14 research outputs found
Additional file 1: of A case of Raine syndrome presenting with facial dysmorphy and review of literature
Molecular investigations. The file describes the method used in isolation of genomic DNA, NGS and bioinformatics tools used during analysis. (DOCX 16 kb
Additional file 3: of A case of Raine syndrome presenting with facial dysmorphy and review of literature
Homology modeling, structure validation and protein stability due to c.1228T>A (p.Ser410Thr) variant. File describes the influence of variant change on the protein structure (DOCX 16 kb
Additional file 4: of A case of Raine syndrome presenting with facial dysmorphy and review of literature
Conservation of the FAM20C p.Ser410Thr residue in orthologs. Conservation of the variant in orthologs and Homo sapiens. (DOCX 15 kb
Additional file 2: of A case of Raine syndrome presenting with facial dysmorphy and review of literature
Sanger sequencing (Variant Confirmation Test). It describes the details of primer’s used during Sanger sequencing of the proband and parents (DOCX 15 kb
Additional file 5: of A case of Raine syndrome presenting with facial dysmorphy and review of literature
Population screening for c.1228T>A (p.Ser410Thr) variant by ARMS-PCR. The file provides details of normal healthy individuals studied for variant (c.1228T>A (p.Ser410Thr)) by ARMS-PCR. (DOCX 15 kb
Additional file 1: of Molecular characterization and evaluation of complex rearrangements in a case of ring chromosome 15
Microcephaly panel (a total of 69 genes) was analyzed. The list of genes is mentioned. (DOCX 11 kb
Multiple protein sequence alignment using ClustalW shows evolutionary conservation of amino acid residues.
<p>Fig. 3a: αE114 and αR170; Fig. 3b: αD322 and αR393; Fig. 3c: αE462 and αG478.</p
Clinical, biochemical and molecular details of the Indian patients with Tay Sachs disease.
*<p>DNA of index case is not available, HLC-heat labile activity in carrier parents, ND – not done.</p><p>Normal total hexosaminidase values using MUG substrate in our controls –703 to 1785 nmol/hr/mg protein, normal hexosaminidase A levels – (62 to 77%); normal MUGS activity 80 to 390 nmol/hr/mg.</p
Stereoscopic view of the docking experiments.
<p>Green sticks indicate C<sup>α</sup> trace of amino acids involved in the active site and CPK (Corey-Pauling-Koltun) coloring scheme represents ligand GalNAc (N acetyl galactosamine) portion of GM2 ganglioside. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0039122#pone-0039122-g004" target="_blank">Fig 4a:</a> Wild type (αHex-A-GalNAc complex). <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0039122#pone-0039122-g004" target="_blank">Fig 4b:</a> Mutant (αD322N-GalNAc), Red shows mutation p.D322N, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0039122#pone-0039122-g004" target="_blank">Fig 4c:</a> Mutant (αD322Y-GalNAc), Cyan shows mutation p.D322Y, Fig. 4d: Mutant (α E462V-GalNAc), yellow shows mutation p.E462Y.</p
Hydrogen bond interaction for the wild type and Mutant complexes.
<p>Hydrogen bond interaction for the wild type and Mutant complexes.</p