Gilquin B - Search Results

1

A gradual disruption of tight side-chain packing: 2D 1H-NMR characterization of acid-induced unfolding of CHABII.

Song J, Jamin N, Gilquin B, Vita C, Ménez A. Song J, et al. Among authors: gilquin b. Nat Struct Biol. 1999 Feb;6(2):129-34. doi: 10.1038/5815. Nat Struct Biol. 1999. PMID: 10048923

2

NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.

Song J, Gilquin B, Jamin N, Drakopoulou E, Guenneugues M, Dauplais M, Vita C, Ménez A. Song J, et al. Among authors: gilquin b. Biochemistry. 1997 Apr 1;36(13):3760-6. doi: 10.1021/bi962720h. Biochemistry. 1997. PMID: 9092804

3

Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications.

Bontems F, Gilquin B, Roumestand C, Ménez A, Toma F. Bontems F, et al. Among authors: gilquin b. Biochemistry. 1992 Sep 1;31(34):7756-64. doi: 10.1021/bi00149a003. Biochemistry. 1992. PMID: 1380828

4

Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins.

Bontems F, Roumestand C, Boyot P, Gilquin B, Doljansky Y, Menez A, Toma F. Bontems F, et al. Among authors: gilquin b. Eur J Biochem. 1991 Feb 26;196(1):19-28. doi: 10.1111/j.1432-1033.1991.tb15780.x. Eur J Biochem. 1991. PMID: 1705886 Free article.

5

Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins.

Bontems F, Roumestand C, Gilquin B, Ménez A, Toma F. Bontems F, et al. Among authors: gilquin b. Science. 1991 Dec 6;254(5037):1521-3. doi: 10.1126/science.1720574. Science. 1991. PMID: 1720574

6

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: gilquin b. J Mol Biol. 1994 Nov 4;243(4):719-35. doi: 10.1016/0022-2836(94)90043-4. J Mol Biol. 1994. PMID: 7966292

7

Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins.

Dauplais M, Gilquin B, Possani LD, Gurrola-Briones G, Roumestand C, Ménez A. Dauplais M, et al. Among authors: gilquin b. Biochemistry. 1995 Dec 26;34(51):16563-73. doi: 10.1021/bi00051a004. Biochemistry. 1995. PMID: 8527429

8

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: gilquin b. Biochemistry. 1996 Jul 2;35(26):8535-43. doi: 10.1021/bi960466n. Biochemistry. 1996. PMID: 8679614

The resulting chimeric protein, synthesized by chemical means, binds to AcChOR, though with a lower affinity than the snake toxins [Drakopoulou; E., Zinn-Justin, S., Guenneugues, M., Gilquin, B., Menez, A., & Vita, C. (1996) J. Biol. Chem. 271, 11979-11987]. ...

The resulting chimeric protein, synthesized by chemical means, binds to AcChOR, though with a lower affinity than the snake toxins [Drakopou …

9

On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures.

Dauplais M, Lecoq A, Song J, Cotton J, Jamin N, Gilquin B, Roumestand C, Vita C, de Medeiros CL, Rowan EG, Harvey AL, Ménez A. Dauplais M, et al. Among authors: gilquin b. J Biol Chem. 1997 Feb 14;272(7):4302-9. doi: 10.1074/jbc.272.7.4302. J Biol Chem. 1997. PMID: 9020148 Free article.

10

Novel miniproteins engineered by the transfer of active sites to small natural scaffolds.

Vita C, Vizzavona J, Drakopoulou E, Zinn-Justin S, Gilquin B, Ménez A. Vita C, et al. Among authors: gilquin b. Biopolymers. 1998;47(1):93-100. doi: 10.1002/(SICI)1097-0282(1998)47:1<93::AID-BIP10>3.0.CO;2-H. Biopolymers. 1998. PMID: 9692330 Review.

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