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1دورية أكاديمية
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2دورية أكاديمية
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3
المؤلفون: Ida Freda, Beatrice Vallone, C. Savino, Giulietta Smulevich, Linda Celeste Montemiglio, Cécile Exertier, Maurizio Becucci, Lisa Milazzo
المصدر: The FEBS journal
(2020). doi:10.1111/febs.15241
info:cnr-pdr/source/autori:Milazzo, Lisa; Exertier, Cecile; Becucci, Maurizio; Freda, Ida; Montemiglio, Linda Celeste; Savino, Carmelinda; Vallone, Beatrice; Smulevich, Giulietta/titolo:Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy/doi:10.1111%2Ffebs.15241/rivista:The FEBS journal (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volumeمصطلحات موضوعية: 0301 basic medicine, Hemeprotein, Protein Conformation, Resonance Raman spectroscopy, Protein Data Bank (RCSB PDB), Neuroglobin, Heme, Crystallography, X-Ray, Spectrum Analysis, Raman, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, symbols.namesake, Mice, 0302 clinical medicine, Animals, Amino Acid Sequence, Molecular Biology, Conformational isomerism, selected mutants, vinyl groups, Sequence Homology, Amino Acid, reversed heme, Cell Biology, microRaman, single crystal, Recombinant Proteins, Crystallography, 030104 developmental biology, chemistry, 030220 oncology & carcinogenesis, symbols, micro-Raman, Raman spectroscopy, Oxygen binding, Protein Binding
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المؤلفون: Francesca Siepi, Daniela Verzili, Cinzia Rinaldo, Antonella Scaglione, Silvia Soddu, Cristina Cecchetti, Carlotta Zamparelli, Giacomo Parisi, C. Savino, Linda Celeste Montemiglio, Alessandra Giorgi, Beatrice Vallone, Laura Monteonofrio
المصدر: Protein Science. 27:725-737
مصطلحات موضوعية: 0301 basic medicine, chemistry.chemical_classification, 030102 biochemistry & molecular biology, Kinase, Mutant, Wild type, Biochemistry, Cell biology, 03 medical and health sciences, 030104 developmental biology, Enzyme, chemistry, Protein kinase domain, Phosphorylation, Tyrosine, Protein kinase A, Molecular Biology
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5دورية أكاديمية
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6Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments
المؤلفون: S. Della Longa, Martin Weik, Thierry Prangé, Nathalie Colloc'h, Linda Celeste Montemiglio, Philippe Carpentier, C. Savino, Alessandro Arcovito, Cécile Exertier, Chiara Ardiccioni, Beatrice Vallone, Maurizio Brunori, P. van der Linden, G. Avella, Dominique Bourgeois
المساهمون: New York–Marche Structural Biology Center [Ancona, Italia] (NY-MaSBiC), Università Politecnica delle Marche [Ancona] (UNIVPM), Università cattolica del Sacro Cuore [Roma] (Unicatt), Fondazione Policlinico Universitario Agostino Gemelli, Università degli Studi dell'Aquila (UNIVAQ), European Synchrotron Radiation Facility (ESRF), Partnership for Soft Condensed Matter (PSCM), 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 Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Institute of Molecular Pathology and Biology [Rome] (IPBM), Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome]-Consiglio Nazionale delle Ricerche (CNR), Biocatalyse (BIOCAT ), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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 [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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 [2016-2019] (UGA [2016-2019]), Cibles Thérapeutiques et conception de médicaments (CiTCoM - UMR 8038), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Imagerie et Stratégies Thérapeutiques des pathologies Cérébrales et Tumorales (ISTCT), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), This work received funding from the European Union's Horizon 2020 Innovative Training Network (ITN-ETN) program under the Marie Skłodowska-Curie X-probe project (Grant Agreement No. 637295 to BV)., We acknowledge the European Synchrotron Radiation Facility for provision of synchrotron radiation facilities and we would like to thank Michel Pirocchi and Jean-Luc Ferrer for assistance in using beamline BM30-A, and Hassan Behlrali and Babu Manjasetty for assistance in using beamline BM14. IBS acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, CEA)., Thomas, Frank, Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics - X-probe - - H20202015-01-01 - 2018-12-31 - 637295 - VALID, Università cattolica del Sacro Cuore = Catholic University of the Sacred Heart [Roma] (Unicatt), Fondazione Policlinico Universitario Agostino Gemelli IRCCS, Università degli Studi dell'Aquila = University of L'Aquila (UNIVAQ), European Synchroton Radiation Facility [Grenoble] (ESRF), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-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), Consiglio Nazionale delle Ricerche (CNR), Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA)-Consiglio Nazionale delle Ricerche (CNR), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), Biocatalyse (BIOCAT), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Imagerie et Stratégies Thérapeutiques pour les Cancers et Tissus cérébraux (ISTCT), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), the European Synchrotron Radiation Facilityry Research Institute of Grenoble (IRIG, CEA)., European Project: 637295,H2020,H2020-MSCA-ITN-2014,X-probe(2015), 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), National Research Council of Italy | Consiglio Nazionale delle Ricerche (CNR), CNR Istituto di Biologia e Patologia Molecolari [Roma] (CNR | IBPM), Institut de Chimie du CNRS (INC)-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)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)
المصدر: International Union of Crystallography journal
International Union of Crystallography journal, International Union of Crystallography 2019, 5, 6 (5), pp.832-842. ⟨10.1107/S2052252519008157⟩
International Union of Crystallography journal, 2019, 6, pp.832-842. ⟨10.1107/S2052252519008157⟩
IUCrJ 6 (2019): 832–842. doi:10.1107/S2052252519008157
info:cnr-pdr/source/autori:Ardiccioni, Chiara; Arcovito, Alessandro; Della Longa, Stefano; van der Linden, Peter; Bourgeois, Dominique; Weik, Martin; Montemiglio, Linda Celeste; Savino, Carmelinda; Avella, Giovanna; Exertier, Cecile; Carpentier, Philippe; Prange, Thierry; Brunori, Maurizio; Colloc'h, Nathalie; Vallone, Beatrice/titolo:Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments/doi:10.1107%2FS2052252519008157/rivista:IUCrJ/anno:2019/pagina_da:832/pagina_a:842/intervallo_pagine:832–842/volume:6
IUCrJ, Vol 6, Iss 5, Pp 832-842 (2019)
IUCrJ
'IUCrJ ', vol: 6, pages: 832-842 (2019)مصطلحات موضوعية: Hemeprotein, crystal microspectroscopy, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Biochemistry, cryo-trapping, 03 medical and health sciences, structural biology, General Materials Science, Globin, lcsh:Science, Settore BIO/10 - BIOCHIMICA, Structure determination, 030304 developmental biology, ultralow-temperature X-ray crystallography, 0303 health sciences, CO photolysis, Heme protein, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, soak-and-freeze pressurization, 030302 biochemistry & molecular biology, Photodissociation, Hexacoordinate, Oxygen transport, heme protein, neuroglobin, neuroprotection, oxygen binding, protein structure, structure determination, XANES, General Chemistry, Condensed Matter Physics, Research Papers, Neuroprotection, 3. Good health, Docking (molecular), Neuroglobin, Biophysics, Protein structure, lcsh:Q, Oxygen binding
وصف الملف: application/pdf
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المؤلفون: Gabriele Cerutti, C. Savino, Giacomo Parisi, Massimiliano Anselmi, Cécile Exertier, Giulietta Smulevich, Antonella Scaglione, Linda Celeste Montemiglio, Beatrice Vallone, Lisa Milazzo, Ida Freda
المصدر: Scientific Reports
'Scientific Reports ', vol: 9, pages: 5326-1-5326-9 (2019)
Scientific reports (Nature Publishing Group) 9 (2019). doi:10.1038/s41598-019-41780-3
info:cnr-pdr/source/autori:Exertier, Cecile; Milazzo, Lisa; Freda, Ida; Montemiglio, Linda Celeste; Scaglione, Antonella; Cerutti, Gabriele; Parisi, Giacomo; Anselmi, Massimiliano; Smulevich, Giulietta; Savino, Carmelinda; Vallone, Beatrice/titolo:Proximal and distal control for ligand binding in neuroglobin: role of the CD loop and evidence for His64 gating/doi:10.1038%2Fs41598-019-41780-3/rivista:Scientific reports (Nature Publishing Group)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)مصطلحات موضوعية: Models, Molecular, Mutant, Molecular Conformation, lcsh:Medicine, Neuroglobin, Structural Characterization, Gating, Plasma protein binding, Heme, Ligands, Article, 03 medical and health sciences, chemistry.chemical_compound, Structure-Activity Relationship, 0302 clinical medicine, Resonance Raman spectroscopy, structural biology, Humans, neuroglobin, X-ray crystallography, Binding site, lcsh:Science, 030304 developmental biology, 0303 health sciences, Carbon Monoxide, Multidisciplinary, Binding Sites, Chemistry, lcsh:R, Wild type, Temperature, ligand binding, neuroglobin, CO, resonance Raman, mutated Ngbs, Kinetics, Mutation, Biophysics, lcsh:Q, heme sliding, 030217 neurology & neurosurgery, Oxygen binding, Protein Binding
وصف الملف: application/pdf
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المؤلفون: Gabriele Cerutti, Beatrice Vallone, Cécile Exertier, Linda Celeste Montemiglio, C. Savino, Giacomo Parisi, Antonella Scaglione, Alessandro Giuffrè, Alberto Macone
المصدر: The FASEB journal 33 (2019): 1787–1800. doi:10.1096/fj.201800450RR
info:cnr-pdr/source/autori:Parisi, Giacomo; Montemiglio, Linda Celeste; Giuffrè, Alessandro; Macone, Alberto; Scaglione, Antonella; Cerutti, Gabriele; Exertier, Cécile; Savino, Carmelinda; Vallone, Beatrice;/titolo:Substrate-induced conformational change in cytochrome P450 OleP/doi:10.1096%2Ffj.201800450RR/rivista:The FASEB journal/anno:2019/pagina_da:1787/pagina_a:1800/intervallo_pagine:1787–1800/volume:33
The FASEB Journalمصطلحات موضوعية: 0301 basic medicine, Conformational change, Stereochemistry, Protein Conformation, Substrate analog, Crystallography, X-Ray, Biochemistry, Gas Chromatography-Mass Spectrometry, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Biosynthesis, Cytochrome P-450 Enzyme System, Oxidoreductase, Genetics, Clotrimazole, Molecular Biology, 6DEB, X-ray crystallography, chemistry.chemical_classification, biology, spectroscopic intermediate, Cytochrome P450 activity, Cytochrome P450, Substrate (chemistry), Receptor–ligand kinetics, 3. Good health, Kinetics, 030104 developmental biology, chemistry, 14-alpha Demethylase Inhibitors, structural transition, multistep binding kinetics, biology.protein, 030217 neurology & neurosurgery, Biotechnology
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53d5e6250853eba6387ed3f1cf43a47e
http://www.scopus.com/record/display.url?eid=2-s2.0-85061063966&origin=inward -
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المؤلفون: C. Savino, Martina Pitea, Claudia Testi, Alberto Boffi, Alessandro Arcovito, Linda Celeste Montemiglio, F. Mancia, Pierpaolo Ceci, Paola Baiocco, Giovanna Peruzzi, Beatrice Vallone, A. Des Georges, Elisabetta Falvo
المصدر: Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
'Nature Communications ', vol: 10, pages: 1121-1-1121-8 (2019)
Nature communications 10 (2019). doi:10.1038/s41467-019-09098-w
info:cnr-pdr/source/autori:Montemiglio, Linda Celeste; Testi, Claudia; Ceci, Pierpaolo; Falvo, Elisabetta; Pitea, Martina; Savino, Carmelinda; Arcovito, Alessandro; Peruzzi, Giovanna; Baiocco, Paola; Mancia, Filippo; Boffi, Alberto; des Georges, Amedee; Vallone, Beatrice/titolo:Cryo-EM structure of the human ferritin-transferrin receptor 1 complex/doi:10.1038%2Fs41467-019-09098-w/rivista:Nature communications/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:10مصطلحات موضوعية: 0301 basic medicine, Protein Conformation, alpha-Helical, physics and astronomy (all), Protozoan Proteins, General Physics and Astronomy, Gene Expression, 02 engineering and technology, Plasma protein binding, Epitope, Substrate Specificity, Viral Envelope Proteins, Cloning, Molecular, lcsh:Science, Arenaviruses, New World, Transferrin receptor 1, chemistry.chemical_classification, Multidisciplinary, biology, genetics and molecular biology (all), Transferrin, 021001 nanoscience & nanotechnology, Recombinant Proteins, chemistry (all), biochemistry, genetics and molecular biology (all), 3. Good health, Cell biology, Ectodomain, Receptors, Virus, 0210 nano-technology, Protein Binding, Virus genetics, Science, Genetic Vectors, Context (language use), Transferrin receptor, Cryo-EM structure, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, Antigens, CD, Receptors, Transferrin, Escherichia coli, Humans, biochemistry, Protein Interaction Domains and Motifs, Hemochromatosis Protein, Settore BIO/10 - BIOCHIMICA, Ferritin, Binding Sites, Cryoelectron Microscopy, General Chemistry, 030104 developmental biology, chemistry, Apoferritins, biology.protein, lcsh:Q, Protein Conformation, beta-Strand, Plasmodium vivax, HeLa Cells
وصف الملف: application/pdf
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10دورية أكاديمية
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تسجيل الدخول للوصول الكامل.