PDZ domains and the organization of supramolecular complexes.
By M. Sheng, C. Sala. Annual Review of Neuroscience, 2001
1,245 citations recorded by the source corpus.
Subfields: Cell Biology, Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/fe05c78100a64e893030312f1f3fa541e6669577
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In Cell Biology
In Cellular and Molecular Neuroscience
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Citations in the corpus
- Visual transduction in Drosophila (2001, background): “Named after PSD-95 (postsynaptic density protein), Drosophila discs large ( dlg ), and the tight-junction protein ZO-1, PDZ domains are protein modules of about 90 amino acids that bind to a variety of target proteins by means of specific target sequences, such as an S/T-X-V/I motif in the final t”
- Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling (2002, background): “2) also suggests that RGS4 and certain other RGS proteins may bind directly to GPCRs to form a stable ternary complex between the GPCR, G q, PLC , and CaM (for discussion, see Sierra et al., 2000).”
- Dentritic spines : structure, dynamics and regulation (2001, background): “cgi?l=59312">Shank , are believed to organize the PSD and to represent a molecular interface between glutamate receptors in the synaptic membrane and the spine cytoskeleto”
- Functional dynamics of PDZ binding domains: a normal-mode analysis. (2005, background): “j DðjR~ib;jbjÞðjr ~ib;jbj jR~ib;jbjÞ2; (2)”
- Subunit-specific temporal and spatial patterns of AMPA receptor exocytosis in hippocampal neurons (2001, background): “PDZ proteins are widely implicated in targeting, anchoring and/or trafficking of their membrane protein binding partner”
- Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “PDZ-proteins are considered to be one of the major determinants of postsynaptic localization of various proteins (711).”