Catalytic activity and structural analysis of polymer-protected gold-palladium bimetallic clusters prepared by the simultaneous reduction of hydrogen tetrachloroaurate and palladium dichloride

1992 ◽  
Vol 96 (24) ◽  
pp. 9927-9933 ◽  
Author(s):  
Naoki Toshima ◽  
Masafumi Harada ◽  
Yoshinao Yamazaki ◽  
Kiyotaka Asakura
Keyword(s):  
Catalytic Activity ◽  
Structural Analysis ◽  
Bimetallic Clusters ◽  
Simultaneous Reduction ◽  
Hydrogen Tetrachloroaurate

DNA-templated silver and silver-based bimetallic clusters with remarkable and sequence-related catalytic activity toward 4-nitrophenol reduction

2019 ◽  
Vol 55 (3) ◽  
pp. 373-376 ◽  
Author(s):  
Weijun Zhou ◽  
Youxing Fang ◽  
Jiangtao Ren ◽  
Shaojun Dong
Keyword(s):  
Catalytic Activity ◽  
Bimetallic Clusters ◽  
Schematic Representation ◽  
Bimetallic Nanoclusters ◽  
Nitrophenol Reduction

Illustrative pathways for the preparation of bimetallic nanoclusters using DNA-AgNC, and a schematic representation of the reduction of 4-NP to 4-AP in the presence of DNA-AgNC or bimetallic nanoclusters.

Structural analysis of polymer-protected palladium/rhodium bimetallic clusters using EXAFS spectroscopy

1993 ◽  
Vol 97 (41) ◽  
pp. 10742-10749 ◽  
Author(s):  
Masafumi Harada ◽  
Kiyotaka Asakura ◽  
Yasumitsu Ueki ◽  
Naoki Toshima
Keyword(s):  
Structural Analysis ◽  
Exafs Spectroscopy ◽  
Bimetallic Clusters

Structural characterization of Pt–Ir bimetallic clusters on TiO2 nanotubes prepared by simultaneous reduction

2014 ◽  
Vol 258 ◽  
pp. 78-84 ◽  
Author(s):  
C. Angeles-Chavez ◽  
J.A. Toledo-Antonio ◽  
M.A. Cortes-Jacome ◽  
C. Encarnacion-Gomez
Keyword(s):  
Structural Characterization ◽  
Tio2 Nanotubes ◽  
Bimetallic Clusters ◽  
Simultaneous Reduction

scholarly journals Cancer-driving H3G34V/R/D mutations block H3K36 methylation and H3K36me3–MutSα interaction

2018 ◽  
Vol 115 (38) ◽  
pp. 9598-9603 ◽  
Author(s):  
Jun Fang ◽  
Yaping Huang ◽  
Guogen Mao ◽  
Shuang Yang ◽  
Gadi Rennert ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Structural Analysis ◽  
Mismatch Repair ◽  
Somatic Mutations ◽  
Genome Instability ◽  
Histone H3 ◽  
Side Chain ◽  
H3k36 Methylation ◽  
Histone Methyltransferases ◽  
Pediatric Cancers

Somatic mutations on glycine 34 of histone H3 (H3G34) cause pediatric cancers, but the underlying oncogenic mechanism remains unknown. We demonstrate that substituting H3G34 with arginine, valine, or aspartate (H3G34R/V/D), which converts the non-side chain glycine to a large side chain-containing residue, blocks H3 lysine 36 (H3K36) dimethylation and trimethylation by histone methyltransferases, including SETD2, an H3K36-specific trimethyltransferase. Our structural analysis reveals that the H3 “G33-G34” motif is recognized by a narrow substrate channel, and that H3G34/R/V/D mutations impair the catalytic activity of SETD2 due to steric clashes that impede optimal SETD2–H3K36 interaction. H3G34R/V/D mutations also block H3K36me3 from interacting with mismatch repair (MMR) protein MutSα, preventing the recruitment of the MMR machinery to chromatin. Cells harboring H3G34R/V/D mutations display a mutator phenotype similar to that observed in MMR-defective cells. Therefore, H3G34R/V/D mutations promote genome instability and tumorigenesis by inhibiting MMR activity.

Sign in / Sign up

Export Citation Format

Share Document