Breaking the scaling relationship via dual metal doping in a cobalt spinel for the OER: a computational prediction

2020 ◽  
Vol 22 (33) ◽  
pp. 18672-18680
Author(s):  
Yikun Kang ◽  
Feiran Zhang ◽  
Bowen Liu ◽  
Yuanqing Sun ◽  
Xiao Zhang ◽  
...  

The scaling relationship in the OER is found to be broken on a reconstructed Co3O4(110) surface via dual metal doping.

2012 ◽  
pp. 305-311
Author(s):  
Dileep Kumar C J ◽  
Yingjia Liu ◽  
Jason Ganley ◽  
William Tilson ◽  
Adam Dekich ◽  
...  

2013 ◽  
Vol 161 (1) ◽  
pp. F47-F53 ◽  
Author(s):  
C. J. Dileep Kumar ◽  
A. Dekich ◽  
H. Wang ◽  
Y. Liu ◽  
W. Tilson ◽  
...  

2020 ◽  
Vol 529 ◽  
pp. 147117
Author(s):  
Dongchen Han ◽  
Zhaoyan Luo ◽  
Yang Li ◽  
Nanxing Gao ◽  
Junjie Ge ◽  
...  

2020 ◽  
Vol 8 (31) ◽  
pp. 15809-15815 ◽  
Author(s):  
Gan Luo ◽  
Yu Jing ◽  
Yafei Li

Dual-metal-site catalysts could exhibit superior activity for CO2 electroreduction to CO due to the breaking of scaling relationship.


2020 ◽  
Vol 267 ◽  
pp. 118657 ◽  
Author(s):  
Mingxi Yang ◽  
Tanglue Feng ◽  
Yixin Chen ◽  
Junjun Liu ◽  
Xiaohuan Zhao ◽  
...  

1999 ◽  
Vol 09 (PR10) ◽  
pp. Pr10-129-Pr10-132 ◽  
Author(s):  
J. P. McCarten ◽  
T. C. Jones ◽  
X. Wu ◽  
J. H. Miller ◽  
I. Pirtle ◽  
...  

2019 ◽  
Author(s):  
Michael Olp ◽  
Daniel Sprague ◽  
Stefan Kathman ◽  
Ziyang Xu ◽  
Alexandar Statsyuk ◽  
...  

<p>Brd4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding sites and competitively inhibit BET protein interaction with acetylated chromatin. Alternative chemical probes that act orthogonally to the highly-conserved acetyl-lysine binding sites may exhibit selectivity within the BET family and avoid recently reported toxicity in clinical trials of BET bromodomain inhibitors. Here, we report the first identification of a ligandable site on a bromodomain outside the acetyl-lysine binding site. Inspired by our computational prediction of hotspots adjacent to non-homologous cysteine residues within the <i>C</i>-terminal Brd4 bromodomain (Brd4-BD2), we performed a mid-throughput mass spectrometry screen to identify cysteine-reactive fragments that covalently and selectively modify Brd4. Subsequent mass spectrometry, NMR and computational docking analyses of electrophilic fragment hits revealed a novel ligandable site near Cys356 that is unique to Brd4 among all human bromodomains. This site is orthogonal to the Brd4-BD2 acetyl-lysine binding site as Cys356 modification did not impact binding of the pan-BET bromodomain inhibitor JQ1 in fluorescence polarization assays. Finally, we tethered covalent fragments to JQ1 and performed NanoBRET assays to provide proof of principle that this orthogonal site can be covalently targeted in intact human cells. Overall, we demonstrate the potential of targeting sites orthogonal to bromodomain acetyl-lysine binding sites to develop bivalent and covalent inhibitors that displace Brd4 from chromatin.</p>


2019 ◽  
Author(s):  
Nga Phung ◽  
Hans Köbler ◽  
Diego Di Girolamo ◽  
Thi Tuyen Ngo ◽  
Gabrielle Sousa e Silva ◽  
...  

2019 ◽  
Author(s):  
Marina Vildanova ◽  
Anna Nikolskaia ◽  
Sergey Kozlov ◽  
Oleg Shevaleevskiy

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