Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/cmdc.200800050 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Vinyl Sulfone-Based Inhibitors of Nonstructural Protein 2 Block the Replication of Venezuelan Equine Encephalitis Virus.
ACS Med Chem Lett
November 2020
Department of Chemistry, Physics, and Atmospheric Sciences, Jackson State University, Jackson, Mississippi 39217-0095, United States.
Emerging infectious diseases like those caused by arboviruses such as Venezuelan equine encephalitis virus (VEEV) pose a serious threat to public health systems. Development of medical countermeasures against emerging infectious diseases are of utmost importance. In this work, an acrylate and vinyl sulfone-based chemical series was investigated as promising starting scaffolds against VEEV and as inhibitors of the cysteine protease domain of VEEV's nonstructural protein 2 (nsP2).
View Article and Find Full Text PDFAminooxylation Horner-Wadsworth-Emmons Sequence for the Synthesis of Enantioenriched γ-Functionalized Vinyl Sulfones.
J Org Chem
February 2016
Centre for Synthesis and Chemical Biology, School of Chemistry, University College Dublin, Dublin 4, Ireland.
An operationally simple protocol for the synthesis of γ-hydroxy vinyl sulfones has been developed using a proline-based aldehyde aminooxylation, followed by a vinyl sulfone forming Horner-Wadsworth-Emmons olefination. The adducts, formed in high enantiopurity, were subsequently converted to γ-azido vinyl sulfones, and azide-alkyne click chemistry enabled the synthesis of vinyl sulfone-based triazoles as potential nonpeptidic cysteine protease inhibitors.
View Article and Find Full Text PDFA fragment-based method to discover irreversible covalent inhibitors of cysteine proteases.
J Med Chem
June 2014
Department of Chemistry, Center for Molecular Innovation and Drug Discovery, Chemistry of Life Processes Institute, Northwestern University, 2170 Campus Drive, Evanston, Illinois 60208, United States.
A novel fragment-based drug discovery approach is reported which irreversibly tethers drug-like fragments to catalytic cysteines. We attached an electrophile to 100 fragments without significant alterations in the reactivity of the electrophile. A mass spectrometry assay discovered three nonpeptidic inhibitors of the cysteine protease papain.
View Article and Find Full Text PDFProbing the anticancer mechanism of prospective herbal drug Withaferin A on mammals: a case study on human and bovine proteasomes.
BMC Genomics
December 2010
Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology (IIT) Delhi, Hauz Khas, New Delhi, India.
Background: The UPP (ubiquitin proteasome pathway) is the major proteolytic system in the cytosol and nucleus of all eukaryotic cells which regulates cellular events, including mitotis, differentiation, signal transduction, apoptosis, and inflammation. UPP controls activation of the transcriptional factor NF-κB (nuclear factor κB), which is a regulatory protein playing central role in a variety of cellular processes including immune and inflammatory responses, apoptosis, and cellular proliferation. Since the primary interaction of proteasomes occurs with endogenous proteins, the signalling action of transcription factor NF-κB can be blocked by inhibition of proteasomes.
View Article and Find Full Text PDFEstimation of transporters involved in the hepatobiliary transport of TA-0201CA using sandwich-cultured rat hepatocytes from normal and multidrug resistance-associated protein 2-deficient rats.
Drug Metab Dispos
September 2010
Department of Membrane Transport and Biopharmaceutics, Faculty of Pharmacy, Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa, Japan.
N-[6-[2-[(5-Bromo-2-pyrimidinyl)oxy]ethoxy]-5-(4-methylphenyl)-4-pyrimidinyl]-4-(2-hydroxy-1,1-dimethylethyl) benzenesulfonamide sodium salt (TA-0201) carboxylic acid form (TA-0201CA) is the primary and pharmacologically active metabolite of TA-0201, which is an orally active nonpeptide antagonist for endothelin receptors. A major elimination route of TA-0201CA in rats was biliary excretion. The aim of this study was to clarify the transporters responsible for the hepatobiliary transport of TA-0201CA by in vivo pharmacokinetic study and in vitro study using sandwich-cultured rat hepatocytes (SCRH) from normal rats [Sprague-Dawley rats (SDR)] and Eisai hyperbilirubinemic rats (EHBR).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!