Nitrogen-Doped Mesoporous Graphene as a Synergistic Electrocatalyst Matrix for High-Performance Oxygen Reduction Reaction

To balance the anchoring sites and conductivity of the catalyst supports is a dilemma in electrocatalytic oxygen reduction reaction (ORR). Nitrogen-doped mesoporous graphene (N-MG) with large surface area, high porosity, and superior intrinsic conductivity has been developed to address this issue. Using N-MG as the backbone, a hybrid catalyst of Co₃O₄ nanocrystals embedded on N-MG (Co₃O₄/N-MG) was prepared for the electrocatalytic ORR in alkaline media. The Co₃O₄/N-MG showed high catalytic activity for the four-electron ORR, giving a more positive onset potential (0.93 V vs RHE) and a higher current density. The unique property of N-MG and the synergetic effect of Co₃O₄ and N-MG are prominent for ORR. With improved electrocatalytic activity and durability, the Co₃O₄/N-MG can be an efficient nonprecious metal catalyst and potentially used to substitute the platinum-based cathode catalysts in fuel cells and metal–air batteries

Identification of a Novel Missense <i>FBN2</i> Mutation in a Chinese Family with Congenital Contractural Arachnodactyly Using Exome Sequencing - Fig 2

<p><b>(A) The phenotype and (B) X-ray images of hands from an affected member (IV:2) of the family</b>.</p

Clinical and genetic data of 7 patients with <i>FBN2</i> c.3769T>C (p.C1257R) mutation.

<p>Clinical and genetic data of 7 patients with <i>FBN2</i> c.3769T>C (p.C1257R) mutation.</p

Sequencing analysis of p.C1257R mutation in the <i>FBN2</i> gene (DNA).

<p>(A) Unaffected member (II:7) of the family. (B) Heterozygous p.C1257R mutation patient (III:4).</p

Genomic organization of the human CHIP gene and the domain structure of the CHIP protein.

<p>The CHIP gene consists of seven exons. The CHIP protein has two key domains: the TPR domains and the one U-box domain. The five mutations identified in CHIP are indicated with arrows. Three mutations [c.493 CγT (p.L165F); c.389A>T (p.N130I); c.441G>T (p.W147C); c.707G>C (p.S236T)] are were located between the third TPR domain and the second low complexity segment. The c.621C>G (p.Y207X) mutation encodes a truncated protein without a U-box domain and the S236T mutation is located in the U-box domain.</p

Expression of CHIP in the mouse brain and the effect of ARCA-associcated mutations on its ability to promote the degradation of NR2A.

<p>(<b>A</b>) The expression of CHIP in the cerebellum (Cb), hippocampus (Hip), cerebral cortex (Ctx), pons (PN) and medulla oblongata (MO) of mouse brain as analyzed with immunohistochemistry. (<b>B</b>) Co-localization of CHIP (red) and calcium-binding protein calbindin D-28K (green) in Purkinje cells. (<b>C</b>) Co-localization of CHIP (red) and NR2A (green) in Cb, PN and MO. (<b>D</b>) Coexpression of flag-tagged WT, but not ARCA-associated CHIP mutants (CHIP^N130I, CHIP^W147C, CHIP^L165F, CHIP^Y207X, CHIP^S236T), with HA-Fbx2 promoted the degradation of NR2A. Expression vectors for CHIP, Fbx2 and NR2A were transfected into Human Embryonic Kidney 293 cells. At 36 h after transfection, cells were treated with cycloheximide (CHX, 100 μg/ml) and chased for different time periods. NR2A was detected with western blot using the Myc antibody. Quantitative analysis was performed using NIH ImageJ analysis software. Values represent the mean ± S.D. of three independent experiments.</p

The pedigrees, brain MRIs, and CHIP mutations identified.

<p>(<b>A</b>) The pedigree of family 1 with autosomal-recessive spinocerebellar ataxia. (<b>B</b>) The brain MRI of II-5 in family 1. Panel (left): axial T1-weighted image showing atrophy of the cerebellar vermis. Panel (right): midline sagittal T1-weighted image showing cerebellar atrophy, particularly evident in the superior vermis, with enlargement of the fourth ventricle. (<b>C</b>) Sanger sequencing results of codons 164–166 in exon 1 of the CHIP gene in a WT subject (left), an individual carrying the heterozygous variant (middle), and an individual carrying the homozygous c.493C>T (p.L165F) mutation (right). (<b>D</b>) The L165F missense mutation occurred at an evolutionarily conserved amino acid (in red) in the CHIP. (<b>E</b> and <b>F</b>) The pedigrees of families 2 and 3. Sanger sequencing results of the members of these two families. The red arrows indicate the mutation sites. </p