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1. Full Text A post-translational modification of human Norovirus capsid protein attenuates glycan binding
by Mallagaray, Alvaro and Creutznacher, Robert and Dülfer, Jasmin and Mayer, Philipp H. O and Grimm, Lena Lisbeth and Orduña, Jose Maria and Trabjerg, Esben and Stehle, Thilo and Rand, Kasper D and Blaum, Bärbel S and Uetrecht, Charlotte and Peters, Thomas
Nature communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 1320 - 1320
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Isoaspartic Acid - metabolism | Humans | Protein Multimerization | Crystallography, X-Ray | Blood Group Antigens - genetics | Norovirus - metabolism | Blood Group Antigens - chemistry | Isoaspartic Acid - chemistry | Isoaspartic Acid - genetics | Capsid Proteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Polysaccharides - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Asparagine - genetics | Norovirus - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Capsid Proteins - metabolism | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Polysaccharides - metabolism | Host-Pathogen Interactions | Protein Conformation, beta-Strand | Escherichia coli - genetics | Asparagine - metabolism | Protein Binding | Protein Processing, Post-Translational | Kinetics | Blood Group Antigens - metabolism | Asparagine - chemistry | Capsid Proteins - genetics | Antigens | Transformation | Translation | Nuclear magnetic resonance--NMR | Capsid protein | Viruses | Mass spectroscopy | Infections | Crystallography | Glycan | Proteins | Conserved sequence | Asparagine | Post-translation | Mass spectrometry | Blood groups | Binding sites | Recognition | Index Medicus
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2. Full Text Argonaute quenching and global changes in Dicer homeostasis caused by a pathogen-encoded GW repeat protein
by Azevedo, Jacinthe and Garcia, Damien and Pontier, Dominique and Ohnesorge, Stephanie and Yu, Agnes and Garcia, Shahinez and Braun, Laurence and Bergdoll, Marc and Hakimi, Mohamed Ali and Lagrange, Thierry and Voinnet, Olivier
Genes & development, ISSN 0890-9369, 05/2010, Volume 24, Issue 9, pp. 904 - 915
TCV | Viral suppressor | Argonaute | GW motif | Genetics & Heredity | Life Sciences & Biomedicine | Developmental Biology | Science & Technology | Cell Biology | Amino Acid Sequence | Arabidopsis Proteins - genetics | Ribonuclease III - genetics | Ribonuclease III - metabolism | Capsid Proteins - metabolism | Gene Silencing | Molecular Sequence Data | Carmovirus - metabolism | Arabidopsis Proteins - metabolism | Host-Pathogen Interactions | Sequence Alignment | Plant Diseases - virology | Homeostasis - physiology | Capsid Proteins - chemistry | Argonaute Proteins | Cell Cycle Proteins - genetics | Protein Binding | Mutation | RNA, Small Interfering - metabolism | Gene silencing | Gene mutations | Arabidopsis | Analysis | Virus diseases of plants | Genetic aspects | Research | Plant viruses | Index Medicus | Life Sciences | Cellular Biology | viral suppressor | Research Paper
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3. Full Text Helix-mediated protein–protein interactions as targets for intervention using foldamers
by Edwards, Thomas A and Wilson, Andrew J
Amino acids, ISSN 0939-4451, 8/2011, Volume 41, Issue 3, pp. 743 - 754
Life Sciences | Biochemistry, general | Chemical biology | Foldamers | Analytical Chemistry | Protein–protein interactions | Life Sciences, general | Neurobiology | Proteomics | Biochemical Engineering | Helix mimetics | Protein-protein interactions | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Receptors, Notch - metabolism | Amino Acids - chemistry | HIV Envelope Protein gp41 - metabolism | Proto-Oncogene Proteins - chemistry | HIV Envelope Protein gp41 - chemistry | Proto-Oncogene Proteins c-mdm2 - chemistry | Proto-Oncogene Proteins c-bcl-2 - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Receptors, Cytoplasmic and Nuclear - chemistry | Hypoxia-Inducible Factor 1, alpha Subunit - chemistry | Proto-Oncogene Proteins c-bcl-2 - chemistry | Capsid - metabolism | Proto-Oncogene Proteins c-mdm2 - metabolism | Repressor Proteins - metabolism | Proto-Oncogene Proteins - metabolism | Repressor Proteins - chemistry | Peptides - chemistry | Protein Interaction Domains and Motifs - drug effects | Tumor Suppressor Protein p53 - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Peptides - pharmacology | Protein Interaction Mapping | Receptors, Notch - chemistry | Peptidomimetics | Tumor Suppressor Protein p53 - chemistry | Receptors, Cytoplasmic and Nuclear - metabolism | Enzymes | Amino acids | Locks | Mathematical models | Biology | Biological | Inhibition | Molecular biology | Index Medicus
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4. Full Text The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor
by Nielsen, Lau Dalby and Pedersen, Christian Parsbæk and Erlendsson, Simon and Teilum, Kaare
Structure (London), ISSN 0969-2126, 07/2019, Volume 27, Issue 7, pp. 1071 - 1081.e5
protein structure | retroviral capsid | NMR spectroscopy | human retrotranspon | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Cytoskeletal Proteins - genetics | Humans | Protein Multimerization | Receptors, N-Methyl-D-Aspartate - metabolism | Crystallography, X-Ray | Receptors, N-Methyl-D-Aspartate - genetics | Nerve Tissue Proteins - chemistry | Receptors, N-Methyl-D-Aspartate - chemistry | Capsid Proteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Cytoskeletal Proteins - metabolism | Neurons - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Neurons - chemistry | Capsid Proteins - metabolism | Genetic Vectors - metabolism | Models, Molecular | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cytoskeletal Proteins - chemistry | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Kinetics | Capsid Proteins - genetics | Proteins | Oligomers | Nuclear magnetic resonance spectroscopy | RNA | Molecular biology | Protein-protein interactions | Index Medicus
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5. Full Text A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies
by Krishnan, Rajaraman and Tsubery, Haim and Proschitsky, Ming Y and Asp, Eva and Lulu, Michal and Gilead, Sharon and Gartner, Myra and Waltho, Jonathan P and Davis, Peter J and Hounslow, Andrea M and Kirschner, Daniel A and Inouye, Hideyo and Myszka, David G and Wright, Jason and Solomon, Beka and Fisher, Richard A
Journal of molecular biology, ISSN 0022-2836, 06/2014, Volume 426, Issue 13, pp. 2500 - 2519
amyloid | gene 3 protein | amyloid remodeling | Ig fusion | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Neurodegenerative Diseases - etiology | Humans | Protein Multimerization | tau Proteins - metabolism | Bacteriophage M13 - metabolism | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | Bacteriophage M13 - genetics | Amyloid beta-Peptides - metabolism | Capsid Proteins - chemistry | Membrane Transport Proteins - metabolism | Protein Interaction Domains and Motifs | Capsid Proteins - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Neurodegenerative Diseases - metabolism | Recombinant Fusion Proteins - chemistry | Protein Folding | Membrane Transport Proteins - chemistry | alpha-Synuclein - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Conformation | Amyloid beta-Peptides - chemistry | Kinetics | Escherichia coli Proteins - chemistry | alpha-Synuclein - metabolism | Capsid Proteins - genetics | Viral proteins | Isomerization | Protein binding | Index Medicus
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6. Full Text Binding of host factors to stabilized HIV-1 capsid tubes
by Selyutina, Anastasia and Bulnes-Ramos, Angel and Diaz-Griffero, Felipe
Virology (New York, N.Y.), ISSN 0042-6822, 10/2018, Volume 523, pp. 1 - 5
HIV-1 | Binding | Stabilized tubes | CPSF6 | Cyp A | MxB | Human TRIM5α-R332P | TRIMCyp | Capsid | Life Sciences & Biomedicine | Science & Technology | Virology | Adaptor Proteins, Signal Transducing - chemistry | Nucleocapsid - chemistry | mRNA Cleavage and Polyadenylation Factors - metabolism | Humans | mRNA Cleavage and Polyadenylation Factors - chemistry | HIV-1 - chemistry | Nucleocapsid - metabolism | Capsid Proteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Biological Assay | Membrane Proteins - metabolism | mRNA Cleavage and Polyadenylation Factors - genetics | Recombinant Proteins - metabolism | HIV-1 - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Capsid Proteins - metabolism | Membrane Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Host-Pathogen Interactions | Membrane Proteins - chemistry | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Myxovirus Resistance Proteins - chemistry | Protein Binding | HeLa Cells | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Myxovirus Resistance Proteins - genetics | Myxovirus Resistance Proteins - metabolism | Capsid Proteins - genetics | Proteins | Medical colleges | Analysis | Cytochrome P-450 | HIV testing | HIV (Viruses) | Protein binding | Index Medicus | capsid | stabilized tubes | binding | human TRIM5α-R332P
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7. Full Text Functionalization of protein-based nanocages for drug delivery applications
by Schoonen, L and Hest, J.C.M. van
Nanoscale, ISSN 2040-3364, 2014, Volume 6, Issue 13, pp. 7124 - 7141
Physical Sciences | Chemistry | Materials Science | Nanoscience & Nanotechnology | Technology | Materials Science, Multidisciplinary | Science & Technology - Other Topics | Chemistry, Multidisciplinary | Physics | Science & Technology | Physics, Applied | Heat-Shock Proteins, Small - chemistry | Capsid Proteins - metabolism | Viral Proteins - chemistry | Heat-Shock Proteins, Small - metabolism | Humans | Viral Proteins - metabolism | Drug Carriers - chemistry | Animals | Ferritins - metabolism | Proteins - metabolism | Capsid Proteins - chemistry | Nanostructures - chemistry | Proteins - chemistry | Ferritins - chemistry | Index Medicus
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