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Volumn 14, Issue 3, 2004, Pages 639-643

Macrocyclic piperazinones as potent dual inhibitors of farnesyltransferase and geranylgeranyltransferase-I

Author keywords

Farnesyltransferase; Geranylgernyltransferase; Inhibitor

Indexed keywords

GERANYLGERANYLTRANSFERASE I; ISOENZYME; KETONE DERIVATIVE; L 778123; MACROCYCLIC COMPOUND; PIPERAZINE DERIVATIVE; PROTEIN FARNESYLTRANSFERASE INHIBITOR; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 1642575098     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2003.11.051     Document Type: Article
Times cited : (11)

References (21)
  • 20
    • 85030901058 scopus 로고    scopus 로고
    • A model of the FPTase active site containing FPP was derived from the 1LD8 pdb entry (ref 12b). Random conformations of 3o were generated using the distance geometry method JG (S. Kearsley, Merck & Co., Inc., unpublished). These conformations were energy minimized in the static active site using Batchmin and the MMFFs force field, while restraining the Zn-ligating nitrogen to its crystallographic position. The lowest energy structure is shown
    • A model of the FPTase active site containing FPP was derived from the 1LD8 pdb entry (ref 12b). Random conformations of 3o were generated using the distance geometry method JG (S. Kearsley, Merck & Co., Inc., unpublished). These conformations were energy minimized in the static active site using Batchmin and the MMFFs force field, while restraining the Zn-ligating nitrogen to its crystallographic position. The lowest energy structure is shown.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.