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Times Cited: 289
Times Cited: 289
Times Cited
Times Co-cited
Similarity
Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator.
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Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer.
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Structural basis of the activation of a metabotropic GABA receptor.
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Distinct roles of metabotropic glutamate receptor dimerization in agonist activation and G-protein coupling.
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Structure of human GABAB receptor in an inactive state.
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Heptahelical domain of metabotropic glutamate receptor 5 behaves like rhodopsin-like receptors.
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Closed state of both binding domains of homodimeric mGlu receptors is required for full activity.
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Activation and allosteric modulation of a muscarinic acetylcholine receptor.
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Interdomain movements in metabotropic glutamate receptor activation.
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Investigating metabotropic glutamate receptor 5 allosteric modulator cooperativity, affinity, and agonism: enriching structure-function studies and structure-activity relationships.
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A new approach to analyze cell surface protein complexes reveals specific heterodimeric metabotropic glutamate receptors.
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Crystal structure of the µ-opioid receptor bound to a morphinan antagonist.
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Overlapping binding sites drive allosteric agonism and positive cooperativity in type 4 metabotropic glutamate receptors.
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Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer.
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Molecular mechanism of positive allosteric modulation of the metabotropic glutamate receptor 2 by JNJ-46281222.
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Illuminating the activation mechanisms and allosteric properties of metabotropic glutamate receptors.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.