46 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Terminal functionalized thiourea-containing dipeptides as multidrug-resistance reversers that target 20S proteasome and cell proliferation.
Guangxi Normal University
Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.
Kezar Life Sciences
Identification of noncovalent proteasome inhibitors with high selectivity for chymotrypsin-like activity by a multistep structure-based virtual screening.
University of Naples Federico Ii
Development of novel proteasome inhibitors based on phthalazinone scaffold.
Peking University Health Science Center
Optimization of peptidomimetic boronates bearing a P3 bicyclic scaffold as proteasome inhibitors.
Universit£
Identification of a new series of amides as non-covalent proteasome inhibitors.
Universit£
New C(4)- and C(1)-derivatives of furo[3,4-c]pyridine-3-ones and related compounds: evidence for site-specific inhibition of the constitutive proteasome and its immunoisoform.
Yerevan State University
A novel tamoxifen derivative, ridaifen-F, is a nonpeptidic small-molecule proteasome inhibitor.
Institute of Bio-Science and Technology
Potent proteasome inhibitors derived from the unnatural cis-cyclopropane isomer of Belactosin A: synthesis, biological activity, and mode of action.
Hokkaido University
Dimerized linear mimics of a natural cyclopeptide (TMC-95A) are potent noncovalent inhibitors of the eukaryotic 20S proteasome.
University Paris 6
Incorporation of non-natural amino acids improves cell permeability and potency of specific inhibitors of proteasome trypsin-like sites.
Leiden Institute of Chemistry and Netherlands Proteomics Centre
Molecular mechanisms of acquired proteasome inhibitor resistance.
University of California San Diego
Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasome's chymotrypsin-like sites.
Gorlaeus Laboratories
Optimization of subsite binding to the beta5 subunit of the human 20S proteasome using vinyl sulfones and 2-keto-1,3,4-oxadiazoles: syntheses and cellular properties of potent, selective proteasome inhibitors.
Celera
Identification of N, C-capped di- and tripeptides as selective immunoproteasome inhibitors.
Chinese Academy of Medical Sciences and Peking Union Medical College
Development of isoquinolinone derivatives as immunoproteasome inhibitors.
University of Messina
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
Discovery of a Novel Oral Proteasome Inhibitor to Block NLRP3 Inflammasome Activation with Anti-inflammation Activity.
Guangzhou Medical University
A new class of ?-ketoamide derivatives with potent anticancer and anti-SARS-CoV-2 activities.
Tsinghua University
Design, synthesis and biological evaluation of novel naphthoquinone-4-aminobenzensulfonamide/carboxamide derivatives as proteasome inhibitors.
Ege University
Design and synthesis of tripeptidyl furylketones as selective inhibitors against the ?5 subunit of human 20S proteasome.
Peking University Health Science Center
Target Validation and Identification of Novel Boronate Inhibitors of the Plasmodium falciparum Proteasome.
The University of Melbourne
Design, synthesis and biological evaluation of triaryl compounds as novel 20S proteasome inhibitors.
Chinese Academy of Medical Sciences and Peking Union Medical College
LMP2 Inhibitors as a Potential Treatment for Alzheimer's Disease.
University of Kentucky
Structure-Based Design of ?5c Selective Inhibitors of Human Constitutive Proteasomes.
Leiden Institute of Chemistry
Another look at phenolic compounds in cancer therapy the effect of polyphenols on ubiquitin-proteasome system.
Institute of Agricultural and Food Biotechnology
Exploration of novel macrocyclic dipeptide N-benzyl amides as proteasome inhibitors.
Zhejiang University
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
Identification of neomacrophorins isolated from Trichoderma sp. 1212-03 as proteasome inhibitors.
Iwate University
Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases.
Hangzhou Xixi Hospital
Synthesis and Biological Activity of Peptide ?-Ketoamide Derivatives as Proteasome Inhibitors.
University of Ferrara
Structure-Based Design of Inhibitors Selective for Human Proteasome ?2c or ?2i Subunits.
Leiden Institute of Chemistry and Netherlands Proteomics Centre
Design, synthesis, and biological evaluation of novel phenol ether derivatives as non-covalent proteasome inhibitors.
Zhejiang University
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£
Design, synthesis, in vitro and in vivo evaluation, and structure-activity relationship (SAR) discussion of novel dipeptidyl boronic acid proteasome inhibitors as orally available anti-cancer agents for the treatment of multiple myeloma and mechanism studies.
Nanjing Forestry University
Synthesis and biological evaluation of curcumin derivatives modified with ?-amino boronic acid as proteasome inhibitors.
Peking University
Ridaifen-F conjugated with cell-penetrating peptides inhibits intracellular proteasome activities and induces drug-resistant cell death.
Nagahama Institute of Bio-Science and Technology
Neomacrophorin X, a [4.4.3]Propellane-Type Meroterpenoid from Trichoderma sp. 1212-03.
Hirosaki University
Synthesis and biological activity of peptide proline-boronic acids as proteasome inhibitors.
Peking University
Urea-containing peptide boronic acids as potent proteasome inhibitors.
Peking University