Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Gilles Precigoux"'
Publikováno v:
International Journal of Peptide and Protein Research. 27:454-460
The crystal structure of the title compound, an analogue of the angiotensinogen-(10-13) peptide in which the N-terminal leucine and the C-terminal tyrosine are respectively replaced by the phenyloxy-acetic group and by phenylalanine, has been determi
Publikováno v:
International Journal of Peptide and Protein Research. 34:463-470
The tripeptide acetyl-L-prolyl-L-phenylalanyl-L-histidine crystallizes in the orthorhombic space group P2(1)2(1)2(1) with eight molecules in a unit cell of dimensions a = 9.028(2), b = 140.54(6) and c = 42.41(1)A. The structure has been solved by dir
Autor:
Claude Manigand, Gilles Precigoux, Jean-Marie Schmitter, Philippe Picard, Alain Dautant, Céline Aznar‐Derunes, Michael Goetz
Publikováno v:
Journal of Peptide Science. 8:365-372
The yeast Saccharomyces cerevisiae F1FO-ATPase e-subunit (61 residues) was synthesized by the solid-phase peptide approach under both acidic and basic strategies. Only the latter strategy allowed us to obtain a pure e-subunit. The strong propensity o
Autor:
P. Santambrogio, B. Langlois d'Estaintot, Gilles Precigoux, Bernard Gallois, Thierry Granier, Paolo Arosio, J. M. Chevalier, Carole Beaumont, J. M. Mellado, Alain Dautant
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 57:1491-1497
Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room tempe
Autor:
Françoise Bertola, Gilles Precigoux, Claude Manigand, Philippe Picard, Jean-Marie Schmitter, Michael Goetz
Publikováno v:
Journal of Peptide Science. 7:588-597
The HTLV-I integrase N-terminal domain [50-residue peptide (IN50)], and a 35-residue truncated peptide formed by residues 9–43 (IN35) have been synthesized by solid-phase peptide synthesis. Formation of the 50-residue zinc finger type structure thr
Autor:
Alain Dautant, Gilles Precigoux, B. Langlois d'Estaintot, P Saminadin, M Mondon, C Courseille
Publikováno v:
European Journal of Biochemistry. 267:457-464
Doxorubicin is among the most widely used anthracycline in cancer chemotherapy. In an attempt to avoid the cardiotoxicity and drug resistance of doxorubicin therapy, several analogues were synthesized. The cyanomorpholinyl derivative is the most cyto
Autor:
Gilles Precigoux, Béatrice Langlois d'Estaintot, Gérard Comberton, Thierry Granier, Bernard Gallois, Robert Crichton, Alain Dautant
Publikováno v:
Proteins: Structure, Function, and Genetics. 31:477-485
We refined the structure of the tetragonal form of recombinant horse L-chain apoferritin to 2.0 Angstrom and we compared it with that of the cubic form previously refined to the same resolution, The major differences between the two structures concer
Autor:
Michael Goetz, Danielle Londos-Gagliardi, Philippe Picard, Gilles Precigoux, Bernard Guillemain
Publikováno v:
Letters in Peptide Science. 4:351-358
The envelope of the human retrovirus HTLV-I (human T-cell leukemia virus type I), like those of other retroviruses, plays an important role in viral infection. One of the major immunodominant domains of HTLV-I surface glycoprotein (gp46), inducing an
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 53:580-587
Horse-spleen apoferritin is known to crystallize in three different space groups, cubic F432, tetragonal P42(1)2 and orthorhombic P2(1)2(1)2. A structure comparison of the cubic and tetragonal forms is presented here. Both crystal forms were obtained
Autor:
Béatrice Langlois d'Estaintot, Marie-Anges Michaux, Thierry Granier, Octavío Chavas-Alba, Bernard Gallois, Jose-Antonio Soruco, Gilles Precigoux, Robert R. Crichton, Alain Dautant, Francine Roland, Adelina Herbas
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 2:360-367
The X-ray structure of recombinant horse L-chain (rL) apoferritin, solved at 2.0 A resolution with a final R factor of 17.9%, gives evidence that the residue at position 93 in the sequence is a proline and not a leucine, as found in earlier sequencin