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Macrocyclization in the design of non-phosphorus-containing Grb2 SH2 domain-binding ligands

  1. Author:
    Shi, Z. D.
    Wei, C. Q.
    Lee, K. O.
    Liu, H. P.
    Zhang, M. C.
    Araki, T.
    Roberts, L. R.
    Worthy, K. M.
    Fisher, R. J.
    Neel, B. G.
    Kelley, J. A.
    Yang, D. J.
    Burke, T. R.

  2. Author Address

    Burke, TR, NCI, Med Chem Lab, CCR, NIH, Ft Detrick, MD 21702 USA NCI, Med Chem Lab, CCR, NIH, Ft Detrick, MD 21702 USA. Univ Michigan, Sch Med, Ann Arbor, MI 48109 USA. Beth Israel Deaconess Med Ctr, Boston, MA 02215 USA. SAIC, Prot Chem Lab, Frederick, MD 21702 USA.
    1. Year: 2004
  2. Journal: Journal of Medicinal Chemistry
    1. 47
    2. 8
    3. Pages: 2166-2169
  4. Type of Article: Article
  1. Abstract:

    Macrocyclization from the phosphotyrosyl. (pTyr) mimetic's beta-position has previously been shown to enhance Grb2 SH2 domain-binding affinity of phosphonate-based analogues. The current study examined the effects of such macrocyclization using a dicarboxymethyl-based pTyr mimetic. In extracellular assays affinity was enhanced approximately 5-fold relative to an open-chain congener. Enhancement was also observed in whole-cell assays examining blockade of Grb2 binding to the erbB-2 protein-tyrosine kinase

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  2. DOI: 10.1021/jm030510e
  3. PMID: 15056012

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