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Journal Article
Nature, ISSN 0028-0836, 09/2017, Volume 549, Issue 7670, pp. 60 - 65
AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-subtype ionotropic glutamate receptors mediate fast excitatory neurotransmission throughout... 
ELECTRON CRYOMICROSCOPY | ACTIVATION | ACID | TERMINAL DOMAIN | CRYOELECTRON MICROSCOPY | CRYSTAL-STRUCTURE | DESENSITIZATION | MULTIDISCIPLINARY SCIENCES | SEIZURE CONTROL | MEMBRANE-PROTEINS | HIPPOCAMPAL-NEURONS | Calcium Channels - metabolism | Humans | Protein Subunits - agonists | Receptors, AMPA - chemistry | Models, Molecular | Rats | Receptors, AMPA - ultrastructure | Protein Subunits - metabolism | Synaptic Transmission | Cryoelectron Microscopy | Animals | Claudins - metabolism | Receptors, AMPA - agonists | HEK293 Cells | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Mice | Protein Subunits - antagonists & inhibitors | Protein Subunits - chemistry | Ion Channel Gating | Receptors, AMPA - antagonists & inhibitors | Physiological aspects | Glutamate | Neural transmission | Channel opening | Membranes | Desensitization | Synaptic strength | Glutamic acid receptors (ionotropic) | Channel gating | Propionic acid | Central nervous system | Ions | Glutamic acid receptors | Selectivity | Hydrophobicity | Electron microscopy | α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors | Neurological diseases | Proteins | Signal transduction | Signaling | Receptors | Neurotransmitters | Transmission electron microscopy | α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid | Ion channels | Neurotransmission | Index Medicus
Journal Article
Pflügers Archiv - European Journal of Physiology, ISSN 0031-6768, 4/2011, Volume 461, Issue 4, pp. 461 - 468
Low-voltage-activated CaV3 Ca2+ channels have an activation threshold around −60 mV, which is lower than the activation threshold of other voltage-dependent... 
Voltage dependence | Biomedicine | Human Physiology | Voltage gating | T-type calcium channel | Activation kinetics | Gating current | Channel pores | Calcium channels | Kinetics | Mutation | Channel gating | Calcium channels (voltage-gated)
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2007, Volume 104, Issue 41, pp. 16365 - 16370
The cystic fibrosis transmembrane conductance regulator (CFTR) is a Cl⁻ channel gated by ATP-driven nucleotide-binding domain (NBD) dimerization. Here we... 
Complementary DNA | Humans | Homologous recombination | Cystic fibrosis | Mice | Dimers | Chimeras | Kinetics | CHO cells | Dimerization | Chloride ion channel | ATP-binding cassette transporter | Rate-equilibrium free-energy relationships | Recombinational cloning | WILD-TYPE | CELLS | NUCLEOTIDE-BINDING DOMAINS | MECHANISM | rate-equilibrium free-energy relationships | MULTIDISCIPLINARY SCIENCES | ADENYLATE KINASE-ACTIVITY | CL-CHANNELS | recombinational cloning | chloride ion channel | TRANSMEMBRANE-CONDUCTANCE-REGULATOR | CLONING | cystic fibrosis | CYSTIC-FIBROSIS | MUTATIONS | Cystic Fibrosis Transmembrane Conductance Regulator - antagonists & inhibitors | Protein Structure, Tertiary | Diphosphates - pharmacology | Species Specificity | Cystic Fibrosis - metabolism | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | Recombinant Fusion Proteins - chemistry | Cystic Fibrosis Transmembrane Conductance Regulator - chemistry | Recombinant Fusion Proteins - metabolism | Adenosine Triphosphate - pharmacology | Recombinant Fusion Proteins - antagonists & inhibitors | Animals | Cystic Fibrosis - genetics | Recombinant Fusion Proteins - genetics | Cystic Fibrosis Transmembrane Conductance Regulator - genetics | In Vitro Techniques | Binding Sites | Ion Channel Gating | Cystic Fibrosis - drug therapy | Ions | Membranes | Behavior | Chlorine | Adenosine triphosphatase | Index Medicus | Biological Sciences
Journal Article
Journal Article