NMR-based discovery of phosphotyrosine mimetics that bind to the Lck SH2 domain.
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P. Hajduk | S. Fesik | M. Zhou | M. Zhou | Ming-Ming Zhou
[1] J. Proudfoot,et al. Carboxymethyl-phenylalanine as a Replacement for Phosphotyrosine in SH2 Domain Binding* , 1998, The Journal of Biological Chemistry.
[2] P. Hajduk,et al. Discovering High-Affinity Ligands for Proteins , 1997, Science.
[3] P. Hajduk,et al. Discovering High-Affinity Ligands for Proteins: SAR by NMR , 1996, Science.
[4] M. Akamatsu,et al. L-O-(2-malonyl)tyrosine: a new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides. , 1995, Journal of medicinal chemistry.
[5] S. Shoelson,et al. Nonhydrolyzable phosphotyrosyl mimetics for the preparation of phosphatase-resistant SH2 domain inhibitors. , 1994, Biochemistry.
[6] Michael J. Eck,et al. Structure of the regulatory domains of the Src-family tyrosine kinase Lck , 1994, Nature.
[7] J. Brugge. New intracellular targets for therapeutic drug design. , 1993, Science.
[8] S. Harrison,et al. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck , 1993, Nature.
[9] Paul A. Keifer,et al. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity , 1992 .