142769-36-6Relevant articles and documents
Copper-Catalyzed Hydroxylation of (Hetero)aryl Halides under Mild Conditions
Xia, Shanghua,Gan, Lu,Wang, Kailiang,Li, Zheng,Ma, Dawei
supporting information, p. 13493 - 13496 (2016/10/31)
The combination of Cu(acac)2 and N,N′-bis(4-hydroxyl-2,6-dimethylphenyl)oxalamide (BHMPO) provides a powerful catalytic system for hydroxylation of (hetero)aryl halides. A wide range of (hetero)aryl chlorides bearing either electron-donating or -withdrawing groups proceeded well at 130 °C, delivering the corresponding phenols and hydroxylated heteroarenes in good to excellent yields. When more reactive (hetero)aryl bromides and iodides were employed, the hydroxylation reactions completed at relatively low temperatures (80 and 60 °C, respectively) at low catalytic loadings (0.5 mol % Cu).
Pd/C-mediated depropargylation of propargyl ethers/amines in water
Rambabu,Bhavani,Swamy, Nalivela Kumara,Basaveswara Rao,Pal, Manojit
, p. 1169 - 1173 (2013/04/10)
Propargyl ethers and amines are effectively depropargylated to the parent alcohols or amines via a C-O/C-N bond cleavage catalyzed by 10% Pd/C in water. This simple, facile, and inexpensive methodology could be utilized for the selective removal of propargyl groups from a variety of aryl ethers and amines.
2-Aryl-3,3,3-trifluoro-2-hydroxypropionic acids: A new class of protein tyrosine phosphatase 1B inhibitors
Adams, David R.,Abraham, Achamma,Asano, Jun,Breslin, Catherine,Dick, Colin A.J.,Ixkes, Ulrich,Johnston, Blair F.,Johnston, Derek,Kewnay, Justin,Mackay, Simon P.,MacKenzie, Simon J.,McFarlane, Morag,Mitchell, Lee,Spinks, Daniel,Takano, Yasuo
, p. 6579 - 6583 (2008/09/16)
A new series of non-peptidic, mono-acid protein tyrosine phosphatase 1B (PTP1B) inhibitors has been identified by structure-based design. Compounds with 2-(indol-3-yl)- and 2-phenyl-3,3,3-trifluoro-2-hydroxypropionic acid core units targeted at the enzyme's primary site and a hydrophobic chlorophenylthiazole extension in its 2° site exhibit 3-60 μM IC50s for PTP1B inhibition in an Sf9 cell-based assay.
ARYL, ARYLOXY, AND ALKYLOXY SUBSTITUTED 1H-INDOL-3-YL GLYOXYLIC ACID DERIVATIVES AS INHIBITORS OF PLASMINOGEN ACTIVATOR INHIBITOR-1 (PAI-1)
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Page 32, (2010/02/07)
Compounds of formula (I) are provided: wherein R1, R2 and R3, are as defined herein, as well ad pharmaceutical composition and methods using the compounds as inhibitors of plasminogen activator inhibitor (PAI-1) and as the
A novel class of inhibitors for human steroid 5α-reductase: Synthesis and biological evaluation of indole derivatives. II
Igarashi, Susumu,Inami, Hiroshi,Hara, Hiromu,Fujii, Masahiro,Koutoku, Hiroshi,Oritani, Hiroyuki,Mase, Toshiyasu
, p. 382 - 388 (2007/10/03)
In a search for novel nonsteroidal inhibitors of human prostatic 5α- reductase, we found a new series of indole derivatives that showed potent inhibitory activities for the human enzyme. Among them, 4-[(1-benzyl-1- Hindol-5-yl)oxy]-3-chlorobenzoic acid (2d, YM-32906) showed more potent inhibitory activity than finasteride with an IC50 value of 0.44 nM. 3- Chloro-4-{[1-(4-phenoxybenzyl)-1H-indol-5-yl]oxy}benzoic acid (2m) showed inhibitory activities for both human and rat prostatic 5α-reductase with IC50 values of 2.1 and 73 nM, respectively. The synthesis and structure- activity relationships of these indole derivatives are presented.
Indole inhibitors of human nonpancreatic secretory phospholipase A2. 3. Indole-3-glyoxamides
Draheim, Susan E.,Bach, Nicholas J.,Dillard, Robert D.,Berry, Dennis R.,Carlson, Donald G.,Chirgadze, Nickolay Y.,Clawson, David K.,Hartley, Lawrence W.,Johnson, Lea M.,Jones, Noel D.,McKinney, Emma R.,Mihelich, Edward D.,Olkowski, Jennifer L.,Schevitz, Richard W.,Smith, Amy C.,Snyder, David W.,Sommers, Cynthia D.,Wery, Jean-Pierre
, p. 5159 - 5175 (2007/10/03)
The preceding papers of this series detail the development of functionalized indole-3-acetamides as inhibitors of hnps-PLA2. We describe here the extension of the structure-activity relationship to include a series of indole-3-glyoxamide derivatives. Functionalized indole-3-glyoxamides with an acidic substituent appended to the 4- or 5-position of the indole ring were prepared and tested as inhibitors of hnps-PLA2. It was found that the indole-3-glyoxamides with a 4-oxyacetic acid substituent had optimal inhibitory activity. These inhibitors exhibited an improvement in potency over the best of the indole-3-acetamides, and LY315920 (6m) was selected for evaluation clinically as an hnps-PLA2 inhibitor.
