PMID

Data

Article Title

Organization

Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.

Kezar Life Sciences

Structure-based design of฿1i or฿5i specific inhibitors of human immunoproteasomes.

Leiden Institute of Chemistry and Netherlands Proteomics Centre

Identification of N, C-capped di- and tripeptides as selective immunoproteasome inhibitors.

Chinese Academy of Medical Sciences and Peking Union Medical College

Structure-Based Optimization and Discovery of M3258, a Specific Inhibitor of the Immunoproteasome Subunit LMP7 (?5i).

Merck

Cell-based screening of extracts of natural sources to search for inhibitors of the ubiquitin-proteasome system and identification of proteasome inhibitors from the fungus Remotididymella sp.

Kumamoto University

Macrocyclic Peptides that Selectively Inhibit the

Weill Cornell Medicine

Development of peptide epoxyketones as selective immunoproteasome inhibitors.

Zhejiang University

Target Validation and Identification of Novel Boronate Inhibitors of the Plasmodium falciparum Proteasome.

The University of Melbourne

Required Immunoproteasome Subunit Inhibition Profile for Anti-Inflammatory Efficacy and Clinical Candidate KZR-616 ((2 S,3 R)- N-(( S)-3-(Cyclopent-1-en-1-yl)-1-(( R)-2-methyloxiran-2-yl)-1-oxopropan-2-yl)-3-hydroxy-3-(4-methoxyphenyl)-2-(( S)-2-(2-morpholinoacetamido)propanamido)propenamide).

Kezar Life Sciences

Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases.

Hangzhou Xixi Hospital

Structure-Based Design of Inhibitors Selective for Human Proteasome ?2c or ?2i Subunits.

Leiden Institute of Chemistry and Netherlands Proteomics Centre

Tetradehydrohalicyclamine B, a new proteasome inhibitor from the marine sponge Acanthostrongylophora ingens.

Kumamoto University

Structure-based design of human immuno- and constitutive proteasomes inhibitors.

Universit£

Potent and Highly Selective Inhibitors of the Proteasome Trypsin-like Site by Incorporation of Basic Side Chain Containing Amino Acid Derived Sulfonyl Fluorides.

University of Glasgow