681465-87-2Relevant academic research and scientific papers
Terephthalamide derivatives as mimetics of the helical region of Bak peptide target Bcl-xL protein
Yin, Hang,Hamilton, Andrew D.
, p. 1375 - 1379 (2004)
A group of novel Bcl-xL/Bak antagonists, based on a terephthalamide scaffold, were designed to mimic the α-helical region of the Bak peptide. Good in vitro inhibition potencies in disrupting the Bak/Bcl-xL complex have been observed (terephthalamide 4, K
Visible light-induced radical addition/annulation to construct phenylsulfonyl-functionalized dihydrobenzofurans involving an intramolecular 1,5-hydrogen atom transfer process
Sun, Peipei,Xie, Shentong,Li, Yifan
supporting information, p. 8774 - 8779 (2020/12/02)
A visible light-induced radical cascade reaction of 2-alkynylarylethers with sodium sulfinates was established for the synthesis of sulfonyl-functionalized dihydrobenzofurans, and an intramolecular 1,5-hydrogen atom transfer was involved in this transformation. This process provided an efficient and convenient C-C formation protocol for the construction of a dihydrobenzofuran ring. Various substituents on 2-alkynylarylethers and sodium sulfinates were tolerated in the reaction, and the corresponding products were obtained in moderate to good yields.
Terephthalamide peptidomimetic compounds and methods
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Page/Page column 8; sheet 1, (2010/11/27)
The present invention relates to compounds and pharmaceutical compositions based upon terephthalamide which are proteomimetic and to methods for inhibiting the interaction of an alpha-helical protein with another protein or binding site. Methods for treat
Terephthalamide derivatives as mimetics of helical peptides: Disruption of the Bcl-xL/Bak interaction
Yin, Hang,Lee, Gui-In,Sedey, Kristine A.,Rodriguez, Johanna M.,Wang, Hong-Gang,Sebti, Said M.,Hamilton, Andrew D.
, p. 5463 - 5468 (2007/10/03)
A series of Bcl-xL/Bak antagonists, based on a terephthalamide scaffold, was designed to mimic the α-helical region of the Bak peptide. These molecules showed favorable in vitro activities in disrupting the Bcl-xL/Bak BH3 domain comp
