CuAAC Click Chemistry Accelerates the Discovery of Novel Chemical Scaffolds as Promising Protein Tyrosine Phosphatases Inhibitors

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	CuAAC Click Chemistry Accelerates the Discovery of Novel Chemical Scaffolds as Promising Protein Tyrosine Phosphatases Inhibitors
	He, X. -P.1,2; Xie, J.4; Tang, Y.1,2; Li, J.3 ; Chen, G. -R.1,2
刊名	CURRENT MEDICINAL CHEMISTRY
	2012-05
卷号	19 期号:15 页码:2399-2405
关键词	Protein tyrosine phosphatase click chemistry in situ screening drug discovery CuAAC tyrosine phosphorylation dephosphorylation carbohydrate amino acid salicylic acid isoxazole acid ketocarboxylic acid competitive inhibitor bidentate
ISSN号	0929-8673
文献子类	Review
英文摘要	Protein tyrosine phosphatases (PTPs) are crucial regulators for numerous biological processes in nature. The dysfunction and overexpression of many PTP members have been demonstrated to cause fatal human diseases such as cancers, diabetes, obesity, neurodegenerative diseases and autoimmune disorders. In the past decade, considerable efforts have been devoted to the production of PTPs inhibitors by both academia and the pharmaceutical industry. However, there are only limited drug candidates in clinical trials and no commercial drugs have been approved, implying that further efficient discovery of novel chemical entities competent for inhibition of the specific PTP target in vivo remains yet a challenge. In light of the click-chemistry paradigm which advocates the utilization of concise and selective carbon-heteroatom ligation reactions for the modular construction of useful compound libraries, the Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition reaction (CuAAC) has fueled enormous energy into the modern drug discovery. Recently, this ingenious chemical ligation tool has also revealed efficacious and expeditious in establishing large combinatorial libraries for the acquisition of novel PTPs inhibitors with promising pharmacological profiles. We thus offer here a comprehensive review highlighting the development of PTPs inhibitors accelerated by the CuAAC click chemistry.
资助项目	National Natural Science Foundation of China[21176076] ; National Natural Science Foundation of China[81125023] ; Shanghai Committee of Science and Technology[10410702700] ; Fundamental Research Funds for the Central Universities[WK1013002] ; China Postdoctoral Science Foundation[2011M500069] ; French Embassy in PR China[00000000] ; ENS Cachan[00000000]
WOS关键词	COMBINATORIAL SYNTHESIS ; INSULIN SENSITIVITY ; PTP1B INHIBITORS ; TERMINAL ALKYNES ; CANCER ; 1B ; CYCLOADDITION ; MICE ; ACQUISITION ; LIBRARY
WOS研究方向	Biochemistry & Molecular Biology ; Pharmacology & Pharmacy
语种	英语
出版者	BENTHAM SCIENCE PUBL LTD
WOS记录号	WOS:000303130200009
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/278097]
专题	国家新药筛选中心中科院受体结构与功能重点实验室新药研究国家重点实验室药物化学研究室所领导药物安全性评价中心
通讯作者	Li, J.
作者单位	1.E China Univ Sci & Technol, Key Lab Adv Mat, Shanghai 200237, Peoples R China; 2.E China Univ Sci & Technol, Inst Fine Chem, Shanghai 200237, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, Natl Ctr Drug Screening,State Key Lab Drug Res, Shanghai 201203, Peoples R China; 4.CNRS, UMR 8531, Inst Alembert, PPSM,ENS Cachan, F-94235 Cachan, France
推荐引用方式 GB/T 7714	He, X. -P.,Xie, J.,Tang, Y.,et al. CuAAC Click Chemistry Accelerates the Discovery of Novel Chemical Scaffolds as Promising Protein Tyrosine Phosphatases Inhibitors[J]. CURRENT MEDICINAL CHEMISTRY,2012,19(15):2399-2405.
APA	He, X. -P.,Xie, J.,Tang, Y.,Li, J.,&Chen, G. -R..(2012).CuAAC Click Chemistry Accelerates the Discovery of Novel Chemical Scaffolds as Promising Protein Tyrosine Phosphatases Inhibitors.CURRENT MEDICINAL CHEMISTRY,19(15),2399-2405.
MLA	He, X. -P.,et al."CuAAC Click Chemistry Accelerates the Discovery of Novel Chemical Scaffolds as Promising Protein Tyrosine Phosphatases Inhibitors".CURRENT MEDICINAL CHEMISTRY 19.15(2012):2399-2405.