58829-75-7Relevant academic research and scientific papers
Visible-light photocatalytic aerobic annulation for the green synthesis of pyrazoles
Ding, Ya,Zhang, Te,Chen, Qiu-Yun,Zhu, Chunyin
, p. 4206 - 4209 (2016)
A selective and high yielding synthesis of polysubstituted pyrazoles through a VLPC (visible light photoredox catalysis)-promoted reaction of hydrazine with Michael acceptors is reported. The method employs very mild reaction conditions and uses air as the terminal oxidant, which makes the process environmentally benign. Different types of Michael acceptors with various substituents can undergo the reaction to afford corresponding pyrazoles in good to excellent yields. The reaction is proposed to go through VLPC-promoted oxidation of hydrazine to diazene followed by its addition to Michael acceptors, other than the conventional condensation of hydrazine with a carbonyl.
Preparation method of 5-amino-4-cyanopyrazole
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Paragraph 0010-0014, (2020/06/20)
The invention belongs to the field of organic chemistry, relates to a preparation method of 5-amino-4-cyanopyrazole, and discloses a preparation method of 5-amino-4-cyanopyrazole. According to the invention, a series of 5-amino-4-cyanopyrazole are prepare
Regioselective Synthesis of Highly Functionalized Pyrazoles from N-Tosylhydrazones
Zhang, Qian,Tang, Meng
supporting information, (2019/03/19)
A regioselective synthesis of highly functionalized pyrazoles from N-tosylhydrazones was developed. The reaction was general for a wide range of substrates and demonstrated excellent tolerance to a variety of substituents, and the method has been successfully applied to the formal synthesis of ibrutinib.
Dye-sensitized hematite compososite photocatalyst and its photocatalytic performance of aerobic annulation
Huang, Dong-Liang,Zhang, Peng-Li,Qu, Ling-Ling,Chen, Qiu-Yun
, p. 132 - 136 (2018/05/04)
A visible light initiated catalyst (DP-pfa@Fe2O3) is synthesized and used as a photocatalyst for the synthesis of pyrazoles under mild reaction conditions. Holes (h+) and [rad] OH are the essential for the light-induced th
1,3-disubstituted-4-aminopyrazolo [3, 4-d] pyrimidines, a new class of potent inhibitors for phospholipase D
Kulkarni, Aditya,Quang, Phong,Curry, Victoriana,Keyes, Renee,Zhou, Weihong,Cho, Hyejin,Baffoe, Jonathan,T?r?k, Béla,Stieglitz, Kimberly
, p. 270 - 281 (2014/10/15)
Phospholipase D enzymes cleave lipid substrates to produce phosphatidic acid, an important precursor for many essential cellular molecules. Phospholipase D is a target to modulate cancer-cell invasiveness. This study reports synthesis of a new class of phospholipase D inhibitors based on 1,3-disubstituted-4-amino-pyrazolopyrimidine core structure. These molecules were synthesized and used to perform initial screening for the inhibition of purified bacterial phospholipase D, which is highly homologous to the human PLD1. Initially tested with the bacterial phospholipase D enzyme, then confirmed with the recombinant human PLD1 and PLD2 enzymes, the molecules presented here exhibited inhibition of phospholipase D activity (IC50) in the low-nanomolar to low-micromolar range with both monomeric substrate diC4PC and phospholipid vesicles and micelles. The data strongly indicate that these inhibitory molecules directly block enzyme/vesicle substrate binding. Preliminary activity studies using recombinant human phospholipase Ds in in vivo cell assays measuring both transphosphatidylation and head-group cleavage indicate inhibition in the mid- to low-nanomolar range for these potent inhibitory novel molecules in a physiological environment. This study reports synthesis of a new class of PLD inhibitors based on 1,3-disubstituted-4-amino-pyrazolopyrimidine core structure. These molecules exhibited inhibition of human recombinant PLD activity (IC 50) in the low-nanomolar to low-micromolar range with monomeric substrate diC4PC and phospholipid vesicles and micelles. Preliminary activity studies using recombinant human PLDs in in vivo cell assays measuring both transphosphatidylation and head-group cleavage indicates inhibition in the mid- to low-nanomolar range for these potent inhibitory novel molecules in a physiological environment.
A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL
Chapman, Eli,Farr, George W.,Furtak, Krystyna,Horwich, Arthur L.
scheme or table, p. 811 - 813 (2009/09/25)
The chaperonin GroEL is a megadalton-sized molecular machine that plays an essential role in the bacterial cell assisting protein folding to the native state through actions requiring ATP binding and hydrolysis. A combination of medicinal chemistry and genetics has been employed to generate an orthogonal pair, a small molecule that selectively inhibits ATPase activity of a GroEL ATP-binding pocket variant. An initial screen of kinase-directed inhibitors identified an active pyrazolo-pyrimidine scaffold that was iteratively modified and screened against a collective of GroEL nucleotide pocket variants to identify a cyclopentyl carboxamide derivative, EC3016, that specifically inhibits ATPase activity and protein folding by the GroEL mutant, I493C, involving a side chain positioned near the base of ATP. This orthogonal pair will enable in vitro studies of the action of ATP in triggering activation of GroEL-mediated protein folding and might enable further studies of GroEL action in vivo. The approach originated for studying kinases by Shokat and his colleagues may thus also be used to study large macromolecular machines.
