180903-09-7Relevant academic research and scientific papers
A covalent p97/VCP ATPase inhibitor can overcome resistance to CB-5083 and NMS-873 in colorectal cancer cells
Zhang, Gang,Li, Shan,Wang, Feng,Jones, Amanda C.,Goldberg, Alexander F.G.,Lin, Benjamin,Virgil, Scott,Stoltz, Brian M.,Deshaies, Raymond J.,Chou, Tsui-Fen
, (2021/01/25)
Small-molecule inhibitors of p97 are useful tools to study p97 function. Human p97 is an important AAA ATPase due to its diverse cellular functions and implication in mediating the turnover of proteins involved in tumorigenesis and virus infections. Multi
Visible-light photocatalytic aerobic annulation for the green synthesis of pyrazoles
Ding, Ya,Zhang, Te,Chen, Qiu-Yun,Zhu, Chunyin
supporting information, p. 4206 - 4209 (2016/09/09)
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.
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.
One-pot synthesis of tetrasubstituted pyrazoles - Proof of regiochemistry
Hanefeld, Ulf,Rees, Charles W.,White, Andrew J. P.,Williams, David J.
, p. 1545 - 1552 (2007/10/03)
1-Alkyl-5-amino-3-aryl-4-cyanopyrazoles, useful intermediates for fused heterocyclic systems, are synthesised by a one-pot three-step procedure from acid chlorides, malononitrile and alkylhydrazines. The regiochemistry of the hydrazine incorporation was p
