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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2007, Volume 104, Issue 49, pp. 19256 - 19261
Protein-protein recognition is the cornerstone of multiple cellular and pathological functions. Therefore, protein-protein interaction inhibition (2P2I) is... 
Molecules | Databases | Drug interactions | Molecular interactions | Libraries | Drug design | Goods and services tax | Viability | Chemicals | HIV 1 | Docking | NMR | Scoring function | Src homology 3 | COMPLEX | drug design | IMMUNODEFICIENCY-VIRUS | scoring function | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DRUG DISCOVERY | KINASE | PATHOGENESIS | docking | TYPE-1 NEF | HCK | BIOLOGY | SH3 DOMAIN | Anti-HIV Agents - pharmacology | Drug Evaluation, Preclinical - methods | Cercopithecus aethiops | nef Gene Products, Human Immunodeficiency Virus - chemistry | src Homology Domains - drug effects | Two-Hybrid System Techniques | Anti-HIV Agents - chemistry | Animals | Computer Simulation | nef Gene Products, Human Immunodeficiency Virus - antagonists & inhibitors | Drug Design | nef Gene Products, Human Immunodeficiency Virus - metabolism | Protein Conformation | Anti-HIV Agents - isolation & purification | COS Cells | Drugs | Control | Viral proteins | Physiological aspects | Influence | Genetic aspects | Product/Service Evaluations | HIV (Viruses) | Properties | Medical screening | Protein-protein interactions | Methods | Proteins | Biochemistry | Nuclear magnetic resonance--NMR | Human immunodeficiency virus--HIV | Index Medicus | Biochemistry, Molecular Biology | Anti-HIV Agents | src Homology Domains | Life Sciences | Drug Evaluation, Preclinical | nef Gene Products, Human Immunodeficiency Virus | Biological Sciences
Journal Article
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2018, Volume 430, Issue 16, pp. 2360 - 2371
The intrinsically disordered protein β-synuclein is known to inhibit the aggregation of its intrinsically disordered homolog, α-synuclein, which is implicated... 
protein–protein interactions | chimeras | Parkinson's disease | fluorescence | intrinsically disordered proteins | N-TERMINAL ACETYLATION | AMYLOID FORMATION | SEQUENCE DETERMINANTS | UNFOLDED PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein-protein interactions | CO-POLYMERIZATION | NMR | A-BETA | DYNAMICS | THIOFLAVIN-T-BINDING | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2013, Volume 8, Issue 3, pp. e59211 - e59211
Membrane fusion is the central molecular event during the entry of enveloped viruses into cells. The critical agents of this process are viral surface... 
NONINTEGRIN | HUMAN DENDRITIC CELLS | VIRUS-INFECTION | LIGAND-BINDING | PROTEIN | MECHANISM | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | CARBOHYDRATE-RECOGNITION | ENDOTHELIAL-CELLS | IDENTIFICATION | Cell Adhesion Molecules - chemistry | Humans | Lectins, C-Type - immunology | Crystallography, X-Ray | Cell Adhesion Molecules - immunology | Phylogeny | Lectins, C-Type - chemistry | Likelihood Functions | Epitopes, B-Lymphocyte - genetics | Dengue Virus - immunology | Receptors, Cell Surface - chemistry | Antibodies, Monoclonal - immunology | Amino Acid Sequence | Viral Envelope Proteins - genetics | Computational Biology | Models, Molecular | Dengue Virus - chemistry | Receptors, Cell Surface - immunology | Dengue - prevention & control | Protein Folding | Dengue Virus - genetics | Sequence Alignment | Protein Binding | Dengue - transmission | Models, Genetic | Dengue | Dengue viruses | Monoclonal antibodies | Amino acids | Health aspects | Protein-protein interactions | Integrins | Membranes | Laboratories | Viral diseases | Viruses | Infections | Biochemistry | Cell fusion | Tropical diseases | Proteins | Receptors | Endocytosis | Virions | Docking | Bioinformatics | Pharmaceutical sciences | Vector-borne diseases | Stress concentration | Carbohydrates | Encephalitis | Membrane fusion | Immunoglobulins | Dendritic cells | Dengue fever | Glycoprotein | Envelope protein | Glycoproteins | Glycosylation | DC-SIGN protein | Neural networks | Serotypes | Ligands | Force distribution | Molecular biology | Protein interaction | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2009, Volume 106, Issue 12, pp. 4665 - 4670
Journal Article
Assay and Drug Development Technologies, ISSN 1540-658X, 02/2019, Volume 17, Issue 2, pp. 58 - 67
The focal adhesion kinase-growth factor receptor 2 (FAK-Grb2) protein-protein interaction is implicated in pathogenesis of stress-induced cardiac hypertrophy.... 
FAT domain | Grb2-SH2 domain | pharmacophore modeling | pathological cardiac hypertrophy | virtual screening | protein-protein interaction inhibition
Journal Article
Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, 05/2019, Volume 37, Issue 8, pp. 1968 - 1991
Toll-like receptor 4 (TLR4) is a member of Toll-Like Receptors (TLRs) family that serves as a receptor for bacterial lipopolysaccharide (LPS). TLR4 alone... 
ADR: Adverse drug reaction | fs: femto seconds | ps: pico seconds | TLR4: Toll-like receptor 4 | protein-protein interactions (PPIs) | DTs: Drug transporters | TIR: Toll/IL-1 receptor like | RMSF: Root mean square fluctuation | API: Active pharmaceutical ingredient | NF-κB: Nuclear factor Kappa B | ECD: Extra cellular domain | CHARMM: Chemistry at HARvard macromolecular mechanics | RMSD: Root mean square deviation | PAMPs: Pathogen associated molecular patterns | Ro4: Rule of four | Toll-Like Receptor 4 (TLR4) | ns: nano seconds | PPIs: Protein-protein interactions | VMD: Visual molecular dynamics | MD: Molecular dynamics | ADMET: Absorption, distribution, metabolism, excretion and toxicity | NAMD: NAnoscale molecular dynamics | lipopolysaccharide (LPS) | hTLR4−MD-2 complex inhibitors | TLRs: Toll-like receptors | LRRs: Leucine rich repeats | LMWIs: Low molecular weight inhibitors | VS: Virtual screening | PRRs: Pattern recognition receptors | SMPPIIs: Small molecule protein-protein interaction inhibitors | TMD: Transmembrane domain | small molecule protein-protein interaction inhibitors (SMPPIIs) | LPS: LipoPolySaccharide | DMEs: Drug-metabolizing enzymes | DAMPs: Danger/damage associated molecular patterns | MDS: Molecular dynamics simulation | MD-2: Myeloid differentiation factor-2 | LE: Ligand efficiency | protein–protein interactions (PPIs) | small molecule protein–protein interaction inhibitors (SMPPIIs) | hTLR4-MD-2 complex inhibitors | TLR4 ANTAGONIST | BIOCHEMISTRY & MOLECULAR BIOLOGY | IL-1 receptor like | PREDICTION | HOT-SPOTS | metabolism | GENERAL FORCE-FIELD | DAMPs: Danger | FREE TOOL | DESIGN | damage associated molecular patterns | NF-B: Nuclear factor Kappa B | distribution | DRUG-METABOLIZING-ENZYMES | DISCOVERY | SMALL-MOLECULE INHIBITORS | excretion and toxicity | TIR: Toll | BIOPHYSICS | ADMET: Absorption | WEB SERVER
Journal Article
Current protocols in cell biology, 06/2019, Volume 83, Issue 1, p. e83
Protein-protein interactions (PPIs) are principle biological processes that control normal cell growth, differentiation, and homeostasis but are also crucial... 
Journal Article
Journal Article
European Journal of Medicinal Chemistry, ISSN 0223-5234, 04/2015, Volume 94, pp. 480 - 488
Journal Article
Journal Article
RSC Advances, ISSN 2046-2069, 2017, Volume 7, Issue 56, pp. 34963 - 34971
Egg-derived small peptides have various biological activities, including antioxidant properties. The Keap1-Nrf2 pathway is central to cell resistance to... 
UBIQUITINATION | OXIDATIVE STRESS | ACTIVATION | NRF2 | PATHWAY | SERUM-ALBUMIN | ANTIOXIDANT | PROTEIN-PROTEIN INTERACTION | KIDNEY 293 CELLS | IDENTIFICATION | CHEMISTRY, MULTIDISCIPLINARY
Journal Article