51207-85-3Relevant academic research and scientific papers
An Activatable Photosensitizer Targeted to γ-Glutamyltranspeptidase
Chiba, Mayumi,Ichikawa, Yuki,Kamiya, Mako,Komatsu, Toru,Ueno, Tasuku,Hanaoka, Kenjiro,Nagano, Tetsuo,Lange, Norbert,Urano, Yasuteru
, p. 10418 - 10422 (2017)
We adopted a spirocyclization-based strategy to design γ-glutamyl hydroxymethyl selenorhodamine green (gGlu-HMSeR) as a photo-inactive compound that would be specifically cleaved by the tumor-associated enzyme γ-glutamyltranspeptidase (GGT) to generate th
Development of an azo-based photosensitizer activated under mild hypoxia for photodynamic therapy
Piao, Wen,Hanaoka, Kenjiro,Fujisawa, Tomotsumi,Takeuchi, Satoshi,Komatsu, Toru,Ueno, Tasuku,Terai, Takuya,Tahara, Tahei,Nagano, Tetsuo,Urano, Yasuteru
, p. 13713 - 13719 (2017)
Photodynamic therapy (PDT) utilizes photoirradiation in the presence of photosensitizers to ablate cancer cells via generation of singlet oxygen (1O2), but it is important to minimize concomitant injury to normal tissues. One approac
Synergistic Effects of ppm Levels of Palladium on Natural Clinochlore for Reduction of Nitroarenes
Gholinejad, Mohammad,Oftadeh, Erfan,Shojafar, Mohammad,Sansano, José M.,Lipshutz, Bruce H.
, p. 4240 - 4248 (2019/09/06)
Augmenting the modified naturally occurring clay clinochlore with ppm amounts of palladium leads to a new and very effective reagent for the reduction of numerous aromatic nitro species. When palladium nanoparticles are supported on pyridyltriazole-modified clinochlore, iron within clinochlore acts synergistically with palladium to catalyze the reduction of a wide variety of nitroarenes at room temperature in aqueous media. Based on E-factor calculations, the catalyst system is found to be in line with green chemistry standards and can be recycled up to five times.
Starch functionalized creatine for stabilization of gold nanoparticles: Efficient heterogeneous catalyst for the reduction of nitroarenes
Gholinejad, Mohammad,Dasvarz, Neda,Shojafar, Mohammad,Sansano, José M.
, (2019/06/27)
Selective reduction of nitroaromatic pollutants into amines with recoverable and reusable heterogeneous catalysts is highly desirable. Herein, we prepared and characterized an efficient novel catalyst comprising 4 nm size Au nanoparticles supported on creatine modified starch. Using this catalyst, efficient reduction of nitroarenes into amines at room temperature in aqueous media was achieved. The presence of creatine in the structure of the catalyst plays important role in amount of Au loading, efficiency of the catalyst, recycling times, and leaching of Au compared to starch supported Au without creatine.
Design, synthesis and biological evaluation of novel 2-phenyl pyrimidine derivatives as potent Bruton's tyrosine kinase (BTK) inhibitors
Li, Xinyu,Shi, Binyu,Teng, Yu,Cheng, Yu,Yang, Huizhu,Li, Jiurong,Wang, Lianjian,He, Siying,You, Qidong,Xiang, Hua
supporting information, p. 294 - 299 (2019/03/02)
BTK is an effective target for the treatment of B-cell malignant tumors and autoimmune diseases. In this work, a series of 2-phenyl pyrimidine derivatives were prepared and their preliminary in vitro activities on B-cell leukemia cells as well as the BTK enzyme were determined. The results showed that compound 11g displayed the best inhibitory activity on BTK with an inhibition rate of 82.76% at 100 nM and excellent anti-proliferation activity on three B-cell leukemia lines (IC50 = 3.66 μM, 6.98 μM, and 5.39 μM against HL60, Raji and Ramos, respectively). Besides, the flow cytometry analysis results indicated that 11g inhibited the proliferation of the Raji cells in a dose- and time-dependent manner, and blocked the Ramos cells at the G0/G1 phase, which is in accordance with the positive control ibrutinib. The mechanism investigation demonstrated that 11g could inhibit the phosphorylation of BTK and its downstream substrate phospholipase γ2 (PLCγ2). All these results showed that 11g was a promising lead compound that merited further optimization as a novel class of BTK inhibitor for the treatment of B-cell lymphoblastic leukemia.
2-phenylpyrimidine compounds, preparation method and medical application
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Paragraph 0098; 0099; 0100; 0101; 0102, (2018/06/15)
The invention belongs to the field of medicines and particularly relates to 2-phenylpyrimidine compounds and pharmacologically-acceptable salts thereof and an isotope marker. The invention also discloses a pharmaceutical composition containing the substances and application of the pharmaceutical composition for treating diseases related with protein kinase activity, such as cancer and inflammation. (The formula is shown in the description).
HYDROGELS WITH BIODEGRADABLE CROSSLINKING
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Paragraph 01, (2017/11/16)
Hydrogels that degrade under appropriate conditions of pH and temperature by virtue of crosslinking compounds that cleave through an elimination reaction are described. The hydrogels may be used for delivery of various agents, such as pharmaceuticals.
TYK2 INHIBITORS AND USES THEREOF
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Paragraph 001074; 001075, (2015/09/28)
The present invention provides compounds, compositions thereof, and methods of using the same for the inhibition of TYK2, and the treatment of TYK2-mediated disorders.
SLOW-RELEASE CONJUGATES OF SN-38
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Paragraph 0059, (2015/04/22)
Conjugates of SN-38 that provide optimal drug release rates and minimize the formation of the corresponding glucuronate are described. The conjugates release SN-38 from a polyethylene glycol through a β-elimination mechanism.
Structure-activity relationship study of non-steroidal NPC1L1 ligands identified through cell-based assay using pharmacological chaperone effect as a readout
Karaki, Fumika,Ohgane, Kenji,Fukuda, Hiromitsu,Nakamura, Masahiko,Dodo, Kosuke,Hashimoto, Yuichi
, p. 3587 - 3609 (2014/07/07)
Niemann-Pick type C1-like 1 (NPC1L1) is an intestinal cholesterol transporter that is known to be the target of the cholesterol absorption inhibitor ezetimibe. We previously discovered steroidal NPC1L1 ligands by using a novel cell-based assay that employs pharmacological chaperone effect as a readout. Those steroid derivatives bound to a site different from both the sterol-binding domain and the ezetimibe-binding site, implying that they may be a novel class of NPC1L1 inhibitors with a distinct mode of action. As an extension of that work, we aimed here to find non-steroidal NPC1L1 ligands, which may be better candidates for clinical application than steroidal ligands, by using the same assay to screen our focused library of ligands for liver X receptor (LXR), a nuclear receptor that recognizes oxysterols as endogenous ligands. Here we describe identification of a novel class of NPC1L1 ligands with a ring-fused quinolinone scaffold, and an analysis of the structure-activity relationships of their derivatives as NPC1L1 ligands.
