scholarly journals Catalytic Hydrogenation and Hydrodeoxygenation of Furfural over Pt(111): A Model System for the Rational Design and Operation of Practical Biomass Conversion Catalysts

2017 ◽  
Vol 121 (15) ◽  
pp. 8490-8497 ◽  
Author(s):  
Martin J. Taylor ◽  
Li Jiang ◽  
Joachim Reichert ◽  
Anthoula C. Papageorgiou ◽  
Simon K. Beaumont ◽  
...  
2004 ◽  
Vol 11 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Thomas Duerfahrt ◽  
Katrin Eppelmann ◽  
Rolf Müller ◽  
Mohamed A. Marahiel

Molecules ◽  
2019 ◽  
Vol 24 (16) ◽  
pp. 2879 ◽  
Author(s):  
Lucas Ferreira Ribeiro ◽  
Vanesa Amarelle ◽  
Luana de Fátima Alves ◽  
Guilherme Marcelino Viana de Siqueira ◽  
Gabriel Lencioni Lovate ◽  
...  

Protein engineering emerged as a powerful approach to generate more robust and efficient biocatalysts for bio-based economy applications, an alternative to ecologically toxic chemistries that rely on petroleum. On the quest for environmentally friendly technologies, sustainable and low-cost resources such as lignocellulosic plant-derived biomass are being used for the production of biofuels and fine chemicals. Since most of the enzymes used in the biorefinery industry act in suboptimal conditions, modification of their catalytic properties through protein rational design and in vitro evolution techniques allows the improvement of enzymatic parameters such as specificity, activity, efficiency, secretability, and stability, leading to better yields in the production lines. This review focuses on the current application of protein engineering techniques for improving the catalytic performance of enzymes used to break down lignocellulosic polymers. We discuss the use of both classical and modern methods reported in the literature in the last five years that allowed the boosting of biocatalysts for biomass degradation.


2019 ◽  
Vol 21 (3) ◽  
pp. 704-711 ◽  
Author(s):  
Fan Yang ◽  
Minjian Wang ◽  
Wei Liu ◽  
Bin Yang ◽  
Ying Wang ◽  
...  

Noble-metal-free catalytic hydrogenation of nitroarenes is achieved through the rational design of atomically dispersed Ni sites on N-doped porous carbon. The outstanding activity of the catalyst originates from the atomic dispersion of Ni active sites with a high Ni–N3 content.


2017 ◽  
Vol 23 (6) ◽  
pp. 5821-5823 ◽  
Author(s):  
Huixian Yu ◽  
Zhiwei Guo ◽  
Yindi Zang ◽  
Yan Jin ◽  
Tao Shi ◽  
...  

2016 ◽  
Vol 6 (13) ◽  
pp. 5102-5115 ◽  
Author(s):  
Biplab Banerjee ◽  
Ramana Singuru ◽  
Sudipta K. Kundu ◽  
Karnekanti Dhanalaxmi ◽  
Linyi Bai ◽  
...  

Core–shell catalytic nanoreactor was designed, exhibiting high catalytic activity for levulinic acid hydrogenation.


2019 ◽  
Vol 11 (44) ◽  
pp. 41204-41214 ◽  
Author(s):  
Yuan Zhao ◽  
Wei Ke ◽  
Juanjuan Shao ◽  
Fangjie Zheng ◽  
Han Liu ◽  
...  

2021 ◽  
Author(s):  
Brandon Ashfeld ◽  
Francisco Huizar ◽  
Harrison Hill ◽  
Jeremiah Zartman ◽  
Emily Bacher ◽  
...  

Deregulation of dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) plays a significant role in developmental brain defects, early-onset neurodegeneration, neuronal cell loss, and dementia. Herein, we report the discovery of three new classes of <i>N</i>-heterocyclic DYRK1A inhibitors based on the potent, yet toxic kinase inhibitors, harmine and harmol. An initial in vitro evaluation of the small molecule collection assembled revealed that the core heterocyclic motifs benzofuranones, oxindoles, and pyrrolones, showed statistically significant DYRK1A inhibition. Further, the utilization of a low cost, high-throughput functional genomic in vivo model system to identify small molecule inhibitors that normalize DYRK1A overexpression phenotypes is described. This in vivo assay confirmed the in vitro results, and the resulting correspondence validates generated classes as architectural motifs that serve as potential DYRK1A inhibitors. Further expansion and analysis of these core compound structures will allow discovery of safe, more effective chemical inhibitors of DYRK1A to ameliorate phenotypes caused by DYRK1A overexpression.


2021 ◽  
Author(s):  
Brandon Ashfeld ◽  
Francisco Huizar ◽  
Harrison Hill ◽  
Jeremiah Zartman ◽  
Emily Bacher ◽  
...  

Deregulation of dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) plays a significant role in developmental brain defects, early-onset neurodegeneration, neuronal cell loss, and dementia. Herein, we report the discovery of three new classes of <i>N</i>-heterocyclic DYRK1A inhibitors based on the potent, yet toxic kinase inhibitors, harmine and harmol. An initial in vitro evaluation of the small molecule collection assembled revealed that the core heterocyclic motifs benzofuranones, oxindoles, and pyrrolones, showed statistically significant DYRK1A inhibition. Further, the utilization of a low cost, high-throughput functional genomic in vivo model system to identify small molecule inhibitors that normalize DYRK1A overexpression phenotypes is described. This in vivo assay confirmed the in vitro results, and the resulting correspondence validates generated classes as architectural motifs that serve as potential DYRK1A inhibitors. Further expansion and analysis of these core compound structures will allow discovery of safe, more effective chemical inhibitors of DYRK1A to ameliorate phenotypes caused by DYRK1A overexpression.


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