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http://purl.uniprot.org/citations/11335724http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11335724http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11335724http://www.w3.org/2000/01/rdf-schema#comment"Whole cell voltage clamp recordings were performed to assess the ability of conantokin-G (con-G), conantokin-T (con-T), and a 17-residue truncated form of conantokin-R (con-R[1-17]) to inhibit N-methyl-d-aspartate (NMDA)-evoked currents in human embryonic kidney 293 cells transiently expressing various combinations of NR1a, NR1b, NR2A, and NR2B receptor subunits. Con-T and con-R[1-17] attenuated ion currents in cells expressing NR1a/NR2A or NR1a/NR2B. Con-G did not affect NMDA-evoked ionic currents in cells expressing NR1a/NR2A, but it showed inhibitory activity in cells expressing NR1a/NR2B receptors and the triheteromeric combination of NR1a/NR2A/NR2B. An Ala-rich con-G analog, con-G[Q6G/gamma7K/N8A/gamma10A/gamma14A/K15A/S16A/N17A] (Ala/con-G, where gamma is Gla), in which all nonessential amino acids were altered to Ala residues, manifested subunit specificity similar to that of con-G, suggesting that the replaced residues are not responsible for selectivity in the con-G framework. A sarcosine-containing con-T truncation analog, con-T[1-9/G1Src/Q6G], inhibited currents in NR1a/NR2A and NR1a/NR2B receptors, eliminating residues 10-21 as mediators of the broad subunit selectivity of con-T. In contrast to the null effects of con-G and Ala/con-G at a NR1a/NR2A-containing receptor, some inhibition ( approximately 40%) of NMDA-evoked currents was effected by these peptides in cells expressing NR1b/NR2A. This finding suggests that the presence of exon 5 in NR1b plays a role in the activity of the conantokins. Analysis of various conantokin analogs demonstrated that Leu(5) of con-G is an important determinant of conantokin selectivity. Taken as a whole, these results suggest that the important molecular determinants on conantokins responsible for NMDA receptor activity and specificity are discretely housed in specific residues of these peptides, thus allowing molecular manipulation of the NMDA receptor inhibitory properties of the conantokins."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m102428200"xsd:string
http://purl.uniprot.org/citations/11335724http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m102428200"xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Castellino F.J."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Castellino F.J."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Galdzicki Z."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Galdzicki Z."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Klein R.C."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Klein R.C."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Prorok M."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/author"Prorok M."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/pages"26860-26867"xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/pages"26860-26867"xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/title"The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-D-aspartate receptors."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/title"The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-D-aspartate receptors."xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11335724http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11335724http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11335724
http://purl.uniprot.org/citations/11335724http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11335724
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