Entry into a new class of potent proteasome inhibitors having high antiproliferative activity by structure-based design

Journal of Medicinal Chemistry

Volumn 47, Issue 20, 2004, Pages 4810-4813

  Furet, Pascal ^a   Imbach, Patricia ^a   Noorani, Maria ^a   Koeppler, Juergen ^a   Laumen, Kurt ^a   Lang, Marc ^a   Guagnano, Vito ^a   Fuerst, Peter ^a   Roesel, Johannes ^a   Zimmermann, Johann ^a   García Echeverría, Carlos ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME INHIBITOR;

ANTINEOPLASTIC ACTIVITY; ARTICLE; CELL ASSAY; CONTROLLED STUDY; COVALENT BOND; DRUG DESIGN; DRUG POTENCY; DRUG STRUCTURE; DRUG SYNTHESIS; HUMAN; HUMAN CELL;

ANTINEOPLASTIC AGENTS; BINDING SITES; CELL DIVISION; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DRUG SCREENING ASSAYS, ANTITUMOR; HUMANS; HYDROGEN BONDING; INHIBITORY CONCENTRATION 50; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MULTIENZYME COMPLEXES; OLIGOPEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR CELLS, CULTURED;

EID: 4544337315     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm049660v     Document Type: Article

References (33)

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32. The resolution of the racemic N-acetyl-3,4,5-trimethoxy-L,D-phenylalanine methyl ester was performed by enzyme-catalyzed hydrolysis of the L-ester using Alcalase (Novo Nordisk) as described in the literature. Nestor, J. J., Jr.; Ho, T. L.; Simpson, R. A.; Horner, B. L.; Jones, G. H.; McRae, G. I.; Vickery, B. H. Synthesis and Biological Activity of Some Very Hydrophobic Superagonist Analogues of Luteinizing Hormone-Releasing Hormone. J. Med. Chem. 1982, 25, 795-801. Tyagi, O. D.; Boll, P. M. Synthesis of (S)-3,4-dihydroxyphenylalanine (L-DOPA) and unnatural α-amino acids via enzymatic resolution using alcalase. Indian J. Chem. 1992, 851-854.
33. This residue can be Tyr 135 or Ser 157 of subunit HC5. See ref 24.