المؤلفون: Kapil Gupta, Christine Toelzer, Maia Kavanagh Williamson, Deborah K. Shoemark, A. Sofia F. Oliveira, David A. Matthews, Abdulaziz Almuqrin, Oskar Staufer, Sathish K. N. Yadav, Ufuk Borucu, Frederic Garzoni, Daniel Fitzgerald, Joachim Spatz, Adrian J. Mulholland, Andrew D. Davidson, Christiane Schaffitzel, Imre Berger

المصدر: Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)

مصطلحات موضوعية: Science

وصف الملف: electronic resource

Relation: https://doaj.org/toc/2041-1723

URL الوصول: https://doaj.org/article/aca02d9ce50d4ddb8d2a53b3b352d716

المؤلفون: Christine Toelzer, Kapil Gupta, Sathish K. N. Yadav, Lorna Hodgson, Maia Kavanagh Williamson, Dora Buzas, Ufuk Borucu, Kyle Powers, Richard Stenner, Kate Vasileiou, Frederic Garzoni, Daniel Fitzgerald, Christine Payré, Gunjan Gautam, Gérard Lambeau, Andrew D. Davidson, Paul Verkade, Martin Frank, Imre Berger, Christiane Schaffitzel

المصدر: Toelzer, C, Gupta, K, Yadav Kadapalakere, S, Hodgson, L R, Kavanagh Williamson, M, Buzas, D, Borucu, U, Powers, K T, Stenner, R A, Vasileiou, K, Garzoni, F, Fitzgerald, D J, Payré, C, Gautam, G, Lambeau, G, Davidson, A D, Verkade, P, Martin, F, Berger, I & Berger-Schaffitzel, C H 2022, ' The Free Fatty Acid-Binding Pocket is a Conserved Hallmark in Pathogenic β-Coronavirus Spike Proteins from SARS-CoV to Omicron ', Science Advances, vol. 8, no. 47, eadc9179 . https://doi.org/10.1101/2022.04.22.489083, https://doi.org/10.1126/sciadv.adc9179

مصطلحات موضوعية: Multidisciplinary, SARS-CoV-2, Max Planck Bristol, Spike Glycoprotein, Coronavirus, Bristol BioDesign Institute, Humans, COVID-19, Fatty Acids, Nonesterified

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70f2b78395682ad7de4416f8224a32da
https://doi.org/10.1126/sciadv.adc9179

المؤلفون: Imre Berger, author¹, Frederic Garzoni, author¹, Maxime Chaillet, author¹, Matthias Haffke, author¹, Kapil Gupta, author¹, Alice Aubert, author¹

المصدر: Journal of Visualized Experiments. (77)

الإتاحة: http://www.jove.com/video/50159

المؤلفون: Deborah K. Shoemark, A. Sofia F. Oliveira, Frederic Garzoni, Maia Kavanagh Williamson, Kapil Gupta, Joachim P. Spatz, K.N. Sathish Yadav, Ufuk Borucu, Imre Berger, Andrew D. Davidson, Christine Toelzer, Adrian J. Mulholland, Daniel J. Fitzgerald, David A. Matthews, Abdulaziz Almuqrin, Christiane Schaffitzel, Oskar Staufer

مصطلحات موضوعية: chemistry.chemical_classification, Genetics, Infectivity, Cell type, biology, viruses, Allosteric regulation, RNA, chemistry, biology.protein, Glycoprotein, Furin, Tropism, Function (biology)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::986607fc6ad12c797c4d989da7970a1b
https://doi.org/10.1101/2021.05.11.443384

المؤلفون: Daniel J. Fitzgerald, Frederic Garzoni, Christiane Schaffitzel, Duygu Sari-Ak, Kapil Gupta, Joshua C. Bufton, Imre Berger

المصدر: Sari-Ak, D, Bufton, J C, Gupta, K, Garzoni, F, Fitzgerald, D J, Berger-Schaffitzel, C H & Berger, I 2021, ' VLP-factory™ and ADDomer © : Self-assembling Virus-Like Particle (VLP) technologies for multiple protein and peptide epitope display ', Current Protocols, vol. 1, no. 3, e55 . https://doi.org/10.1002/cpz1.55

مصطلحات موضوعية: viruses, Hemagglutinin (influenza), BrisSynBio, Health Informatics, BioBrick, immunization, complex mixtures, General Biochemistry, Genetics and Molecular Biology, Epitope, Virus, 03 medical and health sciences, antigenic epitope, Virus-like particle, Antigen, baculovirus expression vector system (BEVS), vaccine, General Pharmacology, Toxicology and Pharmaceutics, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, General Immunology and Microbiology, biology, General Neuroscience, Bristol BioDesign Institute, 030302 biochemistry & molecular biology, virus diseases, Virology, 3. Good health, Medical Laboratory Technology, virus‐like particle (VLP), Capsid, chemistry, protein and peptide display, MultiBac, biology.protein, Glycoprotein

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6345d72b6d2db8471bdfc57adc6d042e
https://doi.org/10.1002/cpz1.55

المؤلفون: Christine Toelzer, Imre Berger, Frederic Garzoni, Maia Kavanagh Williamson, Julien Capin, Oskar Staufer, Joachim P. Spatz, Andrew D. Davidson, Kapil Gupta, Deborah K. Shoemark, Daniel J. Fitzgerald, Adrian J. Mulholland, Rachel Milligan, Ufuk Borucu, Christiane Schaffitzel, K.N. Sathish Yadav

المصدر: Science
Toelzer, C, Gupta, K, Yadav, S K N, Borucu, U, Davidson, A D, Kavanagh Williamson, M, Shoemark, D K, Garzoni, F, Staufer, O, Milligan, R, Capin, J, Mulholland, A J, Berger, I & Schaffitzel, C 2020, ' Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein ', Science, vol. 370, no. 6517, eabd3255 . https://doi.org/10.1126/science.abd3255
Science (New York, N.y.)

مصطلحات موضوعية: Models, Molecular, Linoleic acid, viruses, UNCOVER, BrisSynBio, Peptidyl-Dipeptidase A, Linoleic Acid, Betacoronavirus, chemistry.chemical_compound, Protein structure, Report, Fatty acid binding, Max Planck Bristol, Chlorocebus aethiops, Animals, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Binding site, skin and connective tissue diseases, Vero Cells, Peptide sequence, chemistry.chemical_classification, Binding Sites, Multidisciplinary, SARS-CoV-2, Cryoelectron Microscopy, Bristol BioDesign Institute, Biochem, Fatty acid, virus diseases, Covid19, Protein Structure, Tertiary, Cell biology, respiratory tract diseases, body regions, Severe acute respiratory syndrome-related coronavirus, chemistry, Spike Glycoprotein, Coronavirus, Middle East Respiratory Syndrome Coronavirus, Tissue tropism, Angiotensin-Converting Enzyme 2, Glycoprotein, Reports

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::900a1a0a17e2248e7197013081ee0f35
https://pubmed.ncbi.nlm.nih.gov/32958580/

المؤلفون: Joachim P. Spatz, Christine Toelzer, Frederic Garzoni, Daniel J. Fitzgerald, Oskar Staufer, Christiane Schaffitzel, Julien Capin, Imre Berger, Ufuk Borucu, Kapil Gupta, K.N. Sathish Yadav

مصطلحات موضوعية: chemistry.chemical_classification, viruses, Linoleic acid, virus diseases, Fatty acid, medicine.disease_cause, Cell biology, chemistry.chemical_compound, chemistry, Fatty acid binding, Metabolome, medicine, Membrane fluidity, Tissue tropism, Glycoprotein, Coronavirus

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::56ab0cd9112791ffb1628a81166e70a6
https://doi.org/10.1101/2020.06.18.158584

المؤلفون: Thibaut Crépin, Bruno Da Costa, Christopher Swale, Imre Berger, Andrew A. McCarthy, Frederic Garzoni, Bernard Delmas, Rob W. H. Ruigrok, Laura Sedano, Christoph Bieniossek

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), Virologie et Immunologie Moléculaires (VIM (UR 0892)), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Laboratoire européen de biologie moléculaire - European Molecular Biology Laboratory (EMBL Grenoble), Max Planck-Bristol Centre for Minimal Biology, F. Hoffmann-La Roche [Basel], Hofmann-La Roche pRED external collaboration programme, ANR-14-CE09-0017,RNAP-IAV,Interactions protéine-protéine et protéine-ARN au sein du complexe réplicatif du virus de la grippe de type A(2014), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), European Project: 279039,EC:FP7:HEALTH,FP7-HEALTH-2011-two-stage,COMPLEXINC(2011), Université Paris-Saclay, Centre Lillois d’Études et de Recherches Sociologiques et Économiques - UMR 8019 (CLERSÉ), Université de Lille-Centre National de la Recherche Scientifique (CNRS)

المصدر: Journal of Molecular Biology
Journal of Molecular Biology, 2020, 432 (10), pp.3353-3359. ⟨10.1016/j.jmb.2020.03.021⟩
Journal of Molecular Biology, Elsevier, 2020, 432 (10), pp.3353-3359. ⟨10.1016/j.jmb.2020.03.021⟩
Journal of Molecular Biology, Elsevier, 2020, S0022-2836(20)30254-0, ⟨10.1016/j.jmb.2020.03.021⟩

مصطلحات موضوعية: Gene isoform, Models, Molecular, Subfamily, Protein Conformation, Protein combining, medicine.disease_cause, Crystallography, X-Ray, 03 medical and health sciences, Viral Proteins, 0302 clinical medicine, Structural Biology, Influenza A virus, medicine, Humans, Point Mutation, Molecular Biology, Polymerase, 030304 developmental biology, Karyopherin, chemistry.chemical_classification, Cell Nucleus, human karyopherin, 0303 health sciences, Binding Sites, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Point mutation, RNA-Dependent RNA Polymerase, beta Karyopherins, influenza polymerase assembly, Cell biology, Molecular Docking Simulation, Protein Transport, Docking (molecular), PA-PB1 sub-complex nuclear import, biology.protein, NLS-binding site, host–pathogen interaction, 030217 neurology & neurosurgery, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33e8fdd993bac3b11d03f5437a199148
https://hal.univ-grenoble-alpes.fr/hal-02555361/document

المؤلفون: Véronique Josserand, Céline Terrat, Matthew Williams, Pascal Fender, Frederic Garzoni, Laurence Chaperot, Fruzsina Rabi, Emilie Stermann, Christopher J. Woods, Bernard Verrier, Joshua C. Bufton, Phil Bates, Gerardo Viedma, Mélanie Guidetti, Imre Berger, Charles Vragniau, Christiane Schaffitzel

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), University of Bristol [Bristol], Imophoron Ltd, Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305 (LBTI), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Oracle Cloud Development Centre, Institut de biologie et chimie des protéines [Lyon] (IBCP), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Max Planck-Bristol Centre for Minimal Biology, COIFFIER, Celine, 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), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de biologie structurale (IBS - UMR 5075), 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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), ANIMAGE, Rhône-Alpes Genopole, University of Cambridge [UK] (CAM), Laboratoire recherche et développement, EFS, Laboratoire européen de biologie moléculaire - European Molecular Biology Laboratory (EMBL Grenoble), European Molecular Biology Laboratory [Grenoble] (EMBL)

المصدر: Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (9), pp.eaaw2853. ⟨10.1126/sciadv.aaw2853⟩
Science Advances, 2019, 5 (9), pp.eaaw2853. ⟨10.1126/sciadv.aaw2853⟩
Vragniau, C, Bufton, J C, Garzoni, F, Stermann, E, Rabi, F, Terrat, C, Guidetti, M, Josserand, V, Williams, M, Woods, C J, Viedma, G, Bates, P, Verrier, B, Chaperot, L, Schaffitzel, C, Berger, I & Fender, P 2019, ' Synthetic self-assembling ADDomer platform for highly efficient vaccination by genetically encoded multiepitope display ', Science Advances, vol. 5, no. 9, eaaw2853 . https://doi.org/10.1126/sciadv.aaw2853

مصطلحات موضوعية: Models, Molecular, Scaffold, minimal biology, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, Protein Conformation, Computer science, viruses, advanced computing, Epitope, Epitopes, Synthetic biology, 0302 clinical medicine, Virus-like particle, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Structural Biology, Nanotechnology, ComputingMilieux_MISCELLANEOUS, Research Articles, Vaccines, Synthetic, 0303 health sciences, Multidisciplinary, Protein therapeutics, Vaccination, SciAdv r-articles, 3. Good health, Vaccinology, Nanomedicine, 030220 oncology & carcinogenesis, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Synthetic Biology, Genetic Engineering, Research Article, BrisSynBio, Computational biology, Communicable Diseases, Biodesign, Adenoviridae, Structure-Activity Relationship, Viral Proteins, 03 medical and health sciences, [SDV.IMM.VAC] Life Sciences [q-bio]/Immunology/Vaccinology, Self assembling, Humans, [SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/Biomaterials, 030304 developmental biology, Bristol BioDesign Institute, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, [SDV.IMM.IMM]Life Sciences [q-bio]/Immunology/Immunotherapy, [SDV.BIO] Life Sciences [q-bio]/Biotechnology, SYNTHETIC BIOLOGY, [CHIM.POLY]Chemical Sciences/Polymers, [SDV.SP.PG]Life Sciences [q-bio]/Pharmaceutical sciences/Galenic pharmacology, Infectious disease (medical specialty), Communicable Disease Control, [SDV.IMM.VAC]Life Sciences [q-bio]/Immunology/Vaccinology, Vaccine, Epitope Mapping

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aa7805a99c30018036acb2d535475a9
https://hal.archives-ouvertes.fr/hal-02333174/document

المؤلفون: Duygu, Sari-Ak, Shervin, Bahrami, Magdalena J, Laska, Petra, Drncova, Daniel J, Fitzgerald, Christiane, Schaffitzel, Frederic, Garzoni, Imre, Berger

المصدر: Methods in molecular biology (Clifton, N.J.). 2025

مصطلحات موضوعية: Hemagglutinins, Genome, Viral, Orthomyxoviridae, Baculoviridae

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::e563d1b7004f6c3cdb2326810239f37f
https://pubmed.ncbi.nlm.nih.gov/31267455