المؤلفون: Theis Jacobsen, Régine Dazzoni, Melvin G. Renault, Benjamin Bardiaux, Michael Nilges, Vladimir Shevchik, Nadia Izadi-Pruneyre

المساهمون: Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Ecole Doctorale Complexité du Vivant (ED515), Sorbonne Université (SU), Microbiologie, adaptation et pathogénie (MAP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), This work was funded by the Institut Pasteur, the Centre National de la Recherche Scientifique (CNRS), the French Agence Nationale de la Recherche (ANR Synergy-T2SS ANR-19-CE11-0020-01) and European Union’s Horizon 2020 Research and Innovation program under the Marie Sklodowska-Curie Grant Agreement No. 765042. The 800-MHz NMR spectrometer of the Institut Pasteur was partially funded by the Région Ile de France (SESAME 2014 NMRCHR Grant No. 4014526)., ANR-19-CE11-0020,SYNERGY_T2SS,Structure et fonction moléculaire du pseudopilus dans la sécrétion de protéines par lla voiè de type 2(2019), European Project: 765042,H2020-EU.1.3.1. - Fostering new skills by means of excellent initial training of researchers ,ViBrANT(2018)

المصدر: Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2022, 16 (2), pp.231-236. ⟨10.1007/s12104-022-10085-4⟩
Biomol NMR Assign

مصطلحات موضوعية: [SDV]Life Sciences [q-bio], Dickeya dadantii, MESH: Periplasm, Type II secretion system, MESH: Protein Subunits, Biochemistry, MESH: Polymers, MESH: Dickeya, Structural Biology, OutG, NMR resonance assignments, MESH: Nuclear Magnetic Resonance, Biomolecular, MESH: Adenosine Triphosphatases, Pseudopilin, MESH: Protein Binding, MESH: Bacterial Proteins

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::867027f71b3eb1944b9104c37687db36Test
https://hal.science/hal-03836613/documentTest

المؤلفون: Henot, Faustine, Crublet, Elodie, Frech, Matthias, Boisbouvier, Jerome

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), NMR-Bio (NMR-Bio), Discovery Technologies, Region Auvergne-Rhône-Alpes (pack ambition recherche 2019 - P089), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), ANR-15-IDEX-0002,UGA,IDEX UGA(2015)

المصدر: Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2022, 16 (2), pp.257-266. ⟨10.1007/s12104-022-10089-0⟩

مصطلحات موضوعية: Ligands, Biochemistry, Assignment, MESH: Benzamides, Adenosine Triphosphate, Structural Biology, MESH: Adenosine Triphosphate, MESH: Nuclear Magnetic Resonance, Biomolecular, MESH: HSP90 Heat-Shock Proteins, MESH: Ligands, HSP90, MESH: Protein Binding, Humans, HSP90 Heat-Shock Proteins, Furans, Nuclear Magnetic Resonance, Biomolecular, Resorcinol ligand, MESH: Humans, Binding Sites, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Nucleotides, MESH: Furans, Backbone, MESH: Transcription Factors, Resorcinols, NMR, MESH: Nucleotides, MESH: Binding Sites, Benzamides, MESH: Resorcinols, MESH: Molecular Chaperones, Methyl groups, Molecular Chaperones, Protein Binding, Transcription Factors

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44fe49d3f372c7f0f51eba016d955385Test
https://pubmed.ncbi.nlm.nih.gov/35701717Test

المؤلفون: Aldo R. Camacho-Zarco, Vincent Schnapka, Serafima Guseva, Anton Abyzov, Wiktor Adamski, Sigrid Milles, Malene Ringkjøbing Jensen, Lukas Zidek, Nicola Salvi, Martin Blackledge

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), Masaryk University [Brno] (MUNI), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

المصدر: Chemical Reviews
Chemical Reviews, 2022, 122 (10), pp.9331-9356. ⟨10.1021/acs.chemrev.1c01023⟩

مصطلحات موضوعية: MESH: Intrinsically Disordered Proteins, Magnetic Resonance Spectroscopy, MESH: Humans, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Conformation, MESH: Magnetic Resonance Spectroscopy, General Chemistry, Intrinsically Disordered Proteins, MESH: Protein Conformation, MESH: Nuclear Magnetic Resonance, Biomolecular, Humans, Thermodynamics, MESH: Thermodynamics, Nuclear Magnetic Resonance, Biomolecular

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58c5cd62e2c477a544ddcfe4b17fd0b7Test
https://hal.science/hal-03810005/documentTest

المؤلفون: Beate Koksch, Benjamin Bardiaux, Hartmut Oschkinat, Hans von Berlepsch, Anne Diehl, Mônica S. Freitas, Franziska Emmerling, Jork Leiterer, Enrico Brandenburg, Kristin Folmert, Ulla I. M. Gerling-Driessen, Christoph Böttcher, Raheleh Rezaei Araghi, Kevin Pagel

المساهمون: Freie Universität Berlin, Universidade Federal do Rio de Janeiro (UFRJ), Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] (FMP), Leibniz Association, BAM Federal Institute for Materials Research and Testing, Federal Institute for Materials Research and Testing - Bundesanstalt für Materialforschung und -prüfung (BAM), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Alexander von Humboldt Foundation Georg Forster Research Fellowship and by the CAPES-DAAD Bilateral Exchange of Academics (both awarded to M.S.F.), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

المصدر: Journal of Structural Biology
Journal of Structural Biology, 2018, 203 (3), pp.263-272. ⟨10.1016/j.jsb.2018.05.009⟩
Journal of Structural Biology, Elsevier, 2018, 203 (3), pp.263-272. ⟨10.1016/j.jsb.2018.05.009⟩

مصطلحات موضوعية: 0301 basic medicine, Amyloid, Materials science, [SDV]Life Sciences [q-bio], MESH: Protein Structure, Secondary, Amyloidogenic Proteins, Peptide, MESH: Amino Acid Sequence, Microscopy, Atomic Force, 010402 general chemistry, 01 natural sciences, Protein Structure, Secondary, law.invention, 03 medical and health sciences, Protein Domains, Alzheimer Disease, Structural Biology, law, MESH: Nuclear Magnetic Resonance, Biomolecular, Electron microscopy, Humans, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Amyloid fibrils, MESH: Microscopy, Atomic Force, chemistry.chemical_classification, Coiled coil, MESH: Amyloid, MESH: Amyloidogenic Proteins, MESH: Humans, MESH: Peptides, Scattering, Cryoelectron Microscopy, Polymer, 0104 chemical sciences, 030104 developmental biology, chemistry, Transmission electron microscopy, Biophysics, MESH: Protein Domains, Substructure, MESH: Cryoelectron Microscopy, Electron microscope, Peptides, MESH: Alzheimer Disease

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff261ebd7c51a8ee3fc24fe6c1ea3badTest
https://doi.org/10.1016/j.jsb.2018.05.009Test

المؤلفون: Anh Tuân Phan, Khac Huy Ngo, Yves Mechulam, Fernaldo Richtia Winnerdy, Blaž Bakalar, Arijit Maity, Emmanuelle Schmitt, Poulomi Das

المساهمون: Nanyang Technological University [Singapour], Laboratoire de Biologie Structurale de la Cellule (BIOC), École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), School of Physical and Mathematical Sciences, NTU Institute of Structural Biology

المصدر: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (3), pp.1724-1736. ⟨10.1093/nar/gkaa1259⟩

مصطلحات موضوعية: Models, Molecular, MESH: DNA / chemistry, AcademicSubjects/SCI00010, Computational biology, Biology, 010402 general chemistry, Left handedness, G-quadruplex, Crystallography, X-Ray, 01 natural sciences, 03 medical and health sciences, Structural Biology, MESH: Nuclear Magnetic Resonance, Biomolecular, Genetics, Nucleotide Motifs, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, Left handed, 0303 health sciences, Crystallography, Right handed, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: G-Quadruplexes, Biological sciences [Science], DNA, MESH: Crystallography, X-Ray, Solution structure, 0104 chemical sciences, G-Quadruplexes, MESH: Nucleotide Motifs, X-Ray, MESH: Sugars / chemistry, Sugars, MESH: Models, Molecular

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9e7a6d3720da82a2b3318aca29a1a3fTest
https://hal-polytechnique.archives-ouvertes.fr/hal-03188426Test

المؤلفون: Elise Delaforge, Damien Maurin, Sigrid Milles, Nicola Salvi, Martin Blackledge, Stephen Cusack, Darren J. Hart, Malene Ringkjøbing Jensen, Aldo Camacho Zarco, Sissy Kalayil

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), European Molecular Biology Laboratory [Grenoble] (EMBL), HFSP fellowship LT001544/2017, ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), European Project: 796490

المصدر: Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), ⟨10.1038/s41467-020-17407-x⟩
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3656. ⟨10.1038/s41467-020-17407-x⟩
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications, 2020, 11 (1), pp.3656. ⟨10.1038/s41467-020-17407-x⟩

مصطلحات موضوعية: 0301 basic medicine, [SDV]Life Sciences [q-bio], Mutant, General Physics and Astronomy, Virus Replication, medicine.disease_cause, 01 natural sciences, MESH: Avian Proteins, Heterotrimeric G protein, MESH: Nuclear Magnetic Resonance, Biomolecular, Influenza A virus, MESH: Animals, lcsh:Science, Polymerase, 0303 health sciences, Multidisciplinary, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, Chemistry, MESH: Influenza, Human, virus diseases, Nuclear Proteins, RNA-Binding Proteins, 3. Good health, Cell biology, MESH: Birds, MESH: Protein Domains, Host adaptation, MESH: RNA Replicase, Protein Binding, MESH: Mutation, MESH: Influenza A Virus, H5N1 Subtype, Science, Protein subunit, 010402 general chemistry, Intrinsically disordered proteins, Article, Virus, General Biochemistry, Genetics and Molecular Biology, Avian Proteins, Birds, Viral Proteins, 03 medical and health sciences, Protein Domains, Species Specificity, MESH: Influenza in Birds, Influenza, Human, medicine, Animals, Humans, MESH: Protein Binding, MESH: Species Specificity, Binding site, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, MESH: Humans, Influenza A Virus, H5N1 Subtype, MESH: Virus Replication, General Chemistry, RNA-Dependent RNA Polymerase, MESH: Viral Proteins, Influenza A virus subtype H5N1, 0104 chemical sciences, MESH: RNA-Binding Proteins, 030104 developmental biology, Influenza in Birds, Mutation, biology.protein, lcsh:Q, Influenza virus, Solution-state NMR, MESH: Nuclear Proteins

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce095ca25613cf9567243b52a9f08146Test
https://hal.archives-ouvertes.fr/hal-03079958Test

المؤلفون: Pavel Macek, Jonathan P. Waltho, J. Willem M. Nissink, Matthew J. Cliff, Kevin J. Embrey, Rick Davies, Martin Blackledge, Stanislava Panova, Malene Ringkjøbing Jensen

المساهمون: Manchester Institute of Biotechnology - Manchester Centre for Synthetic Biology of Fine and Speciality Chemicals (SYNBIOCHEM), University of Manchester, 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), Oncology, IMED Biotech Unit, AstraZeneca [Cambridge, UK], Discovery Sciences, IMED Biotech Unit, AstraZeneca, Institut de biologie structurale (IBS - UMR 5075 ), 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)

المصدر: Structure
Structure, Elsevier (Cell Press), 2019, 27 (10), pp.1537-1546.e4. ⟨10.1016/j.str.2019.07.006⟩
Panova, S, Cliff, M, Macek, P, Blackledge, M, Jensen, M R, Nissink, J W M, Embrey, K J, Davies, R & Waltho, J 2019, ' Mapping hidden residual structure within the Myc bHLH-LZ domain using chemical denaturant titration ', Structure . https://doi.org/10.1016/j.str.2019.07.006Test
Structure, 2019, 27 (10), pp.1537-1546.e4. ⟨10.1016/j.str.2019.07.006⟩

مصطلحات موضوعية: Guanidinium chloride, Models, Molecular, Protein Denaturation, MESH: Protein Structure, Secondary, MESH: Thiazoles, Myc, Residual, Intrinsically disordered proteins, Protein Structure, Secondary, Proto-Oncogene Proteins c-myc, molten globule, 03 medical and health sciences, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, Structural Biology, Manchester Institute of Biotechnology, MESH: Nuclear Magnetic Resonance, Biomolecular, MESH: Proto-Oncogene Proteins c-myc, Humans, guanidinium chloride, Molecular Biology, Protein secondary structure, Conformational isomerism, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, solution NMR, Solution NMR, 0303 health sciences, Binding Sites, MESH: Humans, paramagnetic relaxation enhancement, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], 030302 biochemistry & molecular biology, Helix-Loop-Helix Motifs, ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology, Molten globule, Protein Structure, Tertiary, Thiazoles, chemistry, MESH: Binding Sites, Biophysics, Titration, MESH: Protein Denaturation, intrinsically disordered proteins, Biological regulation, MESH: Helix-Loop-Helix Motifs, MESH: Models, Molecular

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2279504f4c486d035e0b61eb94e5db50Test
https://hal.univ-grenoble-alpes.fr/hal-03016176/documentTest

المؤلفون: Nina Eleni Christou, Bernhard Brutscher

المساهمون: Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-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), 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)-Centre National de la Recherche Scientifique (CNRS)

المصدر: Journal of Biomolecular NMR
Journal of Biomolecular NMR, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩
Journal of Biomolecular NMR, Springer Verlag, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩

مصطلحات موضوعية: 0301 basic medicine, Longitudinal relaxation enhancement, MESH: Algorithms, 010402 general chemistry, 01 natural sciences, Biochemistry, Signal, MESH: Tyrosine, Histidine tautomerization, 03 medical and health sciences, MESH: Histidine, MESH: Protein Conformation, NMR assignment, MESH: Nuclear Magnetic Resonance, Biomolecular, Side chain, MESH: Proteins, Tyrosine, BEST, Spectroscopy, Histidine, Quantitative Biology::Biomolecules, Spins, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Relaxation (NMR), Resonance, MESH: Carbon Isotopes, 3. Good health, 0104 chemical sciences, Crystallography, 030104 developmental biology, Aromatics, Excitation, MESH: Nitrogen Isotopes

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b7c57f709ae90d2d777a21bd05b950Test
https://hal.science/hal-02085961Test

المؤلفون: Wiktor Koźmiński, Benjamin Bardiaux, Barbara Zambelli, Ryan C. Johnson, Chris A. E. M. Spronk, Priyanka Basak, D. Scott Merrell, Francesco Musiani, Mario Piccioli, Michael J. Maroney, Stefano Ciurli, Michał Górka, Faith C. Blum, Szymon Żerko, Heidi Hu

المساهمون: UAB 'Spronk NMR Consultancy', University of Leicester, University of Warsaw (UW), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), University of Bologna/Università di Bologna, Università degli Studi di Firenze = University of Florence (UniFI), University of Massachusetts [Amherst] (UMass Amherst), University of Massachusetts System (UMASS), Uniformed Services University of the Health Sciences (USUHS), This work was supported by a grant from the Polish National Science Centre (MAESTRO—2015/18/A/ST4/00270 to MG, SZ, WK), by a grant from the U.S. National Institutes of Health (NIH—R01-GM069696 to MJM), by the Institut Pasteur, CNRS and the French Institute of Bioinformatics (IFB, ANR-11-INBS-0013, to BB), by the European Cooperation in Science and Technology (COST) Action 15133 (MP), and by the Department of Pharmacy and Biotechnology of the University of Bologna (SC, BZ, FM)., The NMR experiments were partially obtained in the frames of access to NMR infrastructure by EuroBioNMR EEIG (http://www.eurobionmr.euTest/). The Center for Magnetic Resonance of the University of Florence (CERM) provided access to the high-field NMR spectrometers, and Fabio Calogiuri is acknowledged for spectra data collection., ANR-11-INBS-0013,IFB (ex Renabi-IFB),Institut français de bioinformatique(2011), European Project: COST, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), University of Bologna, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), Spronk, Chris A. E. M., Żerko, Szymon, Górka, Michał, Koźmiński, Wiktor, Bardiaux, Benjamin, Zambelli, Barbara, Musiani, Francesco, Piccioli, Mario, Basak, Priyanka, Blum, Faith C., Johnson, Ryan C., Hu, Heidi, Merrell, D. Scott, Maroney, Michael, Ciurli, Stefano

المصدر: Journal of Biological Inorganic Chemistry
Journal of Biological Inorganic Chemistry, 2018, 23 (8), pp.1309-1330. ⟨10.1007/s00775-018-1616-y⟩
Journal of Biological Inorganic Chemistry, Springer Verlag, 2018, 23 (8), pp.1309-1330. ⟨10.1007/s00775-018-1616-y⟩

مصطلحات موضوعية: Protein Conformation, alpha-Helical, 0301 basic medicine, Molecular dynamic, Computational chemistry, MESH: Hydrogen-Ion Concentration, MESH: Metallochaperones, Metal transport, Metallochaperones, Molecular dynamics, Nickel, Nuclear magnetic resonance, 01 natural sciences, Biochemistry, MESH: Zinc, MESH: Nickel, MESH: Nuclear Magnetic Resonance, Biomolecular, MESH: Molecular Dynamics Simulation, MESH: Bacterial Proteins, Density Functional Theory, biology, Chemistry, MESH: Escherichia coli, [CHIM.ORGA]Chemical Sciences/Organic chemistry, MESH: Models, Chemical, Nuclear magnetic resonance spectroscopy, Hydrogen-Ion Concentration, MESH: Glycine, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Zinc, MESH: Mutagenesis, Site-Directed, visual_art, visual_art.visual_art_medium, MESH: Protein Domains, Protein Binding, MESH: Mutation, Absorption spectroscopy, Glycine, chemistry.chemical_element, Molecular Dynamics Simulation, 010402 general chemistry, Article, Inorganic Chemistry, Metal, 03 medical and health sciences, Bacterial Proteins, Protein Domains, Escherichia coli, MESH: Protein Binding, MESH: Density Functional Theory, Binding site, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Nuclear Magnetic Resonance, Biomolecular, MESH: Protein Conformation, alpha-Helical, Binding Sites, Helicobacter pylori, Chemical shift, Metallochaperone, 0104 chemical sciences, Crystallography, 030104 developmental biology, Models, Chemical, MESH: Binding Sites, Chaperone (protein), Mutation, Mutagenesis, Site-Directed, biology.protein, MESH: Helicobacter pylori

وصف الملف: STAMPA

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daf4128788c96d506cc2d51133bbe116Test
https://hal-pasteur.archives-ouvertes.fr/pasteur-02329962Test

المؤلفون: Lewis E. Kay, Jérôme Boisbouvier

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), Department of Molecular Genetics [Toronto], University of Toronto, Isotopic Labelling PF / Cell-Free PF, 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)

المصدر: Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2018, 71 (3), pp.115-117. ⟨10.1007/s10858-018-0199-9⟩
Journal of Biomolecular NMR, 2018, 71 (3), pp.115-117. ⟨10.1007/s10858-018-0199-9⟩

مصطلحات موضوعية: 0301 basic medicine, MESH: Isotope Labeling, 010402 general chemistry, 01 natural sciences, Biochemistry, Isotopic labeling, 03 medical and health sciences, Nucleic Acids, MESH: Nuclear Magnetic Resonance, Biomolecular, Animals, Humans, MESH: Animals, MESH: Proteins, Nuclear Magnetic Resonance, Biomolecular, Spectroscopy, ComputingMilieux_MISCELLANEOUS, MESH: Humans, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Proteins, MESH: Nucleic Acids, 0104 chemical sciences, 030104 developmental biology, Isotope Labeling, Nucleic acid

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d574f1c91005e584e5c4f321b21d74a9Test
https://hal.archives-ouvertes.fr/hal-01991758Test