23 research outputs found
Correction: Mutational analysis of <i>ITPR1</i> in a Taiwanese cohort with cerebellar ataxias
Correction: Mutational analysis of <i>ITPR1</i> in a Taiwanese cohort with cerebellar ataxia
Bioinformatics analyses of <i>ITPR1</i> missense variants.
<p>Bioinformatics analyses of <i>ITPR1</i> missense variants.</p
The molecular and clinical characteristics of <i>ITPR1</i>-associated autosomal dominant cerebellar ataxias in the literature.
<p>The molecular and clinical characteristics of <i>ITPR1</i>-associated autosomal dominant cerebellar ataxias in the literature.</p
The clinical characteristics of the cases reported in this paper.
<p>The clinical characteristics of the cases reported in this paper.</p
The structure of human IP3R1.
<p>(A) The number 1 ~ 19 represent the amino acid residue substitutions reported as far associating with cerebellar ataxia. The blue rectangle represents the IP3 binding region, the red curve line denotes the coupling/regulatory region, and the yellow cylinders stand for the transmembrane segments. (B) The amino acid sequence of the sixth transmembrane segment of human IP3R1 was annotated by the UniProt. The <i>ITPR1</i> p.V2574A mutation resides in an evolutionarily conserved region, as shown by aligning the amino acid sequences of IP3R1 protein orthologs from various species.</p> <p>Abbreviation: ER: endoplasmic reticulum</p> <p><sup>#</sup>Remarks: All the nucleotide positions and amino acid residues represented here were converted to the reference sequence of NM_001168272 for CDS and NP_001161744 for protein sequence.</p
The pedigree and electropherogram of the patients carrying <i>ITPR1</i> c.7721T>C mutation.
<p>(A) The pedigree of the individuals carrying <i>ITPR1</i> p.V2574A (c.7721T>C) mutation in this study. The proband (II-3) is denoted by an arrow. Filled symbols represent symptomatic members, open symbols indicate unaffected individuals, circles stand for females, squares stand for males, WT/WT indicates wild type, and WT/MT stands for individuals harboring the heterozygous mutation. (B) The electropherograms of the patients (II-3 and III-1) carrying the <i>ITPR1</i> mutation (WT/MT) and a healthy family member (II-1) carrying two alleles of wild type <i>ITPR1</i>. The stars denote the location of the mutation.</p
Brain MRI of the patients carrying <i>ITPR1</i> mutation.
<p>The neuroimages of II-3 are shown as A1-E1, and her daughter’s images (III-1) are A2-E2. The T1-weighted sagittal view images denote a mild atrophy of the anterior and posterior lobes of the cerebellar vermis (A1 and A2). The T1-weighted axial view images demonstrate a mild atrophy of the cerebellar hemispheres (B1-C1 and B2-C2). The sizes of the pons and cerebellar peduncles are within normal ranges. The fluid-attenuated inversion recovery (FLAIR) axial view image features normal cerebral cortex, basal ganglia and midbrain (D1-E1 and D2-E2).</p
Clinical and molecular features of mutations in the <i>GARS</i> gene.
<p><sup>a</sup> C: Catalytic domain; DI: dimer interface; W: WHEP domain; Ins I: Insertion I domain; Ins II: Insertion II domain; Ins III: Insertion III domain; ACBD: anti-codon binding domain</p><p><sup>b</sup> * average age of disease onset</p><p><sup>c</sup> CMT: Charcot-Marie-Tooth disease; SMA: spinal muscular atrophy; dSMA: distal SMA;</p><p><sup>d</sup> AD: autosomal dominant; NA: not available</p><p>Clinical and molecular features of mutations in the <i>GARS</i> gene.</p
The crystal structure of human glycyl-tRNA synthetase (GlyRS) (PDB ID: 2PME).
<p>(A) Mapping of the two <i>GARS</i> mutation sites (p.Asp146Tyr and p.Met238Arg) on one subunit of the human GlyRS dimer. (B) A view of the human GlyRS dimers demonstrating that Met238 is located on the interface between the two subunits. Catalytic, Insertion I and Insertion II domains are colored as indicated.</p
Two novel <i>de novo GARS</i> mutations.
<p>(A) The novel <i>GARS</i> mutations identified in this study, p.Asp146Tyr and p.Met238Arg, with the sense strand electropherogram shown on the top and a limited reading frame depicting the corresponding amino acid substitutions shown below. (B) Pedigrees of the 2 patients harboring the novel <i>GARS</i> mutations. The arrows indicate the probands. “M” represents the <i>GARS</i> mutations and “W” means wild type. (C) The <i>GARS</i> p.Asp146Tyr and p.Met238Arg mutations reside in an evolutionarily conserved region, as shown by aligning the amino acid sequences of glycyl-tRNA synthetase protein (GlyRS) orthologs from various species.</p