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Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7613, pp. 556 - 560
Interruption of combination antiretroviral therapy in HIV-1-infected individuals leads to rapid viral rebound. Here we report the results of a phase IIa open... 
POTENT | REPLICATION | GENETIC-DETERMINANTS | BROADLY NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | PASSIVE TRANSFER | SEQUENCE | CD4 BINDING | ANTIRETROVIRAL THERAPY | INFECTION | MONOCLONAL-ANTIBODIES | Anti-HIV Agents - pharmacology | Antibodies, Neutralizing - administration & dosage | Disease Reservoirs - virology | Humans | Middle Aged | Male | Proviruses - immunology | Anti-HIV Agents - administration & dosage | Tissue Distribution | Young Adult | HIV Infections - immunology | Proviruses - drug effects | Antibodies, Neutralizing - immunology | HIV-1 - growth & development | HIV Antibodies - immunology | HIV Envelope Protein gp160 - chemistry | Time Factors | Antibodies, Neutralizing - therapeutic use | Binding Sites - immunology | Adult | Anti-HIV Agents - therapeutic use | Female | HIV Antibodies - therapeutic use | Historically Controlled Study | Binding Sites - drug effects | HIV Envelope Protein gp160 - metabolism | Drug Administration Schedule | HIV-1 - drug effects | HIV Infections - virology | HIV Antibodies - administration & dosage | Viral Load - immunology | Proviruses - growth & development | HIV-1 - immunology | HIV Envelope Protein gp160 - antagonists & inhibitors | Adolescent | HIV Infections - drug therapy | Aged | HIV Envelope Protein gp160 - immunology | Viral Load - drug effects | CD4 Antigens - metabolism | Prevention | Antiviral agents | HIV antibodies | Dosage and administration | Host-virus relationships | Drug therapy, Combination | Drug therapy | Health aspects | HIV infection | Methods | Clinical trials | Antiretroviral drugs | Immunoglobulins | Human immunodeficiency virus--HIV | Binding sites | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 513, Issue 7519, pp. 517 - 522
The ribosome is a molecular machine responsible for protein synthesis and a major target for small-molecule inhibitors. Compared to the wealth of structural... 
CRYPTOPLEURINE RESISTANCE | AMARYLLIDACEAE ALKALOIDS | SACCHAROMYCES-CEREVISIAE MUTANTS | NUCLEOTIDE RESOLUTION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | PEPTIDE-BOND FORMATION | TRANSLATION INITIATION | TRANSFER-RNA | PROTEIN-SYNTHESIS | AMINOGLYCOSIDE ANTIBIOTICS | Eukaryotic Cells - chemistry | Protein Synthesis Inhibitors - chemistry | Molecular Weight | Species Specificity | Ribosomes - metabolism | Substrate Specificity | Crystallography, X-Ray | Molecular Targeted Therapy | RNA, Messenger - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Base Sequence | Macrolides - pharmacology | RNA, Transfer - genetics | Protein Synthesis Inhibitors - pharmacology | Binding Sites - drug effects | Eukaryotic Cells - enzymology | Peptidyl Transferases - metabolism | RNA, Transfer - metabolism | Ribosome Subunits, Large, Eukaryotic - chemistry | Peptidyl Transferases - chemistry | RNA, Messenger - genetics | Ribosomes - chemistry | Models, Molecular | Drug Resistance - drug effects | Peptide Chain Elongation, Translational - drug effects | Piperidones - pharmacology | Cycloheximide - pharmacology | Saccharomyces cerevisiae - chemistry | Eukaryotic Cells - drug effects | Ribosomes - drug effects | Ribosome Subunits, Large, Eukaryotic - drug effects | Kinetics | Eukaryotes | Analysis | Ribosomes | Ribonucleoproteins | Research | Health aspects | Transfer RNA | Proteins | Yeast | Peptides | Antibiotics | Protein synthesis | Bacteria | Drug resistance | Binding sites | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 05/2016, Volume 534, Issue 7606, pp. 272 - 276
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2012, Volume 109, Issue 35, pp. 13961 - 13965
We report the high-resolution (1.9 Å) crystal structure of oligomycin bound to the subunit c₁₀ ring of the yeast mitochondrial ATP synthase. Oligomycin binds... 
Protons | Molecules | Yeasts | Atomic interactions | Adenosine triphosphatases | Crystals | Atoms | Genetic mutation | Oligomycins | Binding sites | Proton pore | F1Fo ATP synthase | VENTURICIDIN | RESISTANT MUTANTS | MULTIDISCIPLINARY SCIENCES | AMINO-ACID SUBSTITUTIONS | ADENOSINE-TRIPHOSPHATASE | MITOCHONDRIAL ATPASE | SACCHAROMYCES-CEREVISIAE | SUBUNIT-9 | PARTIAL RESOLUTION | proton pore | INHIBITORS | CATALYZING OXIDATIVE PHOSPHORYLATION | Mitochondria - enzymology | Humans | Crystallography, X-Ray | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Oligomycins - pharmacology | Hydrogen Bonding - drug effects | ATP Synthetase Complexes - metabolism | Drug Design | ATP Synthetase Complexes - chemistry | Binding Sites - drug effects | Escherichia coli - enzymology | Protein Structure, Secondary | Bacterial Proton-Translocating ATPases - chemistry | Bacterial Proton-Translocating ATPases - metabolism | Escherichia coli Proteins - metabolism | Mitochondria - drug effects | Proton-Translocating ATPases - chemistry | Animals | Mycobacterium tuberculosis - enzymology | Vacuolar Proton-Translocating ATPases - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Anti-Bacterial Agents - pharmacology | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Clinical chemistry | Antibiotics | Yeast fungi | Physiological aspects | Microbiological chemistry | Chemical properties | Research | Structure | Identification and classification | Adenosine triphosphate | Protein binding | Bacteria | Yeast | Adenosine triphosphatase | Crystal structure | Index Medicus | Biological Sciences | Physical Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2012, Volume 109, Issue 27, pp. 10984 - 10989
Aminoglycosides are potent antibacterials, but therapy is compromised by substantial toxicity causing, in particular, irreversible hearing loss. Aminoglycoside... 
Deafness | Antibacterials | Antibiotics | Protein synthesis | Hair cells | Drug interactions | Ribosomes | Glycosides | Aminoglycosides | Inhibitory concentration 50 | Misreading | Antibiotic | Translation | Mycobacteria | antibiotic | SITE | TRANSLOCATION | ANTIBIOTICS | RNA | MULTIDISCIPLINARY SCIENCES | 30S RIBOSOMAL-SUBUNIT | TOXICITY | mycobacteria | INDUCED HEARING-LOSS | HAIR-CELLS | misreading | translation | RESISTANCE | deafness | SELECTIVITY | Humans | Nebramycin - toxicity | Bacteria - drug effects | Protein Biosynthesis - physiology | Ribosomes - metabolism | Gentamicins - toxicity | Drug Design | HEK293 Cells | Anti-Bacterial Agents - toxicity | Binding Sites - drug effects | Organ Culture Techniques | Rabbits | Guinea Pigs | Nebramycin - chemistry | Bacterial Infections - drug therapy | Ribosomes - chemistry | Deafness - physiopathology | Mitochondria - metabolism | Mitochondria - drug effects | Pseudomonas aeruginosa - drug effects | Nebramycin - analogs & derivatives | Mycobacterium - drug effects | Hair Cells, Auditory - drug effects | Animals | Reticulocytes - cytology | Aminoglycosides - toxicity | Ribosomes - drug effects | Protein Biosynthesis - drug effects | Mice | Mutagenesis - physiology | Staphylococcus aureus - drug effects | Deafness - chemically induced | Physiological aspects | Development and progression | Health aspects | Hearing loss | Bacteria | Drug resistance | Ribonucleic acid--RNA | Toxicity | Rodents | Index Medicus | Biological Sciences
Journal Article
Nature, ISSN 0028-0836, 04/2016, Volume 532, Issue 7599, pp. 334 - 339
The serotonin transporter (SERT) terminates serotonergic signalling through the sodium-and chloride-dependent reuptake of neurotransmitter into presynaptic... 
HIGH-AFFINITY RECOGNITION | NEUROTRANSMITTER TRANSPORTERS | NOREPINEPHRINE TRANSPORTERS | N-LINKED GLYCOSYLATION | ALLOSTERIC BINDING | BACTERIAL HOMOLOG | MULTIDISCIPLINARY SCIENCES | BINDING-SITE | SELECTIVE RECOGNITION | MEMBRANE-PROTEINS | DOPAMINE TRANSPORTER | Citalopram - pharmacology | Humans | Protein Conformation - drug effects | Crystallography, X-Ray | Dopamine Plasma Membrane Transport Proteins - chemistry | Structure-Activity Relationship | Antidepressive Agents - metabolism | Citalopram - metabolism | Serotonin Plasma Membrane Transport Proteins - chemistry | Extracellular Space - metabolism | Antidepressive Agents - chemistry | Protein Binding - drug effects | Drug Design | Antidepressive Agents - pharmacology | Protein Stability | Allosteric Regulation - drug effects | Ions - chemistry | Serotonin Plasma Membrane Transport Proteins - immunology | Allosteric Site - drug effects | Models, Molecular | Ions - metabolism | Paroxetine - metabolism | Serotonin Plasma Membrane Transport Proteins - metabolism | Citalopram - chemistry | Intracellular Space - metabolism | Serotonin - metabolism | Ligands | Immunoglobulin Fab Fragments - immunology | Paroxetine - pharmacology | Paroxetine - chemistry | Drug metabolism | Paroxetine | Physiological research | Research | Serotonin | Binding sites (Biochemistry) | X rays | Mutation | Antidepressants | Binding sites | Index Medicus
Journal Article