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H. Gillier-Pandraud

Bio: H. Gillier-Pandraud is an academic researcher from University of Paris. The author has contributed to research in topics: Pyranose & Hydrogen bond. The author has an hindex of 9, co-authored 22 publications receiving 222 citations.

Papers
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Journal ArticleDOI
TL;DR: In this article, the crystal data of 2-acetamido-i- N -( l -aspart-4-oyl)-2-deoxy-β- d -glucopyranosylamine are a 4.932 (2), b 24.218 (8), c 7.788 (3) A, and β 97.718° (5), space group P2 1, Z 2.06 for 1679 independent reflexions.

23 citations

Journal ArticleDOI
TL;DR: In this paper, Melezitose [O-α-d-glucopyranosyl-(1→3)-β-d -fructofuranosyl α- d -glucophyranoside] monohydrate was crystallized in two polymorphic forms (I and II) and the structure of form II, studied by X-ray crystallography, showed an orthorhombic cell having a 7.135 (4), b 15.362 (8), c 19.134 (8) A, space group P212121,

17 citations


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Patent
29 Oct 2007
TL;DR: The present invention encompasses albumin fusion proteins as discussed by the authors, as well as vectors containing these nucleic acids, host cells transformed with the nucleic acid vectors, and methods of making the fusion proteins of the invention.
Abstract: The present invention encompasses albumin fusion proteins. Nucleic acid molecules encoding the albumin fusion proteins of the invention are also encompassed by the invention, as are vectors containing these nucleic acids, host cells transformed with these nucleic acids vectors, and methods of making the albumin fusion proteins of the invention and using these nucleic acids, vectors, and/or host cells. Additionally the present invention encompasses pharmaceutical compositions comprising albumin fusion proteins and methods of treating, preventing, or ameliorating diseases, disorders or conditions using albumin fusion proteins of the invention.

998 citations

Journal ArticleDOI
TL;DR: X-ray diffraction studies yielded 3 A resolution crystal structures of hemagglutinin in complex with four of the synthetic analogs and with the naturally occurring cell-surface saccharide (alpha 2-3)sialyllactose, which could lead to the design of tight binding inhibitors of possible therapeutic value.
Abstract: The interaction between influenza virus hemagglutinin and its cell-surface receptor, 5-N-acetylneuraminic acid (sialic acid), was probed by the synthesis of 12 sialic acid analogs, including derivatives at the 2-carboxylate, 5-acetamido, 4-, 7-, and 9-hydroxyl, and glycosidic positions. The equilibrium dissociation constants of these analogs were determined by nuclear magnetic resonance spectroscopy. Ligand modifications that reduced or abolished binding included the replacement of the 2-carboxylate with a carboxamide, the substitution of azido or N-benzyloxycarbonyl groups for the 5-acetamido group, and the replacement of the 9-hydroxyl with amino or O-acetyl moieties. Modifications having little effect on binding included the introduction of longer chains at the 4-hydroxyl position, the replacement of the acetamido methyl group with an ethyl group, and the removal of the 7-hydroxyl group. X-ray diffraction studies yielded 3 A resolution crystal structures of hemagglutinin in complex with four of the synthetic analogs [alpha-2-O-methyl-, 4-O-acetyl-alpha-2-O-methyl-, 9-amino-9-deoxy-alpha-2-O-methyl-, and alpha-2-O-(4'-benzylamidocarboxybutyl)-N-acetylneuraminic acid] and with the naturally occurring cell-surface saccharide (alpha 2-3)sialyllactose. The X-ray studies unambiguously establish the position and orientation of bound sialic acid, indicate the position of the lactose group of (alpha 2-3)sialyllactose, and suggest the location of an alpha-glycosidic chain (4'-benzylamidocarboxybutyl) that increases the binding affinity of sialic acid by a factor of about 3. Although the protein complexed with alpha-2-O-methylsialic acid contains the mutation Gly-135-->Arg near the ligand binding site, the mutation apparently does not affect the ligand's position. The X-ray studies allow us to interpret the binding affinities in terms of the crystallographic structure. The results suggest further experiments which could lead to the design of tight binding inhibitors of possible therapeutic value.

354 citations

Book ChapterDOI
TL;DR: In this paper, the authors discuss the several possibilities regarding the specification of the energy associated with the anomeric effect, and the experimental data concerning the configurational and conformational equilibria of the Anomeric center and the related variations of valence geometry.
Abstract: Publisher Summary This chapter discusses the several possibilities regarding the specification of the energy associated with the anomeric effect, and the experimental data concerning the configurational and conformational equilibria of the anomeric center and the related variations of valence geometry. The free-energy aspect of the anomeric effect as displayed by the equilibria of isomers is the area wherein the very concept was incepted and developed, and which still dominates its investigation. A considerable amount of data has been accumulated during the past two decades on the anomeric effect in terms of structure, energy, reactivity, and other properties. The description and understanding of the nature of stereoelectronic effects is an appropriate field for the application of organic quantum chemistry. Although several molecular orbital (MO) methods successfully describe the stereochemical behavior of pyranose models, their application to the more complex carbohydrates and oligosaccharides is limited at present due to economical reasons. The various rationalizations of the anomeric effect have been offered over the past years; they may be roughly divided into two main groups—namely, the electrostatic and the delocalization rationalization of the anomeric effect. It may be expected that the intramolecular interactions involved in the anomeric effect also influence the other points on the generalized reaction hypersurface.

277 citations