Marie‐Ange Badet‐Denisot

ORCID: 0000-0003-3417-6330
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About
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Biochemical and Molecular Research
  • Enzyme Structure and Function
  • Polyamine Metabolism and Applications
  • Amino Acid Enzymes and Metabolism
  • Peptidase Inhibition and Analysis
  • Diet, Metabolism, and Disease
  • Advanced Fluorescence Microscopy Techniques
  • X-ray Diffraction in Crystallography
  • Near-Field Optical Microscopy
  • Lysosomal Storage Disorders Research
  • Bacterial Genetics and Biotechnology
  • Erythrocyte Function and Pathophysiology
  • Synthesis and Characterization of Heterocyclic Compounds
  • Crystallization and Solubility Studies
  • Organophosphorus compounds synthesis
  • Antimicrobial Resistance in Staphylococcus
  • Cannabis and Cannabinoid Research
  • Digital Holography and Microscopy
  • Inorganic and Organometallic Chemistry
  • Biochemical and Structural Characterization
  • Photosynthetic Processes and Mechanisms
  • Signaling Pathways in Disease
  • Fungal and yeast genetics research

Centre National de la Recherche Scientifique
2007-2024

Institut de Chimie des Substances Naturelles
2010-2024

Université Paris-Saclay
2024

Institut Pasteur
2000

Advanced Bioscience Laboratories (United States)
2000

European Molecular Biology Laboratory
1994

Chimie ParisTech
1991-1992

Laboratoire de Biodiversité et Biotechnologies Microbiennes
1991

1,3-dialkyl imidazolium salts are one of the most popular and investigated classes room temperature ionic liquids. Although in various cases physical-chemical properties and/or outcome processes these liquids significantly differ from those performed "classical" dipolar organic solvents, they still regarded as merely homogeneous solvents. In this brief overview it is developed concept that pure 1,3-dialkylimidazolium better described hydrogen-bonded polymeric supramolecules type...

10.1590/s0103-50532004000300002 article EN cc-by Journal of the Brazilian Chemical Society 2004-06-01

Abstract Here, we present a 3D localization-based super-resolution technique providing slowly varying localization precision over 1 μm range with precisions down to 15 nm. The axial is performed through combination of point spread function (PSF) shaping and supercritical angle fluorescence (SAF), which yields absolute information. Using dual-view scheme, the detection decoupled from lateral optimized independently provide weakly anisotropic resolution imaging range. This method can be...

10.1038/s41467-019-09901-8 article EN cc-by Nature Communications 2019-04-30

In this paper, we demonstrate the existence of an endogenous mitochondrial azoreductase (AzoR) activity that can induce cleavage N═N double bonds azobenzene compounds under normoxic conditions. To end, 100% OFF-ON azo-based fluorogenic probes derived from 4-amino-1,8-naphthalimide fluorophores were synthesized and evaluated. The in vitro study conducted with other reducing agents cell, including reductases, demonstrated both efficacy selectivity probe for AzoR. Confocal experiments revealed...

10.1021/acs.analchem.3c05030 article EN Analytical Chemistry 2024-01-17

Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine uses a channel to transfer ammonia its glutaminase active site. X-ray structures have been determined at 2.05 Angstroms resolution in presence 2.35 6-diazo-5-oxo-L-norleucine, affinity analog that covalently modifies N-terminal catalytic cysteine, therefore mimicking gamma-glutamyl-thioester intermediate formed during hydrolysis glutamine. The fixation activates enzyme through several major...

10.1074/jbc.m511689200 article EN cc-by Journal of Biological Chemistry 2005-12-10

Glucosamine 6-phosphate synthase converts fructose-6P into glucosamine-6P or glucose-6P depending on the presence absence of glutamine. The isomerase activity is associated with a 40-kDa C-terminal domain, which has already been characterized crystallographically. Now three-dimensional structures complexes reaction product and transition state analog 2-amino-2-deoxyglucitol-6P have determined. Glucose-6P binds in cyclic form whereas an extended conformation. information ligand-protein...

10.1110/ps.8.3.596 article EN Protein Science 1999-01-01

We demonstrate the utility of normal mode analysis in correctly predicting binding modes inhibitors active sites matrix metalloproteinases (MMPs). show accuracy positions MMP‐3 is strongly dependent on which structure used as target, especially when it has been energy minimized. This dependency can be overcome by using intermediate structures generated along one previously calculated for a given target. These results may prime importance further silico drug discovery.

10.1016/j.febslet.2006.08.037 article EN FEBS Letters 2006-09-01

Glutamine:fructose-6-phosphate amidotransferase (Gfat) catalyzes the first and rate-limiting step in hexosamine biosynthetic pathway. The increasing amount of evidence that links excess biosynthesis with pathogenic complications type II diabetes highlights need to understand regulation Gfat. Previous studies showed eukaryotic Gfat is subjected feedback inhibition by UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) phosphorylation cAMP-activated protein kinase A (PKA). In this study, overexpression...

10.1021/bi700694c article EN Biochemistry 2007-10-17

VanX is a zinc-dependent d-Ala-d-Ala amino dipeptidase required for high-level resistance to vancomycin. The enzyme also able process dipeptides with bulky C-terminal acids [Wu, Z., Wright, G. D., and Walsh, C. T. (1995) Biochemistry 34, 2455−2463]. We took advantage of this observation design synthesize the dipeptide-like d-Ala-d-Gly(SΦp-CHF2)-OH (7) as potential mechanism-based inhibitor. VanX-mediated peptide cleavage generates highly reactive 4-thioquinone fluoromethide which covalently...

10.1021/bi001408b article EN Biochemistry 2000-12-01

Ammonia transfer from the glutamine site to fructose-6P of bacterial glucosamine-6-phosphate synthase was studied by molecular dynamics simulations. The studies suggest a key role for Trp74, in sealing hydrophobic channel connecting two binding sites, as well Ala602 and Val605 residues, which form narrow passage whose opening/closing constitutes an essential event ammonia transfer. Kinetic analyses corresponding protein mutants confirmed our predictions. efficiency close zero W74A mutant...

10.1016/j.febslet.2007.05.068 article EN FEBS Letters 2007-06-04

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTCharacterization of a Phosphoglucose Isomerase-like Activity Associated with the Carboxy-Terminal Domain Escherichia coli Glucosamine-6-phosphate SynthaseCaroline Leriche, Marie-Ange Badet-Denisot, and Bernard BadetView Author Information Institut de Chimie des Substances NaturellesCNRS, 91198 Gif-sur-Yvette Cedex, FranceCite this: J. Am. Chem. Soc. 1996, 118, 7, 1797–1798Publication Date (Web):February 21, 1996Publication History Received27...

10.1021/ja953614q article EN Journal of the American Chemical Society 1996-01-01
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