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1. The nucleohistones
by James, Bonner and Ts'o, Paul O. P
1964, xvii, 398
Nucleoproteins
Book
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2. Les glycoprotéines sériques à l'état normal et pathologique
by Sonnet, J
1956, 200
Nucleoproteins
Book
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3. Full Text Cap binding and immune evasion revealed by Lassa nucleoprotein structure
by Wallat, Gregor D and Liang, Yuying and Lan, Shuiyun and Schelde, Lisa McLay and Ly, Hinh and Qi, Xiaoxuan and Dong, Haohao and Dong, Changjiang and Wang, Wenjian
Nature (London), ISSN 0028-0836, 12/2010, Volume 468, Issue 7325, pp. 779 - 783
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Microbiology | Morphology, structure, chemical composition, physicochemical properties | Virology | Nucleoproteins - chemistry | Interferons - biosynthesis | RNA-Binding Proteins - genetics | Exoribonucleases - genetics | Nucleoproteins - genetics | Exoribonucleases - chemistry | Viral Proteins - immunology | Crystallography, X-Ray | Interferons - immunology | RNA Caps - metabolism | Viral Proteins - metabolism | RNA, Viral - genetics | RNA Caps - chemistry | Transcription, Genetic | RNA, Viral - metabolism | RNA Cap Analogs - metabolism | Nucleoproteins - immunology | Protein Structure, Tertiary | Viral Proteins - chemistry | RNA, Viral - biosynthesis | RNA-Binding Proteins - chemistry | Lassa virus - genetics | Models, Molecular | Viral Proteins - genetics | Lassa virus - immunology | RNA Cap Analogs - chemistry | Nucleoproteins - metabolism | Lassa virus - chemistry | Immune Evasion - immunology | Exoribonucleases - metabolism | RNA-Binding Proteins - metabolism | Lassa fever | Immune response | Nucleoproteins | Causes of | Physiological aspects | Development and progression | Genetic aspects | Research | Proteins | Pathology | Immunology | Crystal structure | Index Medicus
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4. Full Text Partner-Mediated Polymorphism of an Intrinsically Disordered Protein
by Bignon, Christophe and Troilo, Francesca and Gianni, Stefano and Longhi, Sonia
Journal of molecular biology, ISSN 0022-2836, 08/2018, Volume 430, Issue 16, pp. 2493 - 2507
induced folding | NTAIL | XD | measles virus | major inducible heat shock protein (hsp70) | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Proteins | Heat shock proteins | Fluorescence | Genetic aspects | Protein binding | Index Medicus | Biotechnology | Viral Proteins/genetics | Intrinsically Disordered Proteins/chemistry | Intrinsically Disordered Proteins/metabolism | Measles virus/metabolism | Neurons and Cognition | Neurobiology | Innate immunity | Nucleoproteins/genetics | Emerging diseases | Nucleoproteins/chemistry | Life Sciences | Viral Proteins/chemistry | Immunology | Biomolecules | Binding Sites | Pharmaceutical sciences | Protein Conformation, alpha-Helical | Quantitative Methods | Biochemistry, Molecular Biology | HSP70 Heat-Shock Proteins/metabolism | Models, Molecular | Pharmacology | Phosphoproteins/metabolism | Protein Folding | Bacteriology | Virology | Nucleoproteins/metabolism | Human health and pathology | Microbiology and Parasitology | Infectious diseases | Intrinsically Disordered Proteins/genetics | Protein Binding | Viral Proteins/metabolism | Amino Acid Substitution | Measles virus/genetics
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5. Full Text How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication
by Longhi, Sonia and Bloyet, Louis-Marie and Gianni, Stefano and Gerlier, Denis
Cellular and molecular life sciences : CMLS, ISSN 1420-682X, 9/2017, Volume 74, Issue 17, pp. 3091 - 3118
Biomedicine, general | Biochemistry, general | Intrinsic structural disorder | Induced folding | Protein–protein interactions | Nucleoprotein | Cell Biology | Life Sciences | Antiviral approaches | Paramyxoviruses | Life Sciences, general | Fuzzy complexes | Phosphoprotein | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Nucleoproteins - chemistry | Molecular Chaperones - metabolism | Viral Proteins - chemistry | Nucleoproteins - genetics | Paramyxoviridae - classification | Viral Proteins - genetics | Antiviral Agents - metabolism | Molecular Chaperones - chemistry | Phosphoproteins - genetics | Phosphoproteins - metabolism | Intrinsically Disordered Proteins - genetics | Viral Proteins - metabolism | Phosphoproteins - chemistry | Virus Replication | Intrinsically Disordered Proteins - chemistry | Nucleoproteins - metabolism | Protein Structure, Quaternary | Paramyxoviridae - metabolism | RNA, Viral - metabolism | Evolution, Molecular | Intrinsically Disordered Proteins - metabolism | Antiviral agents | Information management | Genetic transcription | Phosphoproteins | Protein binding | Proteins | Molecular modelling | Transcription | Nucleoproteins | Measles | Computer applications | Viruses | Homology | Molecular biology | Structure-function relationships | Index Medicus | Biotechnology | Neurons and Cognition | Neurobiology | Innate immunity | Viral Proteins | Emerging diseases | Paramyxoviridae | Immunology | Biomolecules | Pharmaceutical sciences | Molecular Chaperones | Quantitative Methods | Biochemistry, Molecular Biology | Intrinsically Disordered Proteins | Antiviral Agents | Pharmacology | Bacteriology | Virology | Human health and pathology | Microbiology and Parasitology | Infectious diseases | RNA, Viral
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6. Full Text Structure-Based Discovery of the Novel Antiviral Properties of Naproxen against the Nucleoprotein of Influenza A Virus
by Nathalie Lejal and Bogdan Tarus and Edwige Bouguyon and Sylvie Chenavas and Nicolas Bertho and Bernard Delmas and Rob W. H. Ruigrok and Carmelo Di Primo and Anny Slama-Schwok
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 05/2013, Volume 57, Issue 5, pp. 2231 - 2242
Pharmacology & Pharmacy | Life Sciences & Biomedicine | Microbiology | Science & Technology | Biological and medical sciences | Medical sciences | Pharmacology. Drug treatments | Antibiotics. Antiinfectious agents. Antiparasitic agents | Nucleoproteins - chemistry | Influenza A Virus, H3N2 Subtype - drug effects | Influenza A Virus, H3N2 Subtype - metabolism | Naproxen - pharmacology | Anti-Inflammatory Agents, Non-Steroidal - chemistry | Viral Proteins - metabolism | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | RNA, Viral - antagonists & inhibitors | Antiviral Agents - chemistry | Madin Darby Canine Kidney Cells | RNA, Viral - metabolism | Binding Sites | Influenza A Virus, H1N1 Subtype - metabolism | Orthomyxoviridae Infections - drug therapy | Antiviral Agents - pharmacology | Viral Proteins - chemistry | Viral Proteins - antagonists & inhibitors | Drug Repositioning | Influenza A Virus, H1N1 Subtype - drug effects | Drug Discovery | Molecular Dynamics Simulation | Nucleoproteins - antagonists & inhibitors | Naproxen - chemistry | Point Mutation | Animals | Influenza A Virus, H3N2 Subtype - chemistry | RNA, Viral - chemistry | Nucleoproteins - metabolism | Dogs | Protein Binding | Influenza A Virus, H1N1 Subtype - chemistry | Mice | Molecular Docking Simulation | Orthomyxoviridae Infections - virology | Index Medicus | Anti-Inflammatory Agents, Non-Steroidal | Influenza A Virus, H3N2 Subtype | Nucleoproteins | Biochemistry, Molecular Biology | Viral Proteins | Antiviral Agents | Life Sciences | Naproxen | RNA, Viral | Influenza A Virus, H1N1 Subtype | Biomolecules | Orthomyxoviridae Infections
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7. Influenza virus nucleoprotein: Structure, RNA binding, oligomerization and antiviral drug target
by Chenavas, Sylvie and Cre ́pin, Thibaut and Delmas, Bernard and Ruigrok, Rob W.H and Slama-Schwok, Anny
Future microbiology, ISSN 1746-0913, 12/2013, Volume 8, Issue 12, pp. 1537 - 1545
nucleoprotein | viral RNA | RNP | resistance | antiviral | Life Sciences & Biomedicine | Microbiology | Science & Technology | Nucleoproteins - chemistry | Influenza A virus - chemistry | Antiviral Agents - pharmacology | Viral Proteins - chemistry | Humans | Influenza A virus - genetics | Nucleoproteins - genetics | Viral Proteins - genetics | Viral Proteins - antagonists & inhibitors | Viral Proteins - metabolism | Nucleoproteins - antagonists & inhibitors | Animals | Influenza A virus - metabolism | RNA, Viral - genetics | Nucleoproteins - metabolism | Influenza, Human - virology | RNA, Viral - metabolism | Influenza, Human - drug therapy | Influenza A virus - drug effects
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8. Full Text Dimerization through the RING Finger Domain Attenuates Excision Activity of the piggyback Transposese
by Rahul, Sharma and Shivlee, Nirwal and Naveen, Narayanan and Deepak, Nair.T
Biochemistry (Easton), ISSN 0006-2960, 05/2018, Volume 57, Issue 20, p. 2913
Enzymes | Nucleoproteins | Analysis
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9. Full Text NapA and NapB are the Aspergillus nidulans Nap/SET family members and NapB is a nuclear protein specifically interacting with importin [alpha]
Fungal genetics and biology, ISSN 1087-1845, 03/2008, Volume 45, Issue 3, p. 278
Nucleoproteins
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10. Full Text Histone Modifications in Therapy
by Castelo-Branco, Pedro and Jeronimo, Carmen
2020, ISBN 0128164220, 492
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