[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP).
TISSUE=Brain;
PubMed=2166337 [NCBI, ExPASy, EBI, Israel, Japan]
Keinaenen K.,
Wisden W.,
Sommer B.,
Werner P.,
Herb A.,
Verdoorn T.A.,
Sakmann B.,
Seeburg P.H.;
"A family of AMPA-selective glutamate receptors.";
Science 249:556-560(1990).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
PubMed=2168579 [NCBI, ExPASy, EBI, Israel, Japan]
Boulter J.,
Hollmann M.,
O'Shea-Greenfield A.,
Hartley M.,
Deneris E.S.,
Maron C.,
Heinemann S.F.;
"Molecular cloning and functional expression of glutamate receptor subunit genes.";
Science 249:1033-1037(1990).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
TISSUE=Brain cortex, and Hippocampus;
DOI=10.1016/0896-6273(90)90212-X; PubMed=1699567 [NCBI, ExPASy, EBI, Israel, Japan]
Nakanishi N.,
Schneider N.A.,
Axel R.;
"A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties.";
Neuron 5:569-581(1990).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND FUNCTION.
STRAIN=Sprague-Dawley;
PubMed=9351977 [NCBI, ExPASy, EBI, Israel, Japan]
Everts I.,
Villmann C.,
Hollmann M.;
"N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation.";
Mol. Pharmacol. 52:861-873(1997).
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[5]
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SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NSF, IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB, AND MUTAGENESIS OF 851-ASN-PRO-852.
DOI=10.1016/S0896-6273(00)80518-8; PubMed=9697855 [NCBI, ExPASy, EBI, Israel, Japan]
Osten P.,
Srivastava S.,
Inman G.J.,
Vilim F.S.,
Khatri L.,
Lee L.M.,
States B.A.,
Einheber S.,
Milner T.A.,
Hanson P.I.,
Ziff E.B.;
"The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs.";
Neuron 21:99-110(1998).
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[6]
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INTERACTION WITH PRKCABP.
DOI=10.1016/S0896-6273(00)80689-3; PubMed=10027300 [NCBI, ExPASy, EBI, Israel, Japan]
Xia J.,
Zhang X.,
Staudinger J.,
Huganir R.L.;
"Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1.";
Neuron 22:179-187(1999).
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[7]
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ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
PubMed=1699275 [NCBI, ExPASy, EBI, Israel, Japan]
Sommer B.,
Keinaenen K.,
Verdoorn T.A.,
Wisden W.,
Burnashev N.,
Herb A.,
Koehler M.,
Takagi T.,
Sakmann B.,
Seeburg P.H.;
"Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.";
Science 249:1580-1585(1990).
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[8]
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PHOSPHORYLATION AT SER-683 AND SER-717.
DOI=10.1016/0168-0102(95)00977-9; PubMed=8848293 [NCBI, ExPASy, EBI, Israel, Japan]
Nakazawa K.,
Tadakuma T.,
Nokihara K.,
Ito M.;
"Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696.";
Neurosci. Res. 24:75-86(1995).
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[9]
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INTERACTION WITH GRIP1.
TISSUE=Hippocampus;
DOI=10.1038/386279a0; PubMed=9069286 [NCBI, ExPASy, EBI, Israel, Japan]
Dong H.,
O'Brien R.J.,
Fung E.T.,
Lanahan A.A.,
Worley P.F.,
Huganir R.L.;
"GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors.";
Nature 386:279-284(1997).
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[10]
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INTERACTION WITH GRIP2.
PubMed=10414981 [NCBI, ExPASy, EBI, Israel, Japan]
Wyszynski M.,
Valtschanoff J.G.,
Naisbitt S.,
Dunah A.W.,
Kim E.,
Standaert D.G.,
Weinberg R.,
Sheng M.;
"Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo.";
J. Neurosci. 19:6528-6537(1999).
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[11]
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IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
DOI=10.1016/S0896-6273(03)00722-0; PubMed=14687553 [NCBI, ExPASy, EBI, Israel, Japan]
Kolleker A.,
Zhu J.J.,
Schupp B.J.,
Qin Y.,
Mack V.,
Borchardt T.,
Koehr G.,
Malinow R.,
Seeburg P.H.,
Osten P.;
"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors.";
Neuron 40:1199-1212(2003).
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[12]
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PHOSPHORYLATION AT TYR-876, AND TISSUE SPECIFICITY.
DOI=10.1523/JNEUROSCI.0799-04.2004; PubMed=15240807 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T.,
Huganir R.L.;
"Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases.";
J. Neurosci. 24:6152-6160(2004).
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[13]
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SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2.
DOI=10.1074/jbc.M600679200; PubMed=16793768 [NCBI, ExPASy, EBI, Israel, Japan]
Bedoukian M.A.,
Weeks A.M.,
Partin K.M.;
"Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics.";
J. Biol. Chem. 281:23908-23921(2006).
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[14]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE.
DOI=10.1038/27692; PubMed=9804426 [NCBI, ExPASy, EBI, Israel, Japan]
Armstrong N.,
Sun Y.,
Chen G.Q.,
Gouaux E.;
"Structure of a glutamate-receptor ligand-binding core in complex with kainate.";
Nature 395:913-917(1998).
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[15]
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X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC.
DOI=10.1016/S0896-6273(00)00094-5; PubMed=11086992 [NCBI, ExPASy, EBI, Israel, Japan]
Armstrong N.,
Gouaux E.;
"Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core.";
Neuron 28:165-181(2000).
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[16]
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X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH QUISQUALATE, AND FUNCTION.
DOI=10.1021/bi020583k; PubMed=12501192 [NCBI, ExPASy, EBI, Israel, Japan]
Jin R.,
Horning M.,
Mayer M.L.,
Gouaux E.;
"Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate.";
Biochemistry 41:15635-15643(2002).
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[17]
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X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA AND BR-HIBO.
DOI=10.1016/S0022-2836(02)00650-2; PubMed=12215417 [NCBI, ExPASy, EBI, Israel, Japan]
Hogner A.,
Kastrup J.S.,
Jin R.,
Liljefors T.,
Mayer M.L.,
Egebjerg J.,
Larsen I.K.,
Gouaux E.;
"Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core.";
J. Mol. Biol. 322:93-109(2002).
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[18]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; DNQX AND KAINATE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-504 AND ASN-775.
DOI=10.1038/417245a; PubMed=12015593 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Y.,
Olson R.,
Horning M.,
Armstrong N.,
Mayer M.,
Gouaux E.;
"Mechanism of glutamate receptor desensitization.";
Nature 417:245-253(2002).
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[19]
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X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA AND ZINC IONS.
DOI=10.1021/jm021020+; PubMed=12593667 [NCBI, ExPASy, EBI, Israel, Japan]
Lunn M.-L.,
Hogner A.,
Stensboel T.B.,
Gouaux E.,
Egebjerg J.,
Kastrup J.S.;
"Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity.";
J. Med. Chem. 46:872-875(2003).
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[20]
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X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH WILLARDIINES, AND FUNCTION.
DOI=10.1038/nn1091; PubMed=12872125 [NCBI, ExPASy, EBI, Israel, Japan]
Jin R.,
Banke T.G.,
Mayer M.L.,
Traynelis S.F.,
Gouaux E.;
"Structural basis for partial agonist action at ionotropic glutamate receptors.";
Nat. Neurosci. 6:803-810(2003).
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[21]
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X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; KAINATE AND QUISQUALATE, AND FUNCTION.
DOI=10.1073/pnas.1037393100; PubMed=12730367 [NCBI, ExPASy, EBI, Israel, Japan]
Armstrong N.,
Mayer M.,
Gouaux E.;
"Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.";
Proc. Natl. Acad. Sci. U.S.A. 100:5736-5741(2003).
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[22]
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X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ANIRACETAM AND CX614, AND FUNCTION.
DOI=10.1523/JNEUROSCI.2567-05.2005; PubMed=16192394 [NCBI, ExPASy, EBI, Israel, Japan]
Jin R.,
Clark S.,
Weeks A.M.,
Dudman J.T.,
Gouaux E.,
Partin K.M.;
"Mechanism of positive allosteric modulators acting on AMPA receptors.";
J. Neurosci. 25:9027-9036(2005).
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[23]
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X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 AND KAINATE, AND FUNCTION.
DOI=10.1124/mol.104.002931; PubMed=15591246 [NCBI, ExPASy, EBI, Israel, Japan]
Frandsen A.,
Pickering D.S.,
Vestergaard B.,
Kasper C.,
Nielsen B.B.,
Greenwood J.R.,
Campiani G.,
Fattorusso C.,
Gajhede M.,
Schousboe A.,
Kastrup J.S.;
"Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2.";
Mol. Pharmacol. 67:703-713(2005).
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[24]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2006.08.037; PubMed=17018279 [NCBI, ExPASy, EBI, Israel, Japan]
Armstrong N.,
Jasti J.,
Beich-Frandsen M.,
Gouaux E.;
"Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.";
Cell 127:85-97(2006).
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[25]
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X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND S1209, AND FUNCTION.
DOI=10.1016/j.jmb.2006.01.024; PubMed=16483599 [NCBI, ExPASy, EBI, Israel, Japan]
Kasper C.,
Pickering D.S.,
Mirza O.,
Olsen L.,
Kristensen A.S.,
Greenwood J.R.,
Liljefors T.,
Schousboe A.,
Waetjen F.,
Gajhede M.,
Sigurskjold B.W.,
Kastrup J.S.;
"The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209.";
J. Mol. Biol. 357:1184-1201(2006).
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