1252801-16-3Relevant academic research and scientific papers
Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunit
Blackburn, Christopher,Gigstad, Kenneth M.,Hales, Paul,Garcia, Khristofer,Jones, Matthew,Bruzzese, Frank J.,Barrett, Cynthia,Liu, Jane X.,Soucy, Teresa A.,Sappal, Darshan S.,Bump, Nancy,Olhava, Edward J.,Fleming, Paul,Dick, Lawrence R.,Tsu, Christopher,Sintchak, Michael D.,Blank, Jonathan L.
, p. 461 - 476 (2012/05/05)
The mammalian 26S proteasome is a 2500 kDa multi-catalytic complex involved in intracellular protein degradation. We describe the synthesis and properties of a novel series of non-covalent di-peptide inhibitors of the proteasome used on a capped tri-pepti
Optimization of a series of dipeptides with a P3 threonine residue as non-covalent inhibitors of the chymotrypsin-like activity of the human 20S proteasome
Blackburn, Christopher,Barrett, Cynthia,Blank, Jonathan L.,Bruzzese, Frank J.,Bump, Nancy,Dick, Lawrence R.,Fleming, Paul,Garcia, Khristofer,Hales, Paul,Hu, Zhigen,Jones, Matthew,Liu, Jane X.,Sappal, Darshan S.,Sintchak, Michael D.,Tsu, Christopher,Gigstad, Kenneth M.
scheme or table, p. 6581 - 6586 (2011/02/23)
Starting from a tripeptide screening hit, a series of dipeptide inhibitors of the proteasome with Thr as the P3 residue has been optimized with the aid of crystal structures in complex with the β-5/6 active site of y20S. Derivative 25, (β5 IC50
