Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
1R01NS035534-01
Application #
2274802
Study Section
Neurological Sciences Subcommittee 1 (NLS)
Project Start
1996-09-15
Project End
1999-07-31
Budget Start
1996-09-15
Budget End
1997-07-31
Support Year
1
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Saint Louis University
Department
Pharmacology
Type
Schools of Medicine
DUNS #
City
Saint Louis
State
MO
Country
United States
Zip Code
63103
Kucenas, S; Li, Z; Cox, J A et al. (2003) Molecular characterization of the zebrafish P2X receptor subunit gene family. Neuroscience 121:935-45
Diaz-Hernandez, Miguel; Cox, Jane A; Migita, Keisuke et al. (2002) Cloning and characterization of two novel zebrafish P2X receptor subunits. Biochem Biophys Res Commun 295:849-53
Haines, W R; Migita, K; Cox, J A et al. (2001) The first transmembrane domain of the P2X receptor subunit participates in the agonist-induced gating of the channel. J Biol Chem 276:32793-8
Migita, K; Haines, W R; Voigt, M M et al. (2001) Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor. J Biol Chem 276:30934-41
Haines, W R; Voigt, M M; Migita, K et al. (2001) On the contribution of the first transmembrane domain to whole-cell current through an ATP-gated ionotropic P2X receptor. J Neurosci 21:5885-92
Cox, J A; Barmina, O; Voigt, M M (2001) Gene structure, chromosomal localization, cDNA cloning and expression of the mouse ATP-gated ionotropic receptor P2X5 subunit. Gene 270:145-52
Egan, T M; Cox, J A; Voigt, M M (2000) Molecular cloning and functional characterization of the zebrafish ATP-gated ionotropic receptor P2X(3) subunit. FEBS Lett 475:287-90
Haines, W R; Torres, G E; Voigt, M M et al. (1999) Properties of the novel ATP-gated ionotropic receptor composed of the P2X(1) and P2X(5) isoforms. Mol Pharmacol 56:720-7
Torres, G E; Egan, T M; Voigt, M M (1999) Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners. J Biol Chem 274:6653-9
Torres, G E; Egan, T M; Voigt, M M (1998) N-Linked glycosylation is essential for the functional expression of the recombinant P2X2 receptor. Biochemistry 37:14845-51

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