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Scorpion toxins as natural scaffolds for protein engineering.
Vita C, Roumestand C, Toma F, Ménez A. Vita C, et al. Among authors: menez a. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6404-8. doi: 10.1073/pnas.92.14.6404. Proc Natl Acad Sci U S A. 1995. PMID: 7541540 Free PMC article.
Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.
Roumestand C, Gilquin B, Trémeau O, Gatineau E, Mouawad L, Ménez A, Toma F. Roumestand C, et al. Among authors: menez a. J Mol Biol. 1994 Nov 4;243(4):719-35. doi: 10.1016/0022-2836(94)90043-4. J Mol Biol. 1994. PMID: 7966292
Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein.
Zinn-Justin S, Guenneugues M, Drakopoulou E, Gilquin B, Vita C, Ménez A. Zinn-Justin S, et al. Among authors: menez a. Biochemistry. 1996 Jul 2;35(26):8535-43. doi: 10.1021/bi960466n. Biochemistry. 1996. PMID: 8679614
This small and functionally versatile template contains an alpha-helix and a triple beta-sheet linked by three disulfide bridges. With the view to introduce novel functional centers within this fold, we replaced the sequence (the cysteines and glycines excepted) of the ori …
This small and functionally versatile template contains an alpha-helix and a triple beta-sheet linked by three disulfide bridges. Wit …
254 results