Lin Yao
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Lin Yao has a total of 14 co-authors. Here are the top co-authors by number of shared publications:
Dongxu Zhang
Department of Medicinal Chemistry School of Pharmacy Fourth Military Medical University 169 Changle West Road Xi'an 710032 P.R. China
1 shared publication- Huifang Nie
Department of Medicinal Chemistry, School of Pharmacy, Fourth Military Medical University, Xi’an 710032, China
1 shared publication - Huifang Nie
Department of Medicinal Chemistry, School of Pharmacy, Air Force Medical University, Xi’an 300071, China
1 shared publication Libin Wang
Department of Medicinal Chemistry School of Pharmacy Fourth Military Medical University 169 Changle West Road Xi'an 710032 P.R. China
1 shared publication- Qin Ouyang
Third Military Medical University
1 shared publication - Sheng-Yong Zhang
College of Life Sciences, Northwest University
1 shared publication
Latest Publications
- Open Access
Discovery of Novel Non-Oxime Reactivators Showing In Vivo Antidotal Efficiency for Sarin Poisoned Mice
A family of novel efficient non-oxime compounds exhibited promising reactivation efficacy for VX and sarin inhibited human acetylcholinesterase was discovered. It was found that aromatic groups coupled to Mannich phenols and the introduction of imidazole to the ortho position of phenols would dramatically enhance reactivation efficiency. Moreover, the in vivo experiment was conducted, and the results demonstrated that Mannich phenol L10R1 (30 mg/kg, ip) could afford 100% 48 h survival for mice of 2*LD50 sarin exposure, which is promising for the development of non-oxime reactivators with central efficiency.
Open AccessDiscovery of Novel Non-Oxime Reactivators Showing In Vivo Antidotal Efficiency for Sarin Poisoned Mice
A family of novel efficient non-oxime compounds exhibited promising reactivation efficacy for VX and sarin inhibited human acetylcholinesterase was discovered. It was found that aromatic groups coupled to Mannich phenols and the introduction of imidazole to the ortho position of phenols would dramatically enhance reactivation efficiency. Moreover, the in vivo experiment was conducted, and the results demonstrated that Mannich phenol L10R1 (30 mg/kg, ip) could afford 100% 48 h survival for mice of 2*LD50 sarin exposure, which is promising for the development of non-oxime reactivators with central efficiency.
- 29 January 2018
- Published by Wiley in ChemCatChem
- Vol. 10 (4) , 804-809
Chiral Ferrocenyl N,N Ligands with Intramolecular Hydrogen Bonds for Highly Enantioselective Allylic Alkylations
Several new ferrocene‐derived bidentate N ligands, which contain multiple chiral factors, have been designed and synthesized by a rational combination of oxazoline and pyridine. Their catalytic performances were investigated preliminarily in Pd‐catalyzed asymmetric allylic alkylation, and excellent reactivities and enantioselectivities (up to 99 % yield and 98 % ee) were realized if we used the ligand with a matched chirality. DFT calculations were used to illustrate that an intramolecular hydrogen bond formed between the hydroxyl group and the oxazoline fragment of the ligand contributed to the optimal conformation of the ligand‐Pd‐allyl complex.
- 29 January 2018
- Published by Wiley in ChemCatChem
- Vol. 10 (4) , 804-809
Chiral Ferrocenyl N,N Ligands with Intramolecular Hydrogen Bonds for Highly Enantioselective Allylic Alkylations
Several new ferrocene‐derived bidentate N ligands, which contain multiple chiral factors, have been designed and synthesized by a rational combination of oxazoline and pyridine. Their catalytic performances were investigated preliminarily in Pd‐catalyzed asymmetric allylic alkylation, and excellent reactivities and enantioselectivities (up to 99 % yield and 98 % ee) were realized if we used the ligand with a matched chirality. DFT calculations were used to illustrate that an intramolecular hydrogen bond formed between the hydroxyl group and the oxazoline fragment of the ligand contributed to the optimal conformation of the ligand‐Pd‐allyl complex.