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1دورية أكاديمية
المؤلفون: Jessica Lombino, Rosario Vallone, Maura Cimino, Maria Rita Gulotta, Giada De Simone, Maria Agnese Morando, Raffaele Sabbatella, Simona Di Martino, Mario Fogazza, Federica Sarno, Claudia Coronnello, Maria De Rosa, Chiara Cipollina, Lucia Altucci, Ugo Perricone, Caterina Alfano
المصدر: Clinical Epigenetics, Vol 15, Iss 1, Pp 1-16 (2023)
مصطلحات موضوعية: Epigenetic regulation, Lysine demethylases, KDM4 inhibitors, Fragment-based drug discovery (FBDD), KDM4A, Rational drug design, Medicine, Genetics, QH426-470
وصف الملف: electronic resource
Relation: https://doaj.org/toc/1868-7083
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2دورية أكاديمية
المؤلفون: Maria Agnese Morando, Francesca Venturella, Martina Sollazzo, Elisa Monaca, Raffaele Sabbatella, Valeria Vetri, Rosa Passantino, Annalisa Pastore, Caterina Alfano
المصدر: Communications Biology, Vol 5, Iss 1, Pp 1-10 (2022)
مصطلحات موضوعية: Biology (General), QH301-705.5
وصف الملف: electronic resource
Relation: https://doaj.org/toc/2399-3642
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المؤلفون: Alessandro Sicorello, Fabrizio Dal Piaz, Annalisa Pastore, Francesca Venturella, Caterina Alfano, Daniela Giacomazza, Estella Rao, Radha Santonocito, Maria Agnese Morando, Pier Luigi San Biagio, Maria Assunta Costa, Rosa Passantino, Alessia Provenzano, Donatella Bulone
المصدر: Journal of biological chemistry (Online) 294 (2019): 12826–12835. doi:10.1074/jbc.RA119.009531
info:cnr-pdr/source/autori:Santonocito R, Venturella F, Dal Piaz F, Morando MA, Provenzano A, Rao E, Costa MA, Bulone D, San Biagio PL, Giacomazza D, Sicorello A, Alfano C, Passantino R, Pastore A/titolo:Recombinant mussel protein Pvfp-5beta: a potential tissue bioadhesive/doi:10.1074%2Fjbc.RA119.009531/rivista:Journal of biological chemistry (Online)/anno:2019/pagina_da:12826/pagina_a:12835/intervallo_pagine:12826–12835/volume:294
Santonocito, R, Venturella, F, Dal Piaz, F, Morando, M A, Provenzano, A, Rao, E, Costa, M A, Bulone, D, San Biagio, P L, Giacomazza, D, Sicorello, A, Alfano, C, Passantino, R & Pastore, A 2019, ' Recombinant mussel protein Pvfp-5β: a potential tissue bioadhesive ', Journal of Biological Chemistry, vol. 294, no. 34, jbc.RA119.009531, pp. 12826-12835 . https://doi.org/10.1074/jbc.RA119.009531
The Journal of Biological Chemistryمصطلحات موضوعية: 0301 basic medicine, medicine.disease_cause, Biochemistry, epidermal growth factor (EGF), law.invention, Mice, Cell Movement, law, biophysics, structural biology, recombinant, Cells, Cultured, biology, Chemistry, Marine proteins, Adhesion, Recombinant Proteins, adhesion, Protein Structure and Folding, Recombinant DNA, adhesion proteins, biomaterials, Perna, Cell Survival, Surface Properties, Bioadhesive, mussel, 03 medical and health sciences, medicine, Animals, Humans, Molecular Biology, Escherichia coli, Cell Proliferation, Tissue Engineering, 030102 biochemistry & molecular biology, Proteins, Cell Biology, Mussel, biology.organism_classification, EGF-like motifs, 030104 developmental biology, Structural biology, Cell culture, NIH 3T3 Cells, Biophysics, Tissue Adhesives, HeLa Cells, Perna viridis
وصف الملف: application/pdf
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67b376e6b288498b930784a230adb442
https://doi.org/10.1074/jbc.ra119.009531 -
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المؤلفون: Encarna Pucheta-Martínez, Giorgio Saladino, Maria Agnese Morando, Jorge Martinez-Torrecuadrada, Moreno Lelli, Ludovico Sutto, Nicola D’Amelio, Francesco Luigi Gervasio
المساهمون: Engineering and Physical Sciences Research Council (Reino Unido), European Research Council, HECBioSim (EPSRC), Medical Research Council (Reino Unido), The Francis Crick Institute
المصدر: Repisalud
Instituto de Salud Carlos III (ISCIII)
Scientific Reportsمصطلحات موضوعية: inorganic chemicals, Binding Sites, Molecular Dynamics Simulation, environment and public health, Article, enzymes and coenzymes (carbohydrates), Adenosine Triphosphate, src-Family Kinases, Allosteric Regulation, Catalytic Domain, Humans, Nuclear Magnetic Resonance, Biomolecular, Phosphorylation, Thermodynamics, Tyrosine, Multidisciplinary, bacteria
URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::30c3d8f5b0ea24e932d47c091ba311a4
https://hdl.handle.net/20.500.12105/8555
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