About: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density

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About: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density Goto Sponge NotDistinct Permalink

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scientific article (publication date: 2 May 1997)

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 1997 (ast) vědecký článek publikovaný v roce 1997 (cs) 1997 թվականի մայիսին հրատարակված գիտական հոդված (hy) 1997 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в травні 1997 (uk) vedecký článok (publikovaný 1997/05/02) (sk) مقالة علمية (نشرت في 2-5-1997) (ar) wetenschappelijk artikel (gepubliceerd op 1997/05/02) (nl) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Mai 1997 veröffentlichter wissenschaftlicher Artikel (de) scientific article (publication date: 2 May 1997) (en)
publication date	wds:Q28235849-B79CEA2F-8D6A-4671-BB7D-E8136DCDB49B
publication date	1997-05-02 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28235849-230EA33A-D5B3-4F1D-9141-FB571C4DCF90
language of work or name	English
cites work	wds:Q28235849-A78D3080-42BF-454F-B41A-B4AE1DC766BB
cites work	Growth of a rat neuroblastoma cell line in serum-free supplemented medium
author name string	wds:Q28235849-2D24F990-0989-420F-A063-F606DD50D54B wds:Q28235849-44FE3457-7012-4742-9BBC-402A202BCD72 wds:Q28235849-5B6465F9-E487-4740-B79B-7C6F35C96BC7 wds:Q28235849-A9612BF3-4613-4285-900D-B1CBD3DCD4ED wds:Q28235849-EF7E787B-0681-4817-B395-D4E3650B870D wds:Q28235849-FAF9E2C0-551F-4F35-B163-CF3FE0AC2B59
OpenCitations bibliographic resource ID	wds:Q28235849-6AF6B18D-CC64-42EF-85C1-EA04EEE38C5C
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/986367
author name string	A Toyoda M Takeuchi Y Takai M Irie Y Hata K Hirao
OpenCitations bibliographic resource ID	986367
rdfs:label	SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (en) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (nl) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (ast)
skos:prefLabel	SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (en) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (nl) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (ast)
name	SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (en) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (nl) SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (ast)
title	wds:Q28235849-B7E6028C-8A0A-416F-B9B4-A37C06F4B8FC
title	SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density (en)
page(s)	wds:Q28235849-6521156D-37E2-4F26-9C81-CFA3E7BEFB20
page(s)	11943-51
instance of	wds:Q28235849-8D2676BF-8C15-4991-9B88-FFD28917ADAC
instance of	scholarly article
PubMed ID	wds:Q28235849-2F4F262E-6F85-40D8-9514-708536C0681E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9115257
PubMed ID	9115257
published in	wds:Q28235849-872F6CC8-A537-4D24-A2EA-0093E1160FD1
published in	Journal of Biological Chemistry
issue	wds:Q28235849-F40900EA-33B3-4846-B049-8D4E07EB7092
volume	wds:Q28235849-CC03B222-C37E-4097-8392-88EAA6649A4F
issue	18
volume	272
DOI	wds:Q28235849-F12C330C-7360-4DB8-B2A8-5D3E268FFCDF
DOI	http://dx.doi.org/10.1074/JBC.272.18.11943
DOI	10.1074/JBC.272.18.11943
ResearchGate publication ID	wds:Q28235849-00479897-53DE-43FC-A822-DD8B10D89D71
ResearchGate publication ID	238315945
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28235849
is cites work of	Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton The APC-hDLG complex negatively regulates cell cycle progression from the G0/G1 to S phase Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses Synaptic PDZ domain-containing proteins. The protein-tyrosine phosphatase PTPMEG interacts with glutamate receptor delta 2 and epsilon subunits. Ligand binding of the second PDZ domain regulates clustering of PSD-95 with the Kv1.4 potassium channel Sapap3 deletion anomalously activates short-term endocannabinoid-mediated synaptic plasticity Sapap3 deletion causes mGluR5-dependent silencing of AMPAR synapses Circuit-selective striatal synaptic dysfunction in the Sapap3 knockout mouse model of obsessive-compulsive disorder Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs The calcium-independent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins A functional role of postsynaptic density-95-guanylate kinase-associated protein complex in regulating Shank assembly and stability to synapses Sevoflurane anesthesia in pregnant mice induces neurotoxicity in fetal and offspring mice Molecular mechanisms of glutamate receptor clustering at excitatory synapses. A novel two-site enzyme immunoassay reveals the regional distributions of and developmental changes in GluR1 and NMDAR1 protein contents in the rat brain. Autism-associated gene Dlgap2 mutant mice demonstrate exacerbated aggressive behaviors and orbitofrontal cortex deficits SAD-B kinase regulates pre-synaptic vesicular dynamics at hippocampal Schaffer collateral synapses and affects contextual fear memory. The cloning, genomic organization and tissue expression profile of the human DLG5 gene Characterization of PDZ-binding kinase, a mitotic kinase Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin Molecular cloning and characterization of the noncatalytic subunit of the Rab3 subfamily-specific GTPase-activating protein Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1 Recruitment of scribble to the synaptic scaffolding complex requires GUK-holder, a novel DLG binding protein A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia Craniofacial dysmorphogenesis including cleft palate in mice with an insertional mutation in the discs large gene hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions Localization of membrane-associated guanylate kinase (MAGI)-1/BAI-associated protein (BAP) 1 at tight junctions of epithelial cells An enhancer trap screen for ecdysone-inducible genes required for Drosophila adult leg morphogenesis nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM) Identification and characterization of a PDZ protein that interacts with activin type II receptors A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains

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