kutsche
Keyword(s):  
Novel Mutation ◽  
Mirror Movements ◽  
Dcc Gene

Danon Disease: Clinical Presentation and Diagnostic Workup in a Case of a Male Patient with a Novel Mutation in the LAMP2 Gene

2016 ◽  
Vol 47 (S 01) ◽  
Author(s):  
A. Dieckmann ◽  
F. Majer ◽  
H. Hulkova ◽  
M. Farr ◽  
T. Kalina ◽  
...  
Keyword(s):  
Male Patient ◽  
Clinical Presentation ◽  
Novel Mutation ◽  
Diagnostic Workup ◽  
Danon Disease ◽  
Lamp2 Gene

A Novel Mutation Glyl672→Arg in Type 2A and a Homozygous Mutation in Type 2B von Willebrand Disease

1996 ◽  
Vol 76 (02) ◽  
pp. 253-257 ◽  
Author(s):  
Takeshi Hagiwara ◽  
Hiroshi Inaba ◽  
Shinichi Yoshida ◽  
Keiko Nagaizumi ◽  
Morio Arai ◽  
...  
Keyword(s):  
Missense Mutation ◽  
Novel Mutation ◽  
Point Mutations ◽  
Japanese Patients ◽  
Von Willebrand Disease ◽  
Homozygous Mutation ◽  
Missense Mutations ◽  
Reaction Products ◽  
Type 3 ◽  
Von Willebrand

SummaryGenetic materials from 16 unrelated Japanese patients with von Willebrand disease (vWD) were analyzed for mutations. Exon 28 of the von Willebrand factor (vWF) gene, where point mutations have been found most frequent, was screened by various restriction-enzyme analyses. Six patients were observed to have abnormal restriction patterns. By sequence analyses of the polymerase chain-reaction products, we identified a homozygous R1308C missense mutation in a patient with type 2B vWD; R1597W, R1597Q, G1609R and G1672R missense mutations in five patients with type 2A; and a G1659ter nonsense mutation in a patient with type 3 vWD. The G1672R was a novel missense mutation of the carboxyl-terminal end of the A2 domain. In addition, we detected an A/C polymorphism at nucleotide 4915 with HaeIII. There was no particular linkage disequilibrium of the A/C polymorphism, either with the G/A polymorphism at nucleotide 4391 detected with Hphl or with the C/T at 4891 detected with BstEll.

Characterization of the Original Christmas Disease Mutation (Cysteine 206 → Serine): From Clinical Recognition to Molecular Pathogenesis

1992 ◽  
Vol 67 (01) ◽  
pp. 063-065 ◽  
Author(s):  
Sherryl A M Taylor ◽  
Jacalyn Duffin ◽  
Cherie Cameron ◽  
Jerome Teitel ◽  
Bernadette Garvey ◽  
...  
Keyword(s):  
Nucleotide Substitution ◽  
Novel Mutation ◽  
Factor Ix ◽  
Causative Mutation ◽  
Coding Region ◽  
Body Of Knowledge ◽  
Polymerase Chain ◽  
Splice Junctions

SummaryChristmas disease was first reported as a distinct clinical entity in two manuscripts published in 1952 (1, 2). The eponym associated with this disorder, is the surname of the first patient examined in detail and reported by Biggs and colleagues in a paper describing the clinical and laboratory features of seven affected individuals (3). This patient has severe factor IX coagulant deficiency (less than 0.01 units/ml) and no detectable circulating factor IX antigen (less than 0.01 units/ml). Coding sequence and splice junctions of the factor IX gene from this patient have been amplified in vitro through the polymerase chain reaction (PCR). One nucleotide substitution was identified at nucleotide 30,070 where a guanine was replaced by a cytosine. This mutation alters the amino acid encoded at position 206 in the factor IX protein from cysteine to serine. The non conservative nature of this substitution, the absence of this change in more than 200 previously sequenced factor IX genes and the fact that the remainder of the coding region of this gene was normal, all provide strong circumstantial evidence in favour of this change being the causative mutation in this patient. The molecular characterization of this novel mutation in the index case of Christmas disease, contributes to the rapidly expanding body of knowledge pertaining to Christmas disease pathogenesis.

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