PDZ domain proteins of synapses

By Eunjoon Kim, M. Sheng. Nature Reviews Neuroscience, 2004

1,677 citations recorded by the source corpus.

Subfields: Cell Biology, Cellular and Molecular Neuroscience

View Paper: https://www.semanticscholar.org/paper/be77207516561cb38c9d34c475a44e7fb02845fd

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. T. Sūdhof
2. Karel Svoboda
3. M. Sheng
4. R. Malenka
5. Anthony Holtmaat
6. S. Harrison

In Cellular and Molecular Neuroscience

1. T. Sūdhof
2. Karel Svoboda
3. A. Citri
4. Anthony Holtmaat
5. R. Malenka
6. M. Sheng
7. Noah W. Gray
8. Robby M. Weimer

Citations in the corpus

• Synaptic Plasticity: Multiple Forms, Functions, and Mechanisms (2008, background): “Prominent members of the MAGUK family of PSD proteins include PSD-95, SAP97, PSD-93, and SAP102 (Kim and Sheng, 2004; Montgomery et al, 2004).”
• Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. (2010, neutral): “The organization of NRs within the PSD is important for coordinated signal transduction (Kim and Sheng, 2004).”
• Experience-dependent structural synaptic plasticity in the mammalian brain (2009, background): “For example, PSD-95 is an abundant multi-domain postsynaptic scaffolding protein that clusters glutamate receptors and organizes the associated signalling complexe”
• Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “The PDZ-proteins are known to bind various molecules such as glutamate receptors and Kv channels and target them to postsynaptic sites (99, 109, 370, 555, 710).”
• Central Sensitization: A Generator of Pain Hypersensitivity by Central Neural Plasticity (2009, neutral): “The prime binding protein for the MAGUK family is the NMDAR subunit NR2,155 but it also binds to the transmembrane AMPAR regulatory proteins (TARPs),43 nonreceptor tyrosine kinases,329 nNOS,30,31 GKAP,217 and AKAP79/150.53 MAGUKs can be seen as the functional scaffold of the PSD and are essential fo”
• Regulatory mechanisms of AMPA receptors in synaptic plasticity (2007, background): “The C termini also interact with scaffold proteins that bind signalling proteins (for example, kinases, phosphatases) as well as cytoskeletal proteins (for example, actin”
• Neuroligins determine synapse maturation and function. (2006, methodology): “…in contrast to GABAergic/ glycinergic synapses, contain multiple transsynaptic cell adhesion and signaling systems that interact with intracellular scaffolding proteins (Garner et al., 2002; Kim and Sheng, 2004; Li and Sheng, 2003; Montgomery et al., 2004; Scheiffele, 2003; Yamagata et al., 2003).”
• Distinct Roles of NR2A and NR2B Cytoplasmic Tails in Long-Term (2010, neutral): “The apparent contradiction can be explained by the fact that NR2B, in addition to forming part of a ligandgated channel, also has a long cytoplasmic tail that binds (directly or indirectly) to a variety of postsynaptic signaling molecules (Köhr et al., 2003; Kim and Sheng, 2004; Barria and Malinow, ”
• Molecular mechanisms of dendritic spine morphogenesis. (2006, background): “Scaffolds Although lacking catalytic domains, PSD scaffold proteins (such as PSD-95, Shank and Homer) can influence synapse development and spine morphogenesis, presumably by recruiting interacting proteins to postsynaptic sites [49].”
• Rapid Redistribution of Synaptic PSD-95 in the Neocortex In Vivo (2006, background): “family of multi-domain PDZ-domain scaffolding proteins [21].”
• NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders (2007, background): “PSD protein of 95 kDa ( PSD-95 ; also known as synapse-associated protein-90) and synapse-associated protein-102 ( SAP-102 ) are synaptic scaffolding proteins and members of the large PSD-95 family of modular PDZ-containing proteins that anchor NMDARs in the PSD (for a review, see Ref”