A. Dupuis

发表

Transduction of the Scorpion Toxin Maurocalcine into Cells

J. Platel, D. Grunwald, M. Ronjat, 2005, Journal of Biological Chemistry.

Inhibition of H+-transporting ATPase by formation of a tight nucleoside diphosphate-fluoroaluminate complex at the catalytic site.

J. Garin, J. Issartel, J. Lunardi, 1988, Proceedings of the National Academy of Sciences of the United States of America.

NADH:ubiquinone oxidoreductase from bovine mitochondria. cDNA sequence of a 19 kDa cysteine-rich subunit.

J. Walker, J. Skehel, A. Dupuis, 1991, The Biochemical journal.

Biotinylated CdSe/ZnSe nanocrystals for specific fluorescent labeling

T. Livache, A. Roget, P. Reiss, 2004 .

Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus.

J. Lunardi, J. Issartel, M. Chevallet, 2003, Biochimica et biophysica acta.

The nuoM arg368his mutation in NADH:ubiquinone oxidoreductase from Rhodobacter capsulatus: a model for the human nd4-11778 mtDNA mutation associated with Leber's hereditary optic neuropathy.

J. Lunardi, J. Issartel, E. Darrouzet, 1998, Biochimica et biophysica acta.

Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH–ubiquinone oxidoreductase

J. Lunardi, M. Chevallet, S. Albracht, 1998, Molecular microbiology.

The NuoI subunit of the Rhodobacter capsulatus respiratory Complex I (equivalent to the bovine TYKY subunit) is required for proper assembly of the membraneous and peripheral domains of the enzyme.

J. Lunardi, J. Issartel, M. Chevallet, 1997, European journal of biochemistry.

Immuno‐purification of a dimeric subcomplex of the respiratory NAHD‐CoQ reductase of Rhodobacter capsulatus equivalent to the FP fraction of the mitochondrial complex I

A. Chapel, J. Lunardi, S. Kieffer, 1997, FEBS letters.

Cavbeta-subunit displacement is a key step to induce the reluctant state of P/Q calcium channels by direct G protein regulation.

D. Grunwald, M. Ronjat, X. Altafaj, 2004, Proceedings of the National Academy of Sciences of the United States of America.

[70] Modifiers of F1-ATPases and associated peptides

J. Lunardi, G. Klein, M. Satre, 1986 .

Photolabeling of the phosphate binding site of mitochondrial F1-ATPase by [32P]azidonitrophenyl phosphate. Identification of the photolabeled amino acid residues.

J. Garin, J. Lunardi, J. Issartel, 1989, Biochemistry.

The complex I from Rhodobacter capsulatus.

J. Lunardi, J. Issartel, M. Chevallet, 1998, Biochimica et biophysica acta.

Toward a Characterization of the Connecting Module of Complex I

J. Lunardi, A. Dupuis, I. Prieur, 2001, Journal of bioenergetics and biomembranes.

Genetic disruption of the respiratory NADH-ubiquinone reductase of Rhodobacter capsulatus leads to an unexpected photosynthesis-negative phenotype

J. Lunardi, E. Darrouzet, A. Dupuis, 1997 .

Interactions between the oligomycin sensitivity conferring protein (OSCP) and beef heart mitochondrial F1-ATPase. 2. Identification of the interacting F1 subunits by cross-linking.

J. Issartel, J. Lunardi, P. Vignais, 1985, Biochemistry.

Interactions between the oligomycin sensitivity conferring protein (OSCP) and beef heart mitochondrial F1-ATPase. 1. Study of the binding parameters with a chemically radiolabeled OSCP.

J. Lunardi, M. Satre, J. Issartel, 1985, Biochemistry.

A kinetic and binding study of the reactivity of Escherichia coli ATPase to N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline.

M. Satre, P. Vignais, M. Bof, 1983, Biochemical and biophysical research communications.

Fluoride, beryllium and ADP combine as a ternary complex in aqueous solution as revealed by a multinuclear NMR study

J. Issartel, J. Girardet, A. Dupuis, 2004, European Biophysics Journal.

Identification of the subunits of F1F0-ATPase from bovine heart mitochondria.

J. Walker, M. Runswick, A. Dupuis, 1991, Biochemistry.

Direct identification of the fluoroaluminate and fluoroberyllate species responsible for inhibition of the mitochondrial F1‐ATPase

J. Issartel, P. Vignais, A. Dupuis, 1989 .

Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction.

J. Walker, M. Finel, M. Runswick, 1992, Journal of molecular biology.

Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I.

J. Lunardi, A. Dupuis, I. Prieur, 2001, Biochimica et biophysica acta.

Early Expression of Sodium Channel Transcripts and Sodium Current by Cajal-Retzius Cells in the Preplate of the Embryonic Mouse Neocortex

W. Moody, J. Platel, M. Albrieux, 2004, The Journal of Neuroscience.

Synchrony of spontaneous calcium activity in mouse neocortex before synaptogenesis

J. Platel, M. Albrieux, J. Brocard, 2007, The European journal of neuroscience.

A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes.

J. Walker, J. Skehel, A. Dupuis, 1991, Biochemistry.

Interaction between the oligomycin sensitivity conferring protein and the F0 sector of the mitochondrial adenosinetriphosphatase complex: cooperative effect of the F1 sector.

P. Vignais, A. Dupuis, 1987, Biochemistry.

Photolabeling of mitochondrial F1-ATPase by an azido derivative of the oligomycin-sensitivity conferring protein.

P. Vignais, A. Dupuis, 1985, Biochemical and biophysical research communications.

Titration of the binding sites for the oligomycin‐sensitivity conferring protein in beef heart submitochondrial particles

M. Satre, P. Vignais, A. Dupuis, 1983, FEBS Letters.

Spectral properties of fluorescent derivatives of the oligomycin sensitivity conferring protein and analysis of their interaction with the F1 and F0 sectors of the mitochondrial ATPase complex.

J. Duszyński, P. Vignais, A. Dupuis, 1988, Biochemistry.

Optical properties and small-angle neutron scattering of bovine heart mitochondrial oligomycin sensitivity conferring protein.

G. Zaccai, M. Satre, A. Dupuis, 1983, Biochemistry.

Na+ channel-mediated Ca2+ entry leads to glutamate secretion in mouse neocortical preplate.

J. Platel, M. Savasta, A. Poupard, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Identification of two genes of Rhodobacter capsulatus coding for proteins homologous to the ND1 and 23 kDa subunits of the mitochondrial Complex I

A. Dupuis, 1992, FEBS letters.

The 49‐kDa subunit of NADH‐ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone‐related inhibitors

J. Lunardi, J. Issartel, E. Darrouzet, 1998, FEBS letters.

The ATP synthase (F0−F1) complex in oxidative phosphorylation

J. Garin, J. Lunardi, J. Issartel, 1992, Experientia.

Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymatic mechanism of the mitochondrial F1-ATPase.

J. Issartel, J. Lunardi, P. Vignais, 1991, Biochemistry.

Exploration of δ‐subunit interactions in beef heart mitochondrial F1 ‐ATPase by monoclonal antibodies

J. Grassi, J. Lunardi, Y. Frobert, 1989, FEBS letters.

Fluoroaluminum and Fluoroberyllium Complexes as Probes of the Catalytic Sites of Mitochondrial F1-ATPase

J. Garin, J. Lunardi, J. Issartel, 1992 .

Identification of five Rhodobacter capsulatus genes encoding the equivalent of ND subunits of the mitochondrial NADH-ubiquinone oxidoreductase.

V. Procaccio, J. Lunardi, J. Issartel, 1995, Gene.