Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK).
about
Regulation of the catalytic activity of the human phosphatase PTPN4 by its PDZ domainPost-translational modifications modulate ligand recognition by the third PDZ domain of the MAGUK protein PSD-95DoReMi: context-based prioritization of linear motif matchesThe impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95.Supertertiary structure of the synaptic MAGuK scaffold proteins is conservedEnergy exchange network of inter-residue interactions within a thermally fluctuating protein molecule: A computational study.Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled receptor 30 (GPR30), an estrogen receptor that can be identified in hippocampal dendritic spines.Plasticity of PDZ domains in ligand recognition and signaling.Ligand binding by PDZ domains.The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains.Structures and target recognition modes of PDZ domains: recurring themes and emerging pictures.Understanding the effect of alternative splicing in the folding and function of the second PDZ from protein tyrosine phosphatase-BL.A complex affair: Attraction and repulsion make occludin and ZO-1 function!Pyk2 modulates hippocampal excitatory synapses and contributes to cognitive deficits in a Huntington's disease model.Common features in the unfolding and misfolding of PDZ domains and beyond: the modulatory effect of domain swapping and extra-elements.Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity.Site-Specific Phosphorylation of PSD-95 PDZ Domains Reveals Fine-Tuned Regulation of Protein-Protein Interactions.NOMA-GAP/ARHGAP33 regulates synapse development and autistic-like behavior in the mouse.
P2860
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P2860
Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK).
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@ast
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@en
type
label
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@ast
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@en
prefLabel
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@ast
Phosphorylation of a PDZ domai ...... ated guanylate kinase (MAGUK).
@en
P2093
P2860
P356
P1476
Phosphorylation of a PDZ domai ...... iated guanylate kinase (MAGUK)
@en
P2093
Andrew L Lee
Chad M Petit
David S King
P2860
P304
41776-41785
P356
10.1074/JBC.M111.272583
P407
P50
P577
2011-09-30T00:00:00Z