Sandrine Magnard

ORCID: 0000-0003-1195-1840
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Drug Transport and Resistance Mechanisms
  • Lipid Membrane Structure and Behavior
  • DNA and Nucleic Acid Chemistry
  • Protein Interaction Studies and Fluorescence Analysis
  • Chemical Synthesis and Analysis
  • Receptor Mechanisms and Signaling
  • Monoclonal and Polyclonal Antibodies Research
  • Drug-Induced Hepatotoxicity and Protection
  • Bioactive Compounds and Antitumor Agents
  • Caveolin-1 and cellular processes
  • Glycosylation and Glycoproteins Research
  • Mass Spectrometry Techniques and Applications
  • Microfluidic and Bio-sensing Technologies
  • Antifungal resistance and susceptibility
  • Pneumocystis jirovecii pneumonia detection and treatment
  • Nanoparticle-Based Drug Delivery
  • Cancer therapeutics and mechanisms
  • Microfluidic and Capillary Electrophoresis Applications
  • Neonatal Health and Biochemistry
  • Metabolomics and Mass Spectrometry Studies
  • Trace Elements in Health
  • Advanced Proteomics Techniques and Applications
  • HIV/AIDS drug development and treatment
  • Natural Compound Pharmacology Studies
  • Pharmacological Effects and Toxicity Studies

Centre National de la Recherche Scientifique
2010-2025

Université Claude Bernard Lyon 1
2010-2025

Institut de Biologie et de Chimie des Protéines
2011-2022

Laboratoire de Biochimie
2021-2022

Institut de Pharmacologie Moléculaire et Cellulaire
2022

Université Côte d'Azur
2022

Structural and Molecular Basis of Infectious Systems
2014

Multidrug ABC transporters translocate drugs across membranes by a mechanism for which the molecular features of drug release are so far unknown. Here, we resolved three ATP-Mg2+-bound outward-facing conformations Bacillus subtilis (homodimeric) BmrA x-ray crystallography and single-particle cryo-electron microscopy (EM) in detergent solution, one them with rhodamine 6G (R6G), substrate exported when overexpressed B. subtilis. Two R6G molecules bind to drug-binding cavity at level outer...

10.1126/sciadv.abg9215 article EN cc-by-nc Science Advances 2022-01-26

Abstract Most membrane proteins studies require the use of detergents, but because lack a general, accurate and rapid method to quantify them, many uncertainties remain that hamper proper functional structural data analyses. To solve this problem, we propose based on matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS) allows quantification pure or mixed detergents in complex with proteins. We validated wide variety automated process, thereby allowing routine for...

10.1038/srep41751 article EN cc-by Scientific Reports 2017-02-08

Multidrug ABC transporters harness the energy of ATP binding and hydrolysis to translocate substrates out cell detoxify them. While this involves a well-accepted alternating access mechanism, molecular details interplay are still elusive. Rhodamine6G on catalytic inactive mutant homodimeric multidrug transporter BmrA triggers cooperative two identical nucleotide-binding-sites, otherwise michaelian. Here, we investigate asymmetric behavior via structural-enzymology approach, solving cryoEM...

10.1038/s41467-025-56849-z article EN cc-by Nature Communications 2025-02-18

Abstract Multidrug‐resistance protein 1 (MRP1) belongs to the ATP‐binding cassette (ABC) transporter family. MRP1 mediates MDR (multidrug resistance) by causing drug efflux either conjugation glutathione (GSH) or co‐transport with free GSH (without covalent bonding between and GSH). We recently reported that calcium channel blocker verapamil can activate massive in MRP1‐overexpressing cells, leading cell death through apoptosis. However, clinical use of is hampered its cardiotoxicity. Then,...

10.1002/cmdc.201100102 article EN ChemMedChem 2011-06-01

To tackle the problems associated with membrane protein (MP) instability in detergent solutions, we designed a series of glycosyl-substituted dicarboxylate detergents (DCODs) which optimized polar head to clamp domain by including, on one side, two carboxyl groups that form salt bridges basic residues abundant at membrane-cytoplasm interface MPs and, other sugar hydrogen bonds. Upon extraction, DCODs 8 b, c, and 9 b preserved ATPase function BmrA, an ATP-binding cassette pump, much more...

10.1002/anie.201713395 article EN Angewandte Chemie International Edition 2018-01-29

The tri-carboxylatomethylene-mono-alkoxy calix[4]arenes have been shown by fluorescence spectroscopy to bind the NBD1 domain of MRP1 protein in a magnesium dependent manner. observed associations constants are same order as that for ATP–Mg, natural substrate this protein.

10.1039/c0nj00323a article EN New Journal of Chemistry 2010-01-01

Abstract To tackle the problems associated with membrane protein (MP) instability in detergent solutions, we designed a series of glycosyl‐substituted dicarboxylate detergents (DCODs) which optimized polar head to clamp domain by including, on one side, two carboxyl groups that form salt bridges basic residues abundant at membrane–cytoplasm interface MPs and, other sugar hydrogen bonds. Upon extraction, DCODs 8 b , c and 9 preserved ATPase function BmrA, an ATP‐binding cassette pump, much...

10.1002/ange.201713395 article EN Angewandte Chemie 2018-01-29

Abstract Multidrug ABC transporters translocate drugs across membranes by a mechanism for which the molecular features of drug release are so far unknown. Here, we resolved two ATP-Mg 2+ -bound outward-facing (OF) conformations Bacillus subtilis (homodimeric) BmrA, one X-ray crystallography without drug, and another single-particle cryo-EM with rhodamine 6G (R6G). Two R6G molecules bind to drug-binding cavity at level outer leaflet, between transmembrane (TM) helices 1-2 monomer TM5’-6’...

10.1101/2021.03.12.435132 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-03-12

Abstract Multidrug ABC transporters harness the energy of ATP binding and hydrolysis to change conformation thereby translocate substrates out cell detoxify them. While this general access mechanism scheme is well accepted, molecular details interplay still elusive. Rhodamine6G on a catalytic mutant homodimeric multidrug transporter BmrA triggers cooperative two identical nucleotide-binding-sites, otherwise Michaelian. We investigated asymmetric behavior via structural-enzymology approach,...

10.1101/2024.03.15.585201 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-03-15
Coming Soon ...