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Science, ISSN 0036-8075, 9/2010, Volume 329, Issue 5996, pp. 1175 - 1180
Recent reports of increased tolerance to artemisinin derivatives—the most recently adopted class of antimalarials— have prompted a need for new treatments. The... 
Malaria | Artemisinins | RESEARCH ARTICLES | Genomics | Adenosine triphosphatases | Antimalarials | Parasites | Inhibitory concentration 50 | Drug resistance | Dosage | Genetic mutation | VIVAX | MULTIDISCIPLINARY SCIENCES | PARASITE PLASMODIUM-FALCIPARUM | ERADICATION | CALCIUM-PUMP | DRUG-RESISTANCE | SARCOPLASMIC-RETICULUM | ANTIMALARIALS | IDENTIFICATION | CHLOROQUINE | ARTEMISININ | Parasitic Sensitivity Tests | Humans | Male | Plasmodium falciparum - drug effects | Indoles - administration & dosage | Plasmodium falciparum - genetics | Protein Synthesis Inhibitors - pharmacology | Mutant Proteins - antagonists & inhibitors | Antimalarials - pharmacokinetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Rats | Spiro Compounds - pharmacokinetics | Adenosine Triphosphatases - antagonists & inhibitors | Antimalarials - administration & dosage | Malaria - parasitology | Adenosine Triphosphatases - genetics | Mice | Mutation | Erythrocytes - parasitology | Plasmodium berghei - drug effects | Plasmodium vivax - growth & development | Protein Synthesis Inhibitors - chemistry | Rats, Wistar | Spiro Compounds - administration & dosage | Genes, Protozoan | Protozoan Proteins - genetics | Protein Synthesis Inhibitors - administration & dosage | Protozoan Proteins - metabolism | Female | Indoles - pharmacology | Protozoan Proteins - chemistry | Drug Resistance | Spiro Compounds - chemistry | Cell Line | Plasmodium vivax - drug effects | Mutant Proteins - metabolism | Drug Discovery | Protozoan Proteins - biosynthesis | Antimalarials - pharmacology | Protein Synthesis Inhibitors - pharmacokinetics | Animals | Mutant Proteins - chemistry | Antimalarials - chemistry | Adenosine Triphosphatases - chemistry | Indoles - pharmacokinetics | Malaria - drug therapy | Plasmodium falciparum - growth & development | Indoles - chemistry | Spiro Compounds - pharmacology | Research | Pharmacology | Inhibitor drugs | Drug therapy | Protein synthesis | Drugs | Mutations | Nanomaterials | Encoding | Cations | Nanostructure | Ablation | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 508, Issue 7497, pp. 550 - 553
Journal Article
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7659, pp. 504 - 509
ABCG2 is a constitutively expressed ATP-binding cassette (ABC) transporter that protects many tissues against xenobiotic molecules. Its activity affects the... 
BINDING CASSETTE TRANSPORTER | PHOSPHOLIPID-BILAYER NANODISCS | STEROL TRANSPORTER | PARTICLE ELECTRON CRYOMICROSCOPY | RESISTANCE PROTEIN BCRP/ABCG2 | MULTIDISCIPLINARY SCIENCES | EM STRUCTURE DETERMINATION | CRYO-EM | MONOCLONAL-ANTIBODY | MEMBRANE-PROTEINS | P-GLYCOPROTEIN | Immunoglobulin Fab Fragments - ultrastructure | Antibodies - chemistry | Humans | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - metabolism | Cholesterol - chemistry | Biological Transport | Antibodies - immunology | Protein Domains | Adenosine Triphosphatases - ultrastructure | Binding Sites | Amino Acid Sequence | Neoplasm Proteins - ultrastructure | Adenosine Triphosphatases - metabolism | Antibodies - ultrastructure | Models, Molecular | Neoplasm Proteins - chemistry | Cholesterol - metabolism | Cryoelectron Microscopy | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - antagonists & inhibitors | Immunoglobulin Fab Fragments - chemistry | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - chemistry | Polymorphism, Single Nucleotide - genetics | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - ultrastructure | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Immunoglobulin Fab Fragments - immunology | Physiological aspects | Binding proteins | Observations | Drug interactions | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2013, Volume 110, Issue 24, pp. 9710 - 9715
ABCB10 is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria. In mammals ABCB10 is essential for... 
ATP binding cassette transporters | Proteins | Crystals | Adenosine triphosphatases | Lipids | Nucleotides | Exporters | Binding sites | Monomers | Crystal structure | X-ray crystallography | Nucleotide complex | Abc mitochondrial erythroid | Cardiolipin | Human membrane protein structure | COMPLEX | nucleotide complex | MECHANISM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOCHONDRIA | HYDROLYSIS | cardiolipin | ABC mitochondrial erythroid | P-GLYCOPROTEIN | MITOFERRIN-1 | RESISTANCE | human membrane protein structure | PROTEINS | REVEALS | Humans | Molecular Conformation | Molecular Sequence Data | Crystallography, X-Ray | Nucleotides - chemistry | ATP-Binding Cassette Transporters - chemistry | Sf9 Cells | ATP-Binding Cassette Transporters - genetics | Adenosine Triphosphate - metabolism | ATP-Binding Cassette Transporters - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Adenosine Triphosphatases - metabolism | Models, Molecular | Binding Sites - genetics | Phosphatidylcholines - chemistry | Nucleotides - metabolism | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Mutation | Adenosine Triphosphate - chemistry | Phosphatidylethanolamines - chemistry | Biological transport, Active | Physiological aspects | Research | Binding proteins | Structure | Health aspects | Adenosine triphosphate | Oxidative stress | Mitochondria | ABC transporters | Index Medicus | Biological Sciences
Journal Article
Science, ISSN 0036-8075, 6/2012, Volume 336, Issue 6087, pp. 1448 - 1451
Journal Article
Molecular Cell, ISSN 1097-2765, 2008, Volume 29, Issue 2, pp. 169 - 179
The ATPase RIG-I senses viral RNAs that contain 5′-triphosphates in the cytoplasm. It initiates a signaling cascade that activates innate immune response by... 
RNA | MOLIMMUNO | RESPONSES | HELICASE LGP2 | VIRUS | ACID | REPLICATION | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIVIRAL INNATE IMMUNITY | HOST | IDENTIFICATION | ADAPTER PROTEIN | CELL BIOLOGY | RNA Caps - immunology | RNA Helicases - metabolism | Zinc - metabolism | Humans | rab GTP-Binding Proteins - genetics | Structure-Activity Relationship | RNA Helicases - chemistry | Interferons - immunology | RNA Caps - metabolism | Zinc - chemistry | Adenosine Triphosphatases - immunology | Interferon-Induced Helicase, IFIH1 | RNA, Viral - genetics | Immunity, Innate - physiology | RNA Caps - chemistry | Zinc - immunology | RNA Helicases - genetics | RNA, Viral - metabolism | Interferons - genetics | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Dimerization | RNA Caps - genetics | rab GTP-Binding Proteins - metabolism | Cell Line | DEAD Box Protein 58 | Adenosine Triphosphatases - metabolism | Protein Structure, Tertiary - genetics | Binding Sites - genetics | Substrate Specificity - genetics | Polyphosphates - metabolism | DEAD-box RNA Helicases - genetics | Animals | RNA, Viral - chemistry | Polyphosphates - immunology | rab GTP-Binding Proteins - immunology | DEAD-box RNA Helicases - immunology | Interferons - metabolism | Adenosine Triphosphatases - chemistry | RNA, Viral - immunology | rab GTP-Binding Proteins - chemistry | Adenosine Triphosphatases - genetics | Structural Homology, Protein | RNA Helicases - immunology | Polyphosphates - chemistry | Sensors | G proteins | Biological response modifiers | Adenosine triphosphatase | Index Medicus
Journal Article
Journal Article
Nature, ISSN 0028-0836, 10/2017, Volume 550, Issue 7677, pp. 539 - 542
Chromatin-remodelling factors change nucleosome positioning and facilitate DNA transcription, replication, and repair(1). The conserved remodelling factor... 
TRANSLOCATION | COMPLEX | PROTEIN | MULTIDISCIPLINARY SCIENCES | BIOLOGY | RECOMBINANT HISTONES | CHROMODOMAIN | MECHANISMS | CONTAINS | CHD1 | BINDING | Nucleosomes - chemistry | Saccharomyces cerevisiae - ultrastructure | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphatases - ultrastructure | Nucleosomes - ultrastructure | Saccharomyces cerevisiae Proteins - ultrastructure | Adenosine Triphosphatases - metabolism | Chromatin Assembly and Disassembly | Models, Molecular | Nucleosomes - metabolism | DNA - metabolism | DNA-Binding Proteins - chemistry | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Enzyme Activation | Histones - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Physiological aspects | Chromatin | Gene expression | Observations | Yeast | Transcription | Saccharomyces | DNA-directed RNA polymerase | Mimicry | DNA helicase | Proteins | Catalysis | Serrated yielding | Deoxyribonucleic acid--DNA | Binding | Translocation | Superhelical DNA | Ratcheting | Electron microscopy | Chromatin remodeling | Gyres | Lobes | DNA biosynthesis | Polymerase | Histone H4 | Ribonucleic acids | Loosening | Saccharomyces cerevisiae | Binding sites | Adenosine triphosphatase | RNA polymerase II | Pluripotency | Index Medicus
Journal Article
Journal Article
Science, ISSN 0036-8075, 10/2011, Volume 334, Issue 6054, pp. 380 - 385
The ability of electrospray to propel large viruses into a mass spectrometer is established and is rationalized by analogy to the atmospheric transmission of... 
Protons | Pumping | Vapor phases | REPORTS | Adenosine triphosphatases | Lead | Lipids | Mass spectroscopy | Dimers | Nucleotides | Mass spectra | ATP SYNTHESIS | NA+-ATPASE | ENTEROCOCCUS-HIRAE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MACROMOLECULAR ASSEMBLIES | THERMOPHILUS H+-ATPASE/SYNTHASE | PERIPHERAL STALK | ROTOR RING | THERMUS-THERMOPHILUS | VACUOLAR ATPASE | Protein Multimerization | Bacterial Proteins - chemistry | Vacuolar Proton-Translocating ATPases - metabolism | Protein Subunits - metabolism | Enterococcus - enzymology | Spectrometry, Mass, Electrospray Ionization | Adenosine Triphosphate - metabolism | Mass Spectrometry | Membrane Lipids - analysis | Binding Sites | Protein Structure, Tertiary | Thermus thermophilus - enzymology | Phosphatidylethanolamines - analysis | Adenosine Triphosphatases - metabolism | Models, Molecular | Cardiolipins - metabolism | Hydrolysis | Cardiolipins - analysis | Vacuolar Proton-Translocating ATPases - chemistry | Hydrophobic and Hydrophilic Interactions | Membrane Lipids - metabolism | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Protein Subunits - chemistry | Phosphatidylethanolamines - metabolism | Physiological aspects | Identification and classification | Mass spectrometry | Methods | Adenosine triphosphatase | Binding sites | Index Medicus
Journal Article