D Moras

发表

Overexpression, purification, and crystal structure of native ER alpha LBD.

D. Moras, S. Eiler, M. Ruff, 2001, Protein expression and purification.

Structural and functional relationships between aminoacyl-tRNA synthetases.

D. Moras, D Moras, 1992, Trends in biochemical sciences.

An operational RNA code for amino acids and possible relationship to genetic code.

R Giegé, P. Schimmel, S. Yokoyama, 1993, Proceedings of the National Academy of Sciences of the United States of America.

An attempt to unify the structure of polymerases.

P Argos, M Delarue, P. Argos, 1990, Protein engineering.

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.

D. Moras, N. Rochel, J. Wurtz, 2000, Molecular cell.

Conformational flexibility of tRNA: structural changes in yeast tRNA(Asp) upon binding to aspartyl-tRNA synthetase.

D. Moras, B. Rees, D Moras, 1996, Biochimie.

Crystal Structure of the Ligand-binding Domain of the Ultraspiracle Protein USP, the Ortholog of Retinoid X Receptors in Insects*

D. Moras, N. Rochel, I. Billas, 2001, The Journal of Biological Chemistry.

DNA self‐fitting: the double helix directs the geometry of its supramolecular assembly.

D. Moras, Y. Timsit, D Moras, 1994, The EMBO journal.

Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor.

D. Moras, J. Wurtz, D Moras, 2000, Molecular endocrinology.

Structural basis for isotype selectivity of the human retinoic acid nuclear receptor.

D. Moras, B. Klaholz, A. Mitschler, 2000, Journal of molecular biology.

Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli.

D. Moras, C. Romier, S. Fribourg, 2001, Journal of molecular biology.

Crystallographic structure of an RNA helix: [U(UA)6A]2.

B Chevrier, D. Moras, J. Johnson, 1989, Journal of molecular biology.

Binding of ligands and activation of transcription by nuclear receptors.

A. Steinmetz, D. Moras, J. Renaud, 2001, Annual review of biophysics and biomolecular structure.

Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)

D. Moras, A. Mitschler, A. Podjarny, 1991, Science.

Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR.

D. Moras, N. Rochel, C. Birck, 2001, Journal of molecular biology.

Overproduction and purification of native and queuine-lacking Escherichia coli tRNA(Asp). Role of the wobble base in tRNA(Asp) acylation.

G. Eriani, F. Martin, D. Moras, 1993, Journal of molecular biology.

Restrained refinement of two crystalline forms of yeast aspartic acid and phenylalanine transfer RNA crystals.

E Westhof, E. Westhof, D. Moras, 1987, Acta crystallographica. Section A, Foundations of crystallography.

Crystal Structure of a Mutant hERα Ligand-binding Domain Reveals Key Structural Features for the Mechanism of Partial Agonism*

D. Moras, J. Wurtz, S. Eiler, 2001, The Journal of Biological Chemistry.

Structural basis for engineering of retinoic acid receptor isotype-selective agonists and antagonists.

P Chambon, P. Chambon, R. Losson, 1999, Chemistry & biology.

A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.

D. Moras, P. Barth, A. Urzhumtsev, 1997, Structure.

Three-dimensional models of estrogen receptor ligand binding domain complexes, based on related crystal structures and mutational and structure-activity relationship data.

N Heinrich, N. Heinrich, D. Moras, 1998, Journal of medicinal chemistry.

Crystallographic refinement of yeast aspartic acid transfer RNA.

E Westhof, E. Westhof, D. Moras, 1985, Journal of molecular biology.

Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase.

M G Rossmann, M. Rossmann, D. Moras, 1977, The Journal of biological chemistry.

Ultrahigh resolution drug design I: Details of interactions in human aldose reductase–inhibitor complex at 0.66 Å

R E Cachau, B Chevrier, V. Lamour, 2004, Proteins.

Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine.

D. Moras, A. Dock-Brégeon, D Moras, 1999, Journal of molecular biology.

Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations.

M Karplus, M. Karplus, D. Moras, 1998, Journal of molecular biology.

Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.

B Chevrier, D. Moras, B. Chevrier, 1994, Structure.

Retinoic acid receptor: a simulation analysis of retinoic acid binding and the resulting conformational changes.

M Karplus, M. Karplus, S. Fischer, 1999, Journal of molecular biology.

Recognition of tRNAs by aminoacyl‐tRNA synthetases

D. Moras, D Moras, J Cavarelli, 1993, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Enantiomer discrimination illustrated by high-resolution crystal structures of the human nuclear receptor hRARgamma.

D. Moras, B. Klaholz, A. Mitschler, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Synthesis of aspartyl‐tRNAAsp in Escherichia coli—a snapshot of the second step

D. Moras, S. Eiler, J. Thierry, 1999, The EMBO journal.

The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit.

B Chevrier, D. Moras, B. Chevrier, 1996, European journal of biochemistry.

The nuclear receptor ligand-binding domain: structure and function.

H. Gronemeyer, D. Moras, D Moras, 1998, Current opinion in cell biology.

The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 A resolution.

B Chevrier, D. Moras, L. Mourey, 1997, Structure.

The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.

R Giegé, B Lorber, O. Nureki, 2000, Structure.