X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (12603) 12603
Publication (3102) 3102
Book Chapter (147) 147
Book Review (71) 71
Conference Proceeding (48) 48
Streaming Video (11) 11
Magazine Article (8) 8
Data Set (5) 5
Dissertation (5) 5
Paper (3) 3
Book / eBook (1) 1
Newspaper Article (1) 1
Web Resource (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (5054) 5054
animals (4288) 4288
virology (4035) 4035
humans (3949) 3949
molecular sequence data (3814) 3814
viruses (3632) 3632
amino acid sequence (3468) 3468
biochemistry & molecular biology (3310) 3310
capsid - chemistry (2898) 2898
capsid proteins - chemistry (2749) 2749
capsid proteins - genetics (2692) 2692
proteins (2364) 2364
capsid proteins (2041) 2041
models, molecular (2002) 2002
capsid proteins - metabolism (1972) 1972
capsid - metabolism (1969) 1969
base sequence (1803) 1803
capsid - genetics (1615) 1615
capsid protein (1566) 1566
cell line (1482) 1482
protein conformation (1457) 1457
analysis (1351) 1351
mice (1282) 1282
virus diseases (1201) 1201
biotechnology & applied microbiology (1196) 1196
rna (1166) 1166
protein (1160) 1160
protein binding (1156) 1156
microbiology (1153) 1153
viral proteins (1127) 1127
research (1116) 1116
mutation (1108) 1108
research article (1075) 1075
virus assembly (1063) 1063
dna (1013) 1013
biophysics (984) 984
cell biology (980) 980
article (967) 967
phylogeny (925) 925
identification (922) 922
infection (921) 921
virus (894) 894
multidisciplinary sciences (857) 857
expression (848) 848
health aspects (821) 821
genome, viral (794) 794
binding sites (773) 773
capsid (770) 770
rna, viral - genetics (770) 770
capsid - ultrastructure (760) 760
cryoelectron microscopy (720) 720
protein structure, tertiary (718) 718
viral proteins - genetics (717) 717
replication (715) 715
sequence alignment (707) 707
binding (704) 704
virus replication (688) 688
coat protein (687) 687
in-vitro (683) 683
capsid proteins - immunology (661) 661
female (658) 658
viral proteins - chemistry (657) 657
genomes (642) 642
gene expression (638) 638
sequence homology, amino acid (630) 630
cloning, molecular (626) 626
viral proteins - metabolism (618) 618
rna, viral - metabolism (612) 612
capsid - immunology (608) 608
infectious diseases (606) 606
sequence (591) 591
escherichia-coli (588) 588
genetic aspects (571) 571
crystallography, x-ray (570) 570
kinetics (570) 570
microscopy, electron (568) 568
capsids (567) 567
biology (563) 563
antibodies (554) 554
rna, viral - chemistry (548) 548
cells (544) 544
dna, viral - genetics (544) 544
virus-like particles (543) 543
particles (537) 537
sequence analysis, dna (535) 535
genes, viral (533) 533
immunology (533) 533
nucleic acid conformation (533) 533
nucleotide-sequence (521) 521
crystal-structure (519) 519
protein structure, secondary (515) 515
genetic vectors (503) 503
structure and assembly (501) 501
resolution (499) 499
life sciences (492) 492
infections (491) 491
peptides (479) 479
genetics & heredity (469) 469
vaccines (464) 464
gene (463) 463
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (12584) 12584
Japanese (66) 66
Chinese (65) 65
Russian (27) 27
German (5) 5
French (4) 4
Czech (2) 2
Hungarian (2) 2
Polish (1) 1
Spanish (1) 1
Swedish (1) 1
Ukrainian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


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
Journal Article
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
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 2004, Volume 32, Issue 17, pp. 5260 - 5279
Journal Article
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
Journal Article
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
Journal Article
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
Journal Article
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
Journal Article
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
Journal Article
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
Journal Article