79902-31-1Relevant articles and documents
HMG-COA REDUCTASE DEGRADATION INDUCING COMPOUND
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, (2021/10/11)
The present invention relates HMG-CoA reductase degradation inducing compounds. Specifically, the present invention relates a bifunctional compound in which a HMG-CoA reductase binding moiety and an E3 ubiquitin ligase-binding moiety are linked by a chemical linker. The present invention also relates a method for preparing the compounds, and a method for degradation of HMG-CoA reducatase using the compounds, as well as use for prevention or treatment of HMG-CoA reductase related diseases using the compounds.
Hydroxy methyl glutaryl coenzyme A reductase inhibitors
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, (2017/04/29)
The invention relates to a compound, in particular to an HMG-GoA reductase inhibitor. The HMG-GoA reductase inhibitor is ester formed by naphthol and Cn polyhydroxyalkanoate or Cn olefine acid of the compound in the formula I, wherein n is an integer from six to fourteen. The compound can be effectively used for treating or preventing dyslipidemia, for example, the compound can effectively treat or prevent hypercholesteremia or mixed type hyperlipidemia.
Design and synthesis of dual-action inhibitors targeting histone deacetylases and 3-hydroxy-3-methylglutaryl coenzyme a reductase for cancer treatment
Chen, Jhih-Bin,Chern, Ting-Rong,Wei, Tzu-Tang,Chen, Ching-Chow,Lin, Jung-Hsin,Fang, Jim-Min
, p. 3645 - 3655 (2013/06/27)
A series of dual-action compounds were designed to target histone deacetylase (HDAC) and 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) by having a hydroxamate group essential for chelation with the zinc ion in the active site of HDAC and the key structural elements of statin for binding with both proteins. In our study, the statin hydroxamic acids prepared by a fused strategy are most promising in cancer treatments. These compounds showed potent inhibitory activities against HDACs and HMGR with IC50 values in the nanomolar range. These compounds also effectively reduced the HMGR activity as well as promoted the acetylations of histone and tubulin in cancer cells, but were not toxic to normal cells.