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pmid: 14766169
AMPA receptors are tetramers assembled as a dimer-of-dimers with a 2-fold rotational symmetry in their extracellular domains. Two papers in this issue of Neuron, by Horning and Mayer and Sobolevsky et al., provide complementary data that extend this view and highlight the role of dimers in channel gating.
Binding Sites, Protein Conformation, Neuroscience(all), Crystallography, X-Ray, Allosteric Regulation, Mutation, Animals, Humans, Receptors, AMPA, Dimerization, Ion Channel Gating, Cells, Cultured
Binding Sites, Protein Conformation, Neuroscience(all), Crystallography, X-Ray, Allosteric Regulation, Mutation, Animals, Humans, Receptors, AMPA, Dimerization, Ion Channel Gating, Cells, Cultured
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 3 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |