يعرض 51 - 60 نتائج من 106 نتيجة بحث عن '"Nicola Salvi"', وقت الاستعلام: 1.82s تنقيح النتائج
  1. 51
    Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly

    المؤلفون: Nicola Salvi, Damien Maurin, Martin Blackledge, Serafima Guseva, Jean-Philippe Kleman, Rob W. H. Ruigrok, Sigrid Milles, Malene Ringkjøbing Jensen

    المساهمون: Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

    المصدر: Science Advances
    Science Advances, American Association for the Advancement of Science (AAAS), 2020, 6 (14), pp.eaaz7095. ⟨10.1126/sciadv.aaz7095⟩
    Science Advances, 2020, 6 (14), pp.eaaz7095. ⟨10.1126/sciadv.aaz7095⟩

    مصطلحات موضوعية: endocrine system, Magnetic Resonance Spectroscopy, viruses, Plasma protein binding, Virus Replication, law.invention, Measles virus, 03 medical and health sciences, Viral Proteins, law, Virology, Organelle, Protein Interaction Domains and Motifs, Health and Medicine, Nucleocapsid, Research Articles, Cellular compartment, 030304 developmental biology, 0303 health sciences, Multidisciplinary, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Virus Assembly, fungi, 030302 biochemistry & molecular biology, technology, industry, and agriculture, food and beverages, SciAdv r-articles, RNA, biology.organism_classification, Phosphoproteins, eye diseases, Recombinant Proteins, 3. Good health, Cell biology, Nucleoprotein, Nucleoproteins, Viral replication, Recombinant DNA, RNA, Viral, Thermodynamics, Research Article, Measles, Protein Binding

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ed0324a36f7cd7ce3265a8c7436a23f

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  2. 52
    A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy

    المؤلفون: Anton Abyzov, Christophe Moreau, Nicola Salvi, Martin Blackledge, Wiktor Adamski, Malene Ringkjøbing Jensen, Justine Magnat, Damien Maurin, Sigrid Milles

    المساهمون: Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

    المصدر: Journal of the American Chemical Society
    Journal of the American Chemical Society, American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩
    Journal of the American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩

    مصطلحات موضوعية: MAP Kinase Kinase 4, Protein Conformation, 010402 general chemistry, Intrinsically disordered proteins, 01 natural sciences, Biochemistry, Sendai virus, Catalysis, Viral Proteins, Xenopus laevis, Colloid and Surface Chemistry, Protein structure, Protein Domains, Animals, Spectroscopy, Nuclear Magnetic Resonance, Biomolecular, chemistry.chemical_classification, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Nitrogen Isotopes, Biomolecule, Protein dynamics, Relaxation (NMR), General Chemistry, Nuclear magnetic resonance spectroscopy, 0104 chemical sciences, Intrinsically Disordered Proteins, Range (mathematics), Nucleoproteins, chemistry, Chemical physics, Oocytes

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c0930daaf7bd0412b788aeebc03fde
    https://pubmed.ncbi.nlm.nih.gov/31591893

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  3. 53
    Solvent-dependent segmental dynamics in intrinsically disordered proteins

    المؤلفون: Anton Abyzov, Martin Blackledge, Nicola Salvi

    المساهمون: Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-18-CE29-0003,NANO-DISPRO,Une méthode intégrative pour déterminer les mouvements nanométriques des protéines désordonnées(2018)

    المصدر: Science Advances
    Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (6), pp.eaax2348. ⟨10.1126/sciadv.aax2348⟩
    Science Advances, 2019, 5 (6), pp.eaax2348. ⟨10.1126/sciadv.aax2348⟩

    مصطلحات موضوعية: inorganic chemicals, Biophysics, Molecular Dynamics Simulation, 010402 general chemistry, Intrinsically disordered proteins, 01 natural sciences, complex mixtures, 03 medical and health sciences, Molecular dynamics, Water model, Nuclear Magnetic Resonance, Biomolecular, Research Articles, 030304 developmental biology, Physics, 0303 health sciences, Multidisciplinary, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Hydrogen bond, Dynamics (mechanics), Relaxation (NMR), fungi, Temperature, Water, SciAdv r-articles, Hydrogen Bonding, equipment and supplies, 0104 chemical sciences, Intrinsically Disordered Proteins, Solvent, Coupling (physics), Chemistry, Chemical physics, Solvents, bacteria, Research Article

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53bcf35fc5b1fef495c97bb7f26848c9
    http://europepmc.org/articles/PMC6598773

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  4. 54
    Contributors

    المؤلفون: Martin Blackledge, Nicolas Bolik-Coulon, Guillaume Bouvignies, Ludovic Carlier, Charles W. Christoffer, Hoi Sung Chung, A. Keith Dunker, Santiago Esteban-Martin, Fabien Ferrage, Gustavo Fuertes, Alex S. Holehouse, Malene Ringkjøbing Jensen, Daisuke Kihara, Lukasz Kurgan, Laura Nevola, Christopher J. Oldfield, Nicola Salvi, Robert Schneider, Vladimir N. Uversky, Wenwei Zheng

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::cbb4732be20e3399762826abf9a04c5e
    https://doi.org/10.1016/b978-0-12-816348-1.09992-0

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  5. 55
    Intrinsically Disordered Proteins

    المؤلفون: Nicola Salvi

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::6d2975f5c95f45fad5b1e0903f1d8a33
    https://doi.org/10.1016/c2018-0-00038-9

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  6. 56
    Preface

    المؤلفون: Nicola Salvi

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::fb3b10b8af3a2ab0d1195ea67747fba7
    https://doi.org/10.1016/b978-0-12-816348-1.09988-9

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  7. 57
    Conclusion and future directions

    المؤلفون: Nicola Salvi

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::3051a60200299e1b5cde0c08ded9c043
    https://doi.org/10.1016/b978-0-12-816348-1.00010-7

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  8. 58
    Applications of Hyperpolarisation and NMR Long-Lived States in Drug Screening

    المؤلفون: Nicola Salvi

    مصطلحات موضوعية: Spin states, Drug development, Chemical physics, Drug discovery, Dynamic nuclear polarisation

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::cf554d298fd60c096d04ab8668816b86
    https://doi.org/10.1016/bs.arnmr.2018.08.002

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  9. 59
    Dedication

    المؤلفون: Nicola Salvi

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::6bd5f4ab1db59196ab7ad78c1827af6a
    https://doi.org/10.1016/b978-0-12-816348-1.09989-0

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  10. 60
    Molecular mechanisms of fibrillation of IDPs

    المؤلفون: Nicola Salvi

    مصطلحات موضوعية: Structural biology, Chemistry, Amyloidosis, mental disorders, medicine, Synuclein, Biophysics, Amyloid fibril, medicine.disease, Intrinsically disordered proteins

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::17fb0e01cb911c461463221cc28c37aa
    https://doi.org/10.1016/b978-0-12-816348-1.00008-9

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