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The isolation, total synthesis and structure elucidation of chlorofusin, a natural product inhibitor of the p53-mDM2 protein-protein interaction

Academic Article
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Overview

related to degree

  • Clark, Ryan C, Ph.D. in Chemistry, Scripps Research 2003 - 2008
  • Lee, Sang Yeul, Ph.D. in Chemistry, Scripps Research 2003 - 2008

authors

  • Clark, Ryan C
  • Lee, Sang Yeul
  • Searcey, M.
  • Boger, Dale

publication date

  • 2009

journal

  • Natural Product Reports  Journal

abstract

  • Inhibitors of key protein-protein interactions are emerging as exciting therapeutic targets for the treatment of cancer. One such interaction between MDM2 (HDM2) and p53, that silences the tumour suppression activities of p53, was found to be inhibited by the recently isolated natural product chlorofusin. Synthetic studies on this complex natural product summarized herein have served to reassign its chromophore relative stereochemistry, assign its absolute stereochemistry, and provided access to a series of key analogues and partial structures for biological evaluation.

subject areas

  • Antineoplastic Agents
  • Drug Design
  • Fusarium
  • Molecular Structure
  • Neoplasms
  • Peptides, Cyclic
  • Proto-Oncogene Proteins c-mdm2
  • Tumor Suppressor Protein p53
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Identity

PubMed Central ID

  • PMC2719831

International Standard Serial Number (ISSN)

  • 0265-0568

Digital Object Identifier (DOI)

  • 10.1039/b821676b

PubMed ID

  • 19642417
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Additional Document Info

start page

  • 465

end page

  • 477

volume

  • 26

issue

  • 4

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