المؤلفون: Alecu Ciorsac, Alain Sanson, Adriana Isvoran, Dana Craciun, Nadège Jamin, Nahuel Perrot, Pierre Nedellec, Veronica Beswick

المصدر: Journal of the Serbian Chemical Society, Vol 79, Iss 2, Pp 133-150 (2014)

مصطلحات موضوعية: lcsh:Chemistry, Caveolin Proteins, disordered regions, lcsh:QD1-999, Chemistry, functional domains, secondary structure, General Chemistry, Bioinformatics, Protein secondary structure, Sequence (medicine)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ea52ca030e03540268423ee62d0bd51
https://doi.org/10.2298/jsc130716100i

المؤلفون: Adriana Isvoran, Veronica Beswick, Nadège Jamin, Pierre Nedellec, Alain Sanson

المساهمون: Système membranaires, photobiologie, stress et détoxication (SMPSD), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université d'Évry-Val-d'Essonne (UEVE), West University of Timișoara [Roumanie] (WUT)

المصدر: Biophysical Journal
Biophysical Journal, 2011, 100 (7), pp.1660-1667. ⟨10.1016/j.bpj.2011.02.002⟩
Biophysical Journal, Biophysical Society, 2011, 100 (7), pp.1660-1667. ⟨10.1016/j.bpj.2011.02.002⟩

مصطلحات موضوعية: Magnetic Resonance Spectroscopy, Saccharomyces cerevisiae Proteins, Time Factors, Proteolipids, Protein subunit, Biophysics, Phosphatidylserines, Molecular Dynamics Simulation, Protein Structure, Secondary, 03 medical and health sciences, chemistry.chemical_compound, Molecular dynamics, POPC, 030304 developmental biology, 0303 health sciences, Chemistry, Bilayer, Cell Membrane, 030302 biochemistry & molecular biology, Membrane, technology, industry, and agriculture, Membrane Proteins, Hydrogen Bonding, Membranes, Artificial, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Proton-Translocating ATPases, Transmembrane domain, Crystallography, Cytoplasm, Helix, Phosphatidylcholines, lipids (amino acids, peptides, and proteins), [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::303eb67ff76405d41f78deb7f9f69a81
https://doi.org/10.1016/j.bpj.2011.02.002

المؤلفون: Tam Huynh-Dinh, Jean Michel Neumann, Françoise Baleux, François Macquaire, Alain Sanson

المصدر: International Journal of Peptide and Protein Research. 39:117-122

مصطلحات موضوعية: chemistry.chemical_classification, Magnetic Resonance Spectroscopy, Protein Conformation, Stereochemistry, Chemistry, Calcium-Binding Proteins, Molecular Sequence Data, Temperature, Pulse sequence, Peptide, Nuclear magnetic resonance spectroscopy, Nuclear Overhauser effect, Biochemistry, Consensus sequence, Proton NMR, Amino Acid Sequence, Peptides, Peptide sequence, Two-dimensional nuclear magnetic resonance spectroscopy

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acaccb24e50ff4f1affe88009e84504c
https://doi.org/10.1111/j.1399-3011.1992.tb00780.x

المؤلفون: Sandra Pouvelle-Moratille, Hanne Gahery-Segard, André Ménez, Jean-Gérard Guillet, Céline Nonn, Cécile Buhot, Bertrand Georges, Bernard Maillere, Alain Sanson, Florence Castelli, Hassane M. Zarour

المصدر: The Journal of Immunology. 169:6928-6934

مصطلحات موضوعية: Models, Molecular, HLA-DP Antigens, Amino Acid Motifs, Molecular Sequence Data, Immunology, Peptide binding, Peptide, Sequence alignment, Human leukocyte antigen, Biology, Epitope, Cell Line, Epitopes, Gene Frequency, Humans, Immunology and Allergy, Amino Acid Sequence, Peptide sequence, HLA-DP beta-Chains, Genetics, chemistry.chemical_classification, Polymorphism, Genetic, HLA-DP Antigen, Histocompatibility Testing, Ligand binding assay, Amino Acid Substitution, chemistry, Mutation, Peptides, Sequence Alignment, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c19c8ee81b0306c348883a8a0dd85eea
https://doi.org/10.4049/jimmunol.169.12.6928

المؤلفون: Jean-Michel Neumann, Nadège Jamin, Alain Sanson, Céline Landon, Yves-Marie Coïc, Françoise Baleux, Ludmila Ovtracht

المساهمون: Service de Biophysique des Fonctions Membranaires, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Chimie Organique, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

المصدر: FEBS Letters
FEBS Letters, 2002, 529 (2-3), pp.256-60. ⟨10.1016/S0014-5793(02)03353-7⟩
FEBS Letters, Wiley, 2002, 529 (2-3), pp.256-60. ⟨10.1016/S0014-5793(02)03353-7⟩

مصطلحات موضوعية: Models, Molecular, Prions, Protein Conformation, [SDV]Life Sciences [q-bio], Molecular Sequence Data, 030303 biophysics, Biophysics, Beta sheet, Scrapie, Fibril, Biochemistry, Mice, 03 medical and health sciences, Protein structure, Structural Biology, Spectroscopy, Fourier Transform Infrared, Electron microscopy, Genetics, Animals, Amino Acid Sequence, Prion protein, Infrared spectroscopy, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Peptide sequence, 030304 developmental biology, Aggregate, 0303 health sciences, Chemistry, Cell Biology, Microscopy, Electron, Structural propensity, Domain (ring theory), Helix, Prion

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0377603cb1199c43eac4d22b3b934b0
https://doi.org/10.1016/s0014-5793(02)03353-7

المؤلفون: Jeremy C. Smith, Alain Sanson, Tru Huynh

المصدر: ResearcherID

مصطلحات موضوعية: Models, Molecular, Protein Folding, Magnetic Resonance Spectroscopy, Time Factors, Protein Conformation, Molecular Sequence Data, Biophysics, Biophysical Phenomena, Protein Structure, Secondary, Molecular dynamics, Nuclear magnetic resonance, Protein structure, Native state, Intermediate state, Computer Simulation, Amino Acid Sequence, Annexin A1, Quantitative Biology::Biomolecules, Chemistry, Relaxation (NMR), Water, Protein Structure, Tertiary, Unfolded protein response, Radius of gyration, Protein folding, Software, Research Article, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af7de8b447fa229eb8e05d9290199bbf
https://doi.org/10.1016/s0006-3495(02)75200-4

المؤلفون: Pierre Montaville, Jean-Michel Neumann, Alain Sanson, Françoise Ochsenbein, Françoise Russo-Marie

المصدر: Journal of Biological Chemistry. 277:24684-24693

مصطلحات موضوعية: Models, Molecular, DNA, Complementary, Annexins, Protein Conformation, Recombinant Fusion Proteins, Molecular Sequence Data, Phosphatidylserines, Computational biology, Biology, Biochemistry, Protein Structure, Secondary, Conserved sequence, chemistry.chemical_compound, Protein structure, Consensus Sequence, Consensus sequence, Amino Acid Sequence, Binding site, Molecular Biology, Peptide sequence, Annexin A2, Conserved Sequence, Genetics, Binding Sites, Mutagenesis, Cell Biology, Surface Plasmon Resonance, Amino Acid Substitution, chemistry, Mutagenesis, Site-Directed, Calcium, DNA

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e618ba5c3a029d4c3354c2808dad6d13
https://doi.org/10.1074/jbc.m109595200

المؤلفون: Alain Sanson, Gabriel Musat, Tru Huynh, Jean-Michel Neumann, Jeremy C. Smith

المصدر: Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta). 101:82-86

مصطلحات موضوعية: Chemistry, Relaxation (NMR), Electrostatics, symbols.namesake, Crystallography, Molecular dynamics, Structural stability, Chemical physics, Domain (ring theory), Atom, symbols, Molecule, Physical and Theoretical Chemistry, van der Waals force

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::583838818731284d10990a5f4159910d
https://doi.org/10.1007/s002140050411

المؤلفون: Tam Huynh-Dinh, Yves-Marie Coïc, Alain Sanson, Jean-Pierre Noël, Françoise Cordier-Ochsenbein, Raphael Guerois, Jean Tostain, Jean-Michel Neumann, Veronica Beswick

المساهمون: Service de Biophysique des Fonctions Membranaires, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Chimie Organique, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Service des Molécules Marquées, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

المصدر: European Biophysics Journal
European Biophysics Journal, 1999, 28 (1), pp.48-58. ⟨10.1007/s002490050182⟩
European Biophysics Journal, Springer Verlag (Germany), 1999, 28 (1), pp.48-58. ⟨10.1007/s002490050182⟩

مصطلحات موضوعية: Magnetic Resonance Spectroscopy, Annexins, Phosphorylcholine, Proteolipids, Lipid Bilayers, Molecular Sequence Data, Molecular Conformation, Biophysics, Peptide, MESH: Amino Acid Sequence, 010402 general chemistry, 01 natural sciences, Micelle, 03 medical and health sciences, chemistry.chemical_compound, Nuclear magnetic resonance, Phosphatidylcholine, Amino Acid Sequence, MESH: Peptide Fragments, MESH: Annexins, 030304 developmental biology, Phosphocholine, chemistry.chemical_classification, MESH: Molecular Conformation, 0303 health sciences, MESH: Molecular Sequence Data, Aggregation number, MESH: Peptides, MESH: Magnetic Resonance Spectroscopy, MESH: Lipid Bilayers, Bilayer, Relaxation (NMR), Electron Spin Resonance Spectroscopy, Temperature, General Medicine, MESH: Phosphatidylcholines, Peptide Fragments, MESH: Temperature, 0104 chemical sciences, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, chemistry, MESH: Phosphorylcholine, Phosphatidylcholines, MESH: Electron Spin Resonance Spectroscopy, Peptides, Two-dimensional nuclear magnetic resonance spectroscopy, MESH: Proteolipids

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ee7d250354a639f3e8199f18b11d358
https://doi.org/10.1007/s002490050182

المؤلفون: Alain Sanson, Jeffrey L. Brodsky, Jean-Michel Neumann, Veronica Beswick, François Képès, Manuel Garrigos

المصدر: Protein Expression and Purification. 13:423-432

مصطلحات موضوعية: Magnetic Resonance Spectroscopy, Saccharomyces cerevisiae Proteins, Protein Conformation, Recombinant Fusion Proteins, Molecular Sequence Data, Saccharomyces cerevisiae, Cleavage (embryo), Micelle, Chromatography, Affinity, Mass Spectrometry, Fungal Proteins, Amino Acid Sequence, Cloning, Molecular, Protein secondary structure, Chromatography, High Pressure Liquid, DNA Primers, Glutathione Transferase, Expression vector, Chromatography, Base Sequence, Chemistry, Membrane Proteins, Membrane Transport Proteins, Biological Transport, Yeast, Membrane, Secretory protein, Membrane protein, Biochemistry, Electrophoresis, Polyacrylamide Gel, SEC Translocation Channels, Biotechnology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9718339525b98a6a230a079188fbb9e6
https://doi.org/10.1006/prep.1998.0915

المؤلفون: Jean-Michel Neumann, Alain Sanson, Françoise Cordier-Ochsenbein, Raphael Guerois, Françoise Russo-Marie

المصدر: Journal of Molecular Biology. 279:1177-1185

مصطلحات موضوعية: Protein Folding, Magnetic Resonance Spectroscopy, Protein Conformation, Chemistry, Phi value analysis, Computational biology, Crystallography, Sequence homology, Structural Biology, Annexin, Docking (molecular), DOCK, Escherichia coli, Protein folding, Annexin i, Molecular Biology, Heteronuclear single quantum coherence spectroscopy, Annexin A1

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda071cf3286ddee5c685c2b59f5e3fe
https://doi.org/10.1006/jmbi.1998.1828

المؤلفون: Alain Sanson, Françoise Baleux, Jean-Michel Neumann, Tam Huynh-Dinh, Raphael Guerois, Pierre-Noël Lirsac, Françoise Russo-Marie, Françoise Cordier-Ochsenbein

المصدر: Journal of Molecular Biology. 279:1163-1175

مصطلحات موضوعية: Protein Folding, education.field_of_study, Magnetic Resonance Spectroscopy, Protein Conformation, Chemistry, Population, Peptide Fragments, Folding (chemistry), Hydrophobic effect, Crystallography, Structural Biology, Helix, Escherichia coli, Protein folding, education, Polytetrafluoroethylene, Molecular Biology, Two-dimensional nuclear magnetic resonance spectroscopy, Protein secondary structure, Micelles, Heteronuclear single quantum coherence spectroscopy, Annexin A1

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::363b034cffdd8baa49bc0b35d96e8794
https://doi.org/10.1006/jmbi.1998.1829

المؤلفون: Rosilio, Alain Sanson, Patrick A. Curmi, Nadège Jamin, Perrot N, Huynh L, Beswick

المساهمون: Structure et activité des biomolécules normales et pathologiques (SABNP), Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Systèmes membranaires, photobiologie, stress et détoxification (SMPSD - UMR 8221), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11), Université d'Évry-Val-d'Essonne (UEVE), Physico-Chimie des Surfaces (UMR 8612), Université Paris Sud Orsay, Maciejak, Olek

المصدر: Langmuir
Langmuir, 2014, 30 (2), pp.564-573. ⟨10.1021/la4043809⟩
Langmuir, American Chemical Society, 2014, 30 (2), pp.564-573. ⟨10.1021/la4043809⟩

مصطلحات موضوعية: Models, Molecular, Surface Properties, 02 engineering and technology, Dihedral angle, Molecular Dynamics Simulation, 01 natural sciences, Force field (chemistry), Molecular dynamics, chemistry.chemical_compound, 0103 physical sciences, Monolayer, Electrochemistry, General Materials Science, POPC, Spectroscopy, 010304 chemical physics, Molecular Structure, Air, Water, Surfaces and Interfaces, 021001 nanoscience & nanotechnology, Condensed Matter Physics, Lateral compression, [INFO.INFO-MO]Computer Science [cs]/Modeling and Simulation, Crystallography, Membrane, chemistry, Phosphorus atom, Phosphatidylcholines, [INFO.INFO-MO] Computer Science [cs]/Modeling and Simulation, 0210 nano-technology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6cd6dfeb4392779b4086a4f8041c873
https://hal-univ-evry.archives-ouvertes.fr/hal-02292647

المؤلفون: Tam Huynh-Dinh, Veronica Beswick, Alain Sanson, Françoise Baleux, François Képès, Jean-Michel Neumann

المصدر: Biochemistry. 35:14717-14724

مصطلحات موضوعية: Models, Molecular, Cytoplasm, Sec61, Magnetic Resonance Spectroscopy, Protein Conformation, Phosphorylcholine, Molecular Sequence Data, Endoplasmic Reticulum, Biochemistry, Dogs, Calnexin, Animals, Humans, Amino Acid Sequence, Protein secondary structure, Micelles, Sequence Homology, Amino Acid, Chemistry, Endoplasmic reticulum, Membrane Proteins, Water, Biological Transport, STIM1, Intracellular Membranes, Protein superfamily, Protein tertiary structure, Solutions, Secretory protein, Biophysics, SEC Translocation Channels

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02a418d330993798801a81d193774e00
https://doi.org/10.1021/bi961710d

المؤلفون: Tam Huynh-Dinh, Raphaël Guerois, Alain Sanson, Alain Chaffotte, Françoise Cordier-Ochsenbein, Jean-Michel Neumann, Françoise Baleux

المصدر: Biochemistry. 35:10347-10357

مصطلحات موضوعية: Protein Folding, Circular dichroism, Magnetic Resonance Spectroscopy, Nitrogen Isotopes, Chemistry, Circular Dichroism, Molecular Sequence Data, Water, Nuclear magnetic resonance spectroscopy, Amides, Biochemistry, Protein Structure, Secondary, Hydrophobic effect, Annexin, Helix, Biophysics, Protein folding, Amino Acid Sequence, Protons, Peptide sequence, Protein secondary structure, Micelles, Annexin A1

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ccca34c578e4f373d60aa080eec7ac7
https://doi.org/10.1021/bi960747v

المؤلفون: Benoit Odaert, Tam Huynh-Dinh, Françoise Baleux, Jean-Michel Neumann, Alain Sanson

المصدر: Biochemistry. 34:12820-12829

مصطلحات موضوعية: chemistry.chemical_classification, Protein Folding, Magnetic Resonance Spectroscopy, Aqueous solution, Protein Conformation, Molecular Sequence Data, Temperature, Peptide, Biochemistry, Crystallography, Annexin Family, Solubility, chemistry, Proton NMR, Humans, Thermodynamics, Amino Acid Sequence, Protons, Annexin i, Alpha helix, Annexin A1

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cae39f80795208856ce215db0f293027
https://doi.org/10.1021/bi00039a043

المؤلفون: Nadège Jamin, Thierry Brotin, Nawal Tassali, Patrick Berthault, Céline Boutin, Yves Boulard, Gaspard Huber, Fatimazohra Lenda, Marie Carrière, Aurore Bogaert-Buchmann, Alain Sanson, Jean-Pierre Dutasta, François Leteurtre, Antoine Stopin, Hervé Desvaux

المساهمون: Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Laboratoire de Chimie - UMR5182 (LC), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-École normale supérieure - Lyon (ENS Lyon)-Institut de Chimie du CNRS (INC), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Système membranaires, photobiologie, stress et détoxication (SMPSD), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), CNR-ISTEC, National Research Council of Italy, Service de Biologie Intégrative et Génétique Moléculaire (SBIGeM), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Centre de résonance magnétique des systèmes biologiques (CRMSB), Centre National de la Recherche Scientifique (CNRS)-Université de Bordeaux (UB), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), National Research Council of Italy | Consiglio Nazionale delle Ricerche (CNR), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS), Institut Rayonnement Matière de Saclay ( IRAMIS ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay, Laboratoire de Chimie - UMR5182 ( LC ), École normale supérieure - Lyon ( ENS Lyon ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] ( IBMM ), Ecole Nationale Supérieure de Chimie de Montpellier ( ENSCM ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Système membranaires, photobiologie, stress et détoxication ( SMPSD ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), Service de Biologie Intégrative et Génétique Moléculaire ( SBIGeM ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Résonance magnétique des systèmes biologiques ( RMSB ), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique ( CNRS ), Service de Chimie Inorganique et Biologique ( SCIB - UMR E3 ), Institut Nanosciences et Cryogénie ( INAC ), Université Grenoble Alpes ( UGA ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Grenoble Alpes ( UGA ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS )

المصدر: Bioorganic and Medicinal Chemistry
Bioorganic and Medicinal Chemistry, Elsevier, 2011, 19 (13), pp.4135-4143. ⟨10.1016/j.bmc.2011.05.002⟩
Bioorganic and Medicinal Chemistry, 2011, 19 (13), pp.4135-4143. ⟨10.1016/j.bmc.2011.05.002⟩
Bioorganic and Medicinal Chemistry, 2011, 19 (13), pp.4135-4143. 〈http://www.sciencedirect.com/science/article/pii/S0968089611003476〉. 〈10.1016/j.bmc.2011.05.002〉

مصطلحات موضوعية: Magnetic Resonance Spectroscopy, Clinical Biochemistry, Pharmaceutical Science, Transferrin receptor, Biosensing Techniques, macromolecular substances, 010402 general chemistry, Endocytosis, 01 natural sciences, Biochemistry, Cryptophane, Cell membrane, Cell Line, Tumor, Drug Discovery, Fluorescence microscope, medicine, Humans, Hyperpolarization (physics), Molecular Biology, chemistry.chemical_classification, 010405 organic chemistry, Organic Chemistry, Transferrin, 0104 chemical sciences, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, medicine.anatomical_structure, chemistry, [ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistry, Biophysics, Xenon Isotopes, Molecular Medicine, Biosensor, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8f6254d9fc83c810ae683f192a9532c
https://hal.archives-ouvertes.fr/hal-01116905

المؤلفون: Alain Sanson, Hocine Madaoui, Stéphane Orlowski, Raphael Guerois, David Y. Haubertin

المصدر: Biophysical journal. 91(7)

مصطلحات موضوعية: Phosphatidylethanolamine, Models, Molecular, Membranes, Bilayer, Escherichia coli Proteins, Phosphatidylethanolamines, Lipid Bilayers, Biophysics, Membrane Proteins, Transporter, Sequence (biology), ATP-binding cassette transporter, Biology, Protein Structure, Tertiary, Transmembrane domain, Molecular dynamics, chemistry.chemical_compound, Biochemistry, chemistry, Bacteriocins, ATP-Binding Cassette Transporters, Computer Simulation, Hinge region, Porosity

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b1c3df04a8561770a27c2fe30bdaef0
https://pubmed.ncbi.nlm.nih.gov/16782794

المؤلفون: Milan Hodošček, Alain Sanson, Franci Merzel, Dusanka Janezic

المصدر: Journal of computational chemistry. 27(4)

مصطلحات موضوعية: Models, Molecular, Chemical Phenomena, Surface Properties, chemistry.chemical_element, Phosphatidylserines, Calcium, Molecular physics, Force field (chemistry), Molecular dynamics, Annexin, Computer Simulation, Binding site, Annexin A5, Quantum, Binding Sites, Chemistry, Physical, Cell Membrane, Water, General Chemistry, Computational Mathematics, Membrane, chemistry, Potential energy surface, Quantum Theory, Atomic physics, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2265b634e8b93e05ec2b71d19466ab9a
https://pubmed.ncbi.nlm.nih.gov/16419147

المؤلفون: Alain Sanson, F. Briki, Yves-Marie Coïc, Nadège Jamin, Vincent Croixmarie, Jean Baptiste Doucet, Gabriel David, Ludmila Ovtracht

المساهمون: Direction des Applications Militaires (DAM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Physique des Solides (LPS), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Chimie Organique, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Service de Biophysique des Fonctions Membranaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)

المصدر: Journal of Structural Biology
Journal of Structural Biology, 2005, 150 (3), pp.284-99. ⟨10.1016/j.jsb.2005.03.003⟩
Journal of Structural Biology, Elsevier, 2005, 150 (3), pp.284-99. ⟨10.1016/j.jsb.2005.03.003⟩

مصطلحات موضوعية: Models, Molecular, Magnetic Resonance Spectroscopy, Time Factors, Protein Conformation, DNA Mutational Analysis, Beta sheet, MESH: Protein Structure, Secondary, MESH: Amino Acid Sequence, MESH: Amyloid beta-Protein, Protein Structure, Secondary, Molecular dynamics, Mice, 0302 clinical medicine, Protein structure, MESH: Protein Conformation, X-Ray Diffraction, Structural Biology, Spectroscopy, Fourier Transform Infrared, MESH: Animals, MESH: DNA Mutational Analysis, 0303 health sciences, Chemistry, MESH: Peptides, MESH: X-Ray Diffraction, MESH: Microscopy, Electron, Transmission, MESH: Models, Molecular, Amyloid, Prions, Ribbon diagram, Molecular Sequence Data, MESH: Microscopy, Electron, Fibril, MESH: Spectroscopy, Fourier Transform Infrared, Turn (biochemistry), 03 medical and health sciences, MESH: Software, MESH: Prions, Microscopy, Electron, Transmission, Cylinder, Animals, Amino Acid Sequence, MESH: Mice, 030304 developmental biology, MESH: Amyloid, MESH: Molecular Sequence Data, Amyloid beta-Peptides, MESH: Magnetic Resonance Spectroscopy, MESH: Time Factors, Crystallography, Microscopy, Electron, Peptides, 030217 neurology & neurosurgery, Alpha helix, Software

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28bbb99beacbd4b5ddba7265d8192575
https://pubmed.ncbi.nlm.nih.gov/15890277