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1. 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
Protein–protein interactions (PPIs) play a central role in virtually all biological processes and have been the focus of intense investigation from structural... 
Life Sciences | Biochemistry, general | Chemical biology | Foldamers | Analytical Chemistry | Protein–protein interactions | Life Sciences, general | Neurobiology | Proteomics | Biochemical Engineering | Helix mimetics | Protein-protein interactions | HYDROGEN-BOND-SURROGATE | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL-CHARACTERIZATION | DIMERIZATION DOMAIN | BETA-PEPTIDES | ESTROGEN-RECEPTOR | ALPHA-HELICES | INHIBITION | IN-VIVO | ANTAGONISTS | 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
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2. 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
Misfolded protein aggregates, characterized by a canonical amyloid fold, play a central role in the pathobiology of neurodegenerative diseases. Agents that... 
amyloid | gene 3 protein | amyloid remodeling | Ig fusion | FIBRIL FORMATION | MEMBRANE-FILTER ASSAY | N-TERMINAL DOMAINS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ALPHA-SYNUCLEIN | FILAMENTOUS PHAGE FD | PROLYL ISOMERIZATION | CONFORMATIONAL CONVERSION | A-BETA | 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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3. Full Text Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging
by Iyer, Lakshiminarayan M and Makarova, Kira S and Koonin, Eugene V and Aravind, L
Nucleic Acids Research, ISSN 0305-1048, 2004, Volume 32, Issue 17, pp. 5260 - 5279
Recently, it has been shown that a predicted P-loop ATPase (the HerA or MlaA protein), which is highly conserved in archaea and also present in many bacteria... 
ESSENTIAL VIRULENCE PROTEIN | AGROBACTERIUM-TUMEFACIENS | TIGHT JUNCTIONS | SMC PROTEINS | CRYSTAL-STRUCTURE | TRANSFER SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BACTERIAL CONJUGATION | IV SECRETION | EVOLUTIONARY HISTORY | SEQUENCE COMPARISONS | Viruses - genetics | Genomics | Archaeal Proteins - chemistry | Bacterial Proteins - chemistry | Molecular Sequence Data | Phylogeny | Archaea - enzymology | Viruses - enzymology | Capsid Proteins - physiology | Adenosine Triphosphatases - classification | Membrane Transport Proteins - genetics | Virus Assembly - genetics | Cell Division | Archaeal Proteins - genetics | Membrane Proteins - classification | Archaeal Proteins - classification | Protein Structure, Tertiary | Amino Acid Sequence | Chromosome Segregation | Membrane Proteins - genetics | Viral Proteins - chemistry | Bacterial Proteins - genetics | Viral Proteins - genetics | Bacteria - genetics | Viral Proteins - classification | Endonucleases - chemistry | Membrane Transport Proteins - chemistry | Sequence Alignment | Escherichia coli Proteins | Membrane Proteins - chemistry | Membrane Transport Proteins - classification | Adenosine Triphosphatases - chemistry | Bacteria - enzymology | Adenosine Triphosphatases - genetics | Archaea - genetics | Bacterial Proteins - classification | Evolution, Molecular
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4. Full Text The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection
by Woodham, Andrew W and da Silva, Diane M and Skeate, Joseph G and Raff, Adam B and Ambroso, Mark R and Brand, Heike E and Isas, J. Mario and Langen, Ralf and Kast, W. Martin
PLoS ONE, ISSN 1932-6203, 08/2012, Volume 7, Issue 8, p. e43519
Mucosotropic, high-risk human papillomaviruses (HPV) are sexually transmitted viruses that are causally associated with the development of cervical cancer. The... 
MULTIDISCIPLINARY SCIENCES | HUMAN CYTOMEGALOVIRUS | SQUAMOUS-CELL CARCINOMA | INHIBITOR SLPI | VIRUS-LIKE PARTICLES | HEPARAN-SULFATE | CERVICAL-CANCER | II BINDS | MINOR CAPSID PROTEIN | COMMON NEUTRALIZATION EPITOPE | RNA, Small Interfering - genetics | Human papillomavirus 16 - physiology | Oncogene Proteins, Viral - chemistry | Humans | Protein Multimerization | Molecular Sequence Data | Substrate Specificity | Receptors, Cell Surface | S100 Proteins - immunology | S100 Proteins - chemistry | Gene Knockdown Techniques | Epitopes - immunology | Annexin A2 - chemistry | S100 Proteins - genetics | Capsid Proteins - chemistry | Protein Structure, Quaternary | Capsid Proteins - immunology | Oncogene Proteins, Viral - genetics | Annexin A2 - immunology | Oncogene Proteins, Viral - metabolism | Amino Acid Sequence | Capsid Proteins - metabolism | S100 Proteins - metabolism | Human papillomavirus 16 - metabolism | Annexin A2 - genetics | Epithelial Cells - virology | Epitopes - chemistry | Oncogene Proteins, Viral - immunology | HeLa Cells | Mutation | Annexin A2 - metabolism | Capsid Proteins - genetics | Genotype | Genetic aspects | Research | Annexins | Health aspects | Papillomavirus infections | Risk factors | Capsid protein | Peptides | Epithelial cells | Viruses | Amino acids | Infections | Biochemistry | Cell interactions | Cell surface | Nuclei | Proteins | S100 protein | Human papillomavirus | Immunology | Calcium-binding protein | Deoxyribonucleic acid--DNA | Genotypes | Immunoglobulins | Departments | Risk groups | Gynecology | Health risks | Proteinase inhibitors | Epitopes | Cervix | Obstetrics | White blood cells | Disease transmission | Neutralizing | Herpes viruses | Internalization | Nuclei (cytology) | Electron paramagnetic resonance | Molecular biology | Cervical cancer | Cancer | Deoxyribonucleic acid | DNA
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5. Full Text Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection
by Vijay S. Reddy and Glen R. Nemerow
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2014, Volume 111, Issue 32, pp. 11715 - 11720
Adenovirus cement proteins play crucial roles in virion assembly, disassembly, cell entry, and infection. Based on a refined crystal structure of the... 
Proteins | Molecules | Adenoviruses | Virions | Amino acids | Cements | Capsid | Triskelion | Vertices | Crystal structure | Cement protein scaffold | Human adenovirus | Structure-function relationships | VIRION | DNA | MULTIDISCIPLINARY SCIENCES | structure-function relationships | RESOLUTION | cement protein scaffold | human adenovirus | N-TERMINUS | MICROSCOPY | TYPE-2 | PEPTIDE | REVEALS | Viral Core Proteins - chemistry | DNA-Binding Proteins - physiology | Biophysical Phenomena | Capsid - chemistry | Viral Proteins - chemistry | Humans | Adenoviruses, Human - physiology | Models, Molecular | Capsid - physiology | Crystallography, X-Ray | Virus Assembly - physiology | Adenoviruses, Human - pathogenicity | Static Electricity | DNA-Binding Proteins - chemistry | Viral Core Proteins - physiology | Virus Internalization | Multiprotein Complexes - physiology | Multiprotein Complexes - chemistry | Capsid Proteins - physiology | Adenoviruses, Human - chemistry | Capsid Proteins - chemistry | Protein Structure, Quaternary | Viral Proteins - physiology | Protein research | Viral proteins | Host-parasite relationships | Research | Structure | Virus research | Health aspects | Biological Sciences | structure–function relationships
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6. Full Text TRIM5 is an innate immune sensor for the retrovirus capsid lattice
by Pertel, Thomas and Hausmann, Stéphane and Morger, Damien and Züger, Sara and Guerra, Jessica and Lascano, Josefina and Reinhard, Christian and Santoni, Federico A and Uchil, Pradeep D and Chatel, Laurence and Bisiaux, Aurélie and Albert, Matthew L and Strambio-De-Castillia, Caterina and Mothes, Walther and Pizzato, Massimo and Grütter, Markus G and Luban, Jeremy
Nature, ISSN 0028-0836, 04/2011, Volume 472, Issue 7343, pp. 361 - 365
TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV)-1 and other retroviruses immediately following virus... 
HIV-1 | CYCLOPHILIN-A | UNANCHORED POLYUBIQUITIN CHAINS | TRIM5-ALPHA PROTEIN | RECOGNITION | HUMAN-CELLS | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | RESISTANCE | INFECTION | RESTRICTION | Capsid - chemistry | Receptors, Pattern Recognition - immunology | Humans | Ubiquitin - metabolism | NF-kappa B - metabolism | Lipopolysaccharides - immunology | Transcription Factor AP-1 - metabolism | Receptors, Pattern Recognition - metabolism | Signal Transduction - immunology | Ubiquitin-Protein Ligases - immunology | HIV-1 - chemistry | HEK293 Cells | Carrier Proteins - immunology | Cell Line | Retroviridae - chemistry | Ubiquitin-Protein Ligases - metabolism | Retroviridae - immunology | MAP Kinase Kinase Kinases - metabolism | Transcription Factors - metabolism | Capsid - immunology | Carrier Proteins - genetics | Immunity, Innate - immunology | HIV-1 - immunology | Carrier Proteins - metabolism | Signal Transduction - drug effects | Ubiquitin-Conjugating Enzymes - metabolism | Lipopolysaccharides - pharmacology | Protein Binding | Enzyme Activation | Ubiquitin-Protein Ligases - genetics | Signal transduction | Efficiency | RNA polymerase | Pattern recognition | Kinases | Evacuations & rescues | Immune system | HIV-1/immunology | Capsid/immunology | Life Sciences | MAP Kinase Kinase Kinases/metabolism | Carrier Proteins/immunology | Immunology | Transcription Factors/metabolism | Capsid/chemistry | HIV-1/chemistry | Ubiquitin/metabolism | Receptors, Pattern Recognition/immunology | Retroviridae/chemistry | Ubiquitin-Protein Ligases/immunology | Ubiquitin-Conjugating Enzymes/metabolism | HumansImmunity, Innate/immunology | Lipopolysaccharides/pharmacology | Signal Transduction/drug effects | Retroviridae/immunology | Transcription Factor AP-1/metabolism | Lipopolysaccharides/immunology | Ubiquitin-Protein Ligases/metabolism | Carrier Proteins/genetics | Signal Transduction/immunology | NF-kappa B/metabolism | Ubiquitin-Protein Ligases/genetics | Carrier Proteins/metabolism | Receptors, Pattern Recognition/metabolism
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7. Full Text ICM‐DISCO docking by global energy optimization with fully flexible side‐chains
by Fernández‐Recio, Juan and Totrov, Maxim and Abagyan, Ruben
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 07/2003, Volume 52, Issue 1, pp. 113 - 117
The ICM‐DISCO (Docking and Interface Side‐Chain Optimization) protein–protein‐docking method is a direct stochastic global energy optimization from multiple... 
soft grid potentials | protein–protein docking | biased probability stochastic global optimization | pseudo‐Brownian rigid body Monte Carlo | internal coordinate mechanics | Protein-protein docking | Internal coordinate mechanics | Pseudo-Brownian rigid body Monte Carlo | Biased probability stochastic global optimization | Soft grid potentials | COMPLEX | PROTEIN | protein-protein docking | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIBODY | PARAMETERS | pseudo-Brownian rigid body Monte Carlo | PREDICTION | PEPTIDES | GENETICS & HEREDITY | BINDING | CONFORMATIONAL SEARCHES | Antibodies - chemistry | Receptors, Antigen, T-Cell, alpha-beta - chemistry | Bacterial Proteins - chemistry | Amino Acids - chemistry | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Exotoxins - metabolism | Antigens, Viral | Capsid Proteins - chemistry | Antibodies - immunology | Capsid Proteins - immunology | Membrane Proteins - metabolism | Binding Sites | Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry | Protein-Serine-Threonine Kinases - metabolism | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Exotoxins - chemistry | Models, Molecular | alpha-Amylases - metabolism | Macromolecular Substances | Protein Interaction Mapping | Algorithms | Proteins - metabolism | Membrane Proteins - chemistry | alpha-Amylases - chemistry | Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism | Bacterial Proteins - metabolism | Protein-Serine-Threonine Kinases - chemistry | Proteins - chemistry | Receptors, Antigen, T-Cell, alpha-beta - metabolism | Monte Carlo Method
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8. 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
Traditional drug delivery strategies involve drugs which are not targeted towards the desired tissue. This can lead to undesired side effects, as normal cells... 
PHYSICS, APPLIED | EFFICIENT INTRACELLULAR DELIVERY | MATERIALS SCIENCE, MULTIDISCIPLINARY | CELL-SPECIFIC DELIVERY | NANOSCIENCE & NANOTECHNOLOGY | BACTERIOPHAGE-Q-BETA | COWPEA MOSAIC-VIRUS | TRANSFER RADICAL POLYMERIZATION | CHEMISTRY, MULTIDISCIPLINARY | HEAT-SHOCK-PROTEIN | SUPRAMOLECULAR BUILDING-BLOCKS | EPIDERMAL-GROWTH-FACTOR | VIRUS-LIKE PARTICLES | CHLOROTIC MOTTLE VIRUS | 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
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9. Full Text Cryoelectron Microscopy Maps of Human Papillomavirus 16 Reveal L2 Densities and Heparin Binding Site
by Guan, Jian and Bywaters, Stephanie M and Brendle, Sarah A and Ashley, Robert E and Makhov, Alexander M and Conway, James F and Christensen, Neil D and Hafenstein, Susan
Structure, ISSN 0969-2126, 02/2017, Volume 25, Issue 2, pp. 253 - 263
Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. The current commercial vaccines are genotype specific and... 
heparin | entry | receptor | difference density | human papillomavirus | capsid | classification | cryo-EM | heterogeneity | BOVINE PAPILLOMAVIRUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IMAGE-RECONSTRUCTION | EM STRUCTURE DETERMINATION | CRYO-EM | MAJOR CAPSID PROTEIN | CERVICAL-CANCER | CELL BIOLOGY | SULFATE PROTEOGLYCANS | ELECTRON CRYOMICROSCOPY | BIOPHYSICS | VIRUS-LIKE PARTICLES | MONOCLONAL-ANTIBODIES | Heparin - metabolism | Capsid - chemistry | Oncogene Proteins, Viral - chemistry | Humans | Crystallography, X-Ray | Capsid Proteins - chemistry | Cloning, Molecular | HEK293 Cells | Oncogene Proteins, Viral - genetics | Protein Interaction Domains and Motifs | Human papillomavirus 16 - chemistry | Capsid - metabolism | Binding Sites | Oncogene Proteins, Viral - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Capsid Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Human papillomavirus 16 - metabolism | Amino Acid Motifs | Cryoelectron Microscopy | Protein Conformation, beta-Strand | Protein Binding | Human papillomavirus 16 - genetics | Heparin - chemistry | Capsid Proteins - genetics | Papillomaviruses | Medical colleges | Viral proteins | Therapeutics | Atoms | Heparin | Health aspects | Papillomavirus infections | Protein binding | Homeopathy | Materia medica and therapeutics
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10. Full Text Mutated and Bacteriophage T4 Nanoparticle Arrayed F1-V Immunogens from Yersinia pestis as Next Generation Plague Vaccines
by Tao, Pan and Mahalingam, Marthandan and Kirtley, Michelle L and van Lier, Christina J and Sha, Jian and Yeager, Linsey A and Chopra, Ashok K and Rao, Venigalla B
PLoS Pathogens, ISSN 1553-7366, 07/2013, Volume 9, Issue 7, p. e1003495
Pneumonic plague is a highly virulent infectious disease with 100% mortality rate, and its causative organism Yersinia pestis poses a serious threat for... 
SYSTEM | MICROBIOLOGY | OUTER CAPSID PROTEIN | SUBUNIT VACCINE | IN-VITRO | VIROLOGY | V-ANTIGEN | RECOMBINANT | PURIFICATION | FUSION PROTEIN | IMMUNE DEFENSE | PARASITOLOGY | PNEUMONIC PLAGUE | Pore Forming Cytotoxic Proteins - genetics | Antigens, Viral - metabolism | Capsid - chemistry | Bacteriophage T4 - immunology | Plague - microbiology | Bacterial Proteins - chemistry | Bacteriophage T4 - chemistry | Antigens, Viral - genetics | Yersinia pestis - virology | Antigens, Bacterial - genetics | Vaccines, Virus-Like Particle - chemistry | Bacteriophage T4 - metabolism | Rats, Inbred BN | Plague - virology | Plague - immunology | Female | Protein Interaction Domains and Motifs | Capsid - metabolism | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Antigens, Bacterial - chemistry | Pore Forming Cytotoxic Proteins - metabolism | Plague Vaccine - chemistry | Capsid Proteins - metabolism | Bacterial Proteins - genetics | Rats | Recombinant Proteins - chemistry | Antigens, Viral - chemistry | Mutant Proteins - metabolism | Random Allocation | Particle Size | Yersinia pestis - immunology | Capsid - immunology | Peptide Fragments - chemistry | Animals | Pore Forming Cytotoxic Proteins - chemistry | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Vaccines, Virus-Like Particle - immunology | Mice | Mice, Inbred BALB C | Antigens, Bacterial - metabolism | Plague Vaccine - immunology | Plague - prevention & control | Capsid Proteins - genetics | Bacteriophages | Physiological aspects | Virulence (Microbiology) | Research | Health aspects | Yersinia pestis | Plague | Immunization | Mortality | Genomics | Fatalities | FDA approval | Vaccines
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