165256-89-3Relevant academic research and scientific papers
HETEROCYCLIC COMPOUNDS FOR MODULATING NR2F6
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Paragraph 00545-00547, (2021/09/04)
The present disclosure relates to compounds capable of modulating the activity of NR2F6. The compounds of the disclosure may be used in methods for the prevention and/or the treatment of diseases and disorders associated with modulating NR2F6 activity.
Dimethylaminomethylphosphonic acid derivatives-promoted CuI-catalyzed synthesis of aryl ethers
Jin, Ying,Liu, Jinyong,Yin, Yingwu,Fu, Hua,Jiang, Yuyang,Zhao, Yufen
, p. 1564 - 1568 (2007/10/03)
An inexpensive and efficient catalyst system for synthesis of aryl ethers has been developed by using 20 mol% CuI as the catalyst, 30 mol% dimethylaminomethylphosphonic acid derivatives as the new ligands, K 2CO3 as the base and toluene as the solvent. This is the first example using aminophosphonates as the ligands for Ullmann ether coupling reaction. Georg Thieme Verlag Stuttgart.
INHIBITORS OF FARNESYL-PROTEIN TRANSFERASE
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, (2008/06/13)
The present invention comprises peptidomimetic compounds which comprise a suitably aniline and aminoalkylbenzene moieties. The instant compounds inhibit the farnesyl-protein transferase enzyme and the farnesylation of certain proteins. The invention is further directed to chemotherapeutic compositions containing the compounds of this invention and methods for inhibiting farnesyl-protein transferase and the farnesylation of the oncogene protein Ras.
Diarylether inhibitors of farnesyl-protein transferase
Dinsmore, Christopher J.,Williams, Theresa M.,Hamilton, Kelly,O'Neill, Timothy J.,Rands, Elaine,Koblan, Kenneth S.,Kohl, Nancy E.,Gibbs, Jackson B.,Graham, Samuel L.,Hartman, George D.,Oliff, Allen I.
, p. 1345 - 1348 (2007/10/03)
The design and synthesis of simple nonpeptide inhibitors of farnesyl-protein transferase (FTase) are described. Cysteine-derived diarylether frameworks are appropriate structural replacements for the C-terminal tetrapeptide portion of the Ras protein, and possess in vitro potency against FTase. Inhibitory activity is dependent on the ring-substitution pattern, and does not require the presence of a C-terminal carboxylate group.
