Výsledky vyhledávání - "Florent Guillain"

CadA, the Cd2+-ATPase from Listeria monocytogenes, can use Cd2+ as co-substrate

Autor: Florent Guillain, Elisabeth Mintz, Patrice Catty, Chen Chou Wu, Aurélie Gardarin

Publikováno v: Biochimie
Biochimie, Elsevier, 2006, 88 (11), pp.1687-92. ⟨10.1016/j.biochi.2006.06.013⟩
Biochimie, 2006, 88 (11), pp.1687-92. ⟨10.1016/j.biochi.2006.06.013⟩

International audience; CadA is a membrane protein of the P-type ATPase family which is the major determinant of the resistance to Cd2+ in Listeria monocytogenes. During its catalytic cycle, CadA undergoes auto-phosphorylation from ATP at Asp398, whi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9d7fa67dc9da50b92d9ecbe6d340376
https://doi.org/10.1016/j.biochi.2006.06.013

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Membrane Protein Insertion Regulated by Bringing Electrostatic and Hydrophobic Interactions into Play

Autor: Vincent Forge, Philippe Savarin, Alexandre Chenal, Florent Guillain, Philippe Nizard, Daniel Gillet

Publikováno v: Journal of Biological Chemistry. 277:43425-43432

The study of the membrane insertion of the translocation domain of diphtheria toxin deepens our insight into the interactions between proteins and membranes. During cell intoxication, this domain undergoes a change from a soluble and folded state at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ee2cea40bdfb86744825216f783a373
https://doi.org/10.1074/jbc.m204148200

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Purification of Heterologous Sarcoplasmic Reticulum Ca2+-ATPase Serca1a Allowing Phosphoenzyme and Ca2+-Affinity Measurements

Autor: Roger Miras, Martine Cuillel, Patrice Catty, Elisabeth Mintz, Florent Guillain

Publikováno v: Protein Expression and Purification. 22:299-306

We describe here a protocol to prepare milligrams of active and stable heterologous sarcoplasmic reticulum Ca(2+)-ATPase (Serca1a). Serca1a was tagged with 6 histidines at its C-terminal end and overexpressed using the baculovirus-Sf9 system. In a fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44b31e14d2bff78e20bea0f8d0b66ab7
https://doi.org/10.1006/prep.2001.1436

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Ligand Binding to Macromolecules or Micelles: Use of Centrifugal Ultrafiltration to Measure Low-Affinity Binding

Autor: Marc le Maire, Philippe Champeil, Stéphane Chenevois, Thierry Menguy, Florent Guillain, Pierre Falson

Publikováno v: Analytical Biochemistry
Analytical Biochemistry, Elsevier Masson, 1998, 264, pp.141-148

International audience; We describe a method for estimating ligand binding to a macromolecular sample under conditions where this binding is of low affinity and must be measured under equilibrium conditions, without removal of the unbound ligand. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a70fcb800c62169ec9b9e4a4a6c4c95
https://doi.org/10.1006/abio.1998.2854

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Ca2+ transport by the sarcoplasmic reticulum ATPase

Autor: Elisabeth Mintz, Florent Guillain

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1318:52-70

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59394473810d5244280e0a4bd07e83b4
https://doi.org/10.1016/s0005-2728(96)00132-6

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Ca2+ Translocation across Sarcoplasmic Reticulum ATPase Randomizes the Two Transported Ions

Autor: Vincent Forge, Elisabeth Mintz, Denis Canet, Florent Guillain

Publikováno v: Journal of Biological Chemistry. 271:20566-20572

Cytoplasmic Ca2+ dissociation is sequential, and the Ca2+ ions bound to the nonphosphorylated ATPase are commonly represented as superimposed on each other, so that the superficial Ca2+ is freely exchangeable from the cytoplasm, whereas the deeper Ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3369cc8f79b8f519752b949efd0e9d15
https://doi.org/10.1074/jbc.271.34.20566

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The Modulation of Ca2+ Binding to Sarcoplasmic Reticulum ATPase by ATP Analogues Is pH-dependent

Autor: Vincent Forge, Maria Passafiume, Ana M. Mata, Elisabeth Mintz, Florent Guillain

Publikováno v: Journal of Biological Chemistry. 270:27160-27164

Excess ATP is known to enhance Ca(2+)-ATPase activity and, among other effects, to accelerate the Ca2+ binding reaction. In previous work, we studied the pH dependence of this reaction and proposed a 3H+/2Ca2+ exchange at the transport sites, in agre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86461b654e8a159d70e51fc6b7f8e59f
https://doi.org/10.1074/jbc.270.45.27160

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How do Ca2+ ions pass through the sarcoplasmic reticulum membrane

Autor: Florent Guillain, Elisabeth Mintz

Publikováno v: Bioscience Reports. 15:377-385

We propose an overview of the mechanism of Ca2+ transport through the sarcoplasmic reticulum membrane via the Ca2+-ATPase. We describe cytoplasmic calcium binding, calcium occlusion in the membrane and lumenal calcium dissociation. A channel-like str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::444b2127a3a23006b4425cb85737c03c
https://doi.org/10.1007/bf01788369

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Ca2+ binding to sarcoplasmic reticulum ATPase revisited. II. Equilibrium and kinetic evidence for a two-route mechanism

Autor: Vincent Forge, Florent Guillain, Elisabeth Mintz

Publikováno v: Journal of Biological Chemistry. 268:10961-10968

The experiments reported in the present paper were designed to check the model proposed for Ca2+ binding in the preceding paper (Forge, V., Mintz, E., and Guillain, F. (1993) J. Biol. Chem. 268, 10953-10960). The pH dependence of the Mg(2+)-induced v

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c07940fa1292df08fa2e3c7bec26b4c
https://doi.org/10.1016/s0021-9258(18)82079-8

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