Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases

Xiaoyi Hu, Anthony Addlagatta, Brian W. Matthews, Jun O. Liu

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

High-throughput screening of a library of compounds has led to the identification of a new structural class of human methionine aminopeptidases inhibitors. They inhibited the processing of 14-3-3γ in cells and blocked proliferation of both endothelial cells and transformed cancer cell lines. The picture shows the crystal structure of the complex of one inhibitor (yellow) with the type 1 human methionine aminopeptidase (blue CoII, red H2O). (Figure Presented)

Original languageEnglish (US)
Pages (from-to)3772-3775
Number of pages4
JournalAngewandte Chemie - International Edition
Volume45
Issue number23
DOIs
StatePublished - Jun 2 2006

Keywords

  • Cellular effects
  • Drug design
  • Enzymes
  • Inhibitors
  • Structure elucidation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint

Dive into the research topics of 'Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases'. Together they form a unique fingerprint.

Cite this