PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions (Q34730310)

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English	PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions	scientific article

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scholarly article

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Europe PubMed Central

4 August 2017

PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions (English)

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Europe PubMed Central

4 August 2017

G protein-coupled receptor

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Thor C Møller

1

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Karen L Martinez

object named as

Karen L Martinez

10

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object named as

Anders Bach

5

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Jan M. Deussing

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Jan M Deussing

8

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Kristian Strømgaard

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Kristian Strømgaard

7

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Thue W Schwartz

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Thue W Schwartz

9

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Volker F Wirth

2

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Europe PubMed Central

4 August 2017

Nina I Roberts

3

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Europe PubMed Central

4 August 2017

Julia Bender

4

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Europe PubMed Central

4 August 2017

Birgitte P S Jacky

6

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Europe PubMed Central

4 August 2017

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publication date

14 May 2013

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Europe PubMed Central

4 August 2017

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Europe PubMed Central

4 August 2017

8

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Europe PubMed Central

4 August 2017

5

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Europe PubMed Central

4 August 2017

e63352

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Europe PubMed Central

4 August 2017

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Creative Commons Attribution 4.0 International

14 May 2013

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April 2022 Public Data File from Crossref

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3653948/fullTextXML

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Single-synapse analysis of a diverse synapse population: proteomic imaging methods and markers

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Transient protein-protein interactions: structural, functional, and network properties

1 reference

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Deciphering the kinetic binding mechanism of dimeric ligands using a potent plasma-stable dimeric inhibitor of postsynaptic density protein-95 as an example.

1 reference

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GPCR interacting proteins (GIPs) in the nervous system: Roles in physiology and pathologies

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Fine-tuning of GPCR activity by receptor-interacting proteins

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Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density

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The relative binding affinities of PDZ partners for CFTR: a biochemical basis for efficient endocytic recycling

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Residence time of receptor-ligand complexes and its effect on biological function

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Interaction of brain somatostatin receptors with the PDZ domains of PSD-95

1 reference

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The PDZ domain as a complex adaptive system

1 reference

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PDZ domain binding selectivity is optimized across the mouse proteome

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PDZ domains: folding and binding

1 reference

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Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability

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Uncovering quantitative protein interaction networks for mouse PDZ domains using protein microarrays

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The kinetics of PDZ domain-ligand interactions and implications for the binding mechanism

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P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2

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GPCR interacting proteins (GIP).

1 reference

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The PDZ-binding domain is essential for the dendritic targeting of 5-HT2A serotonin receptors in cortical pyramidal neurons in vitro.

1 reference

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A direct interaction of PSD-95 with 5-HT2A serotonin receptors regulates receptor trafficking and signal transduction

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Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95

1 reference

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Seven-transmembrane receptors

1 reference

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Association of the kinesin superfamily motor protein KIF1Balpha with postsynaptic density-95 (PSD-95), synapse-associated protein-97, and synaptic scaffolding molecule PSD-95/discs large/zona occludens-1 proteins

1 reference

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Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach

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Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102

1 reference

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beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors

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Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering

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CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90

1 reference

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95

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Design and synthesis of highly potent and plasma-stable dimeric inhibitors of the PSD-95-NMDA receptor interaction

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N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4.

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Two conserved residues govern the salt and pH dependencies of the binding reaction of a PDZ domain.

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Somatostatin receptor subtype 1 is a PDZ ligand for synapse-associated protein 97 and a potential regulator of growth cone dynamics.

1 reference

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Modified peptides as potent inhibitors of the postsynaptic density-95/N-methyl-D-aspartate receptor interaction

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0063352

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Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization.

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Glutamatergic and dopaminergic neurons mediate anxiogenic and anxiolytic effects of CRHR1.

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Identifiers

10.1371/JOURNAL.PONE.0063352

1 reference

Europe PubMed Central

4 August 2017

2013PLoSO...863352M

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1 reference

Europe PubMed Central

4 August 2017

1 reference

Europe PubMed Central

4 August 2017

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