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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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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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Helix-mediated protein–protein interactions as targets for intervention using foldamers
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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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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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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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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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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