Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
5R01NS031557-12
Application #
6799992
Study Section
Molecular, Cellular and Developmental Neurosciences 2 (MDCN)
Program Officer
Stewart, Randall R
Project Start
1993-04-01
Project End
2005-08-31
Budget Start
2004-09-01
Budget End
2005-08-31
Support Year
12
Fiscal Year
2004
Total Cost
$269,500
Indirect Cost
Name
Duke University
Department
Pharmacology
Type
Schools of Medicine
DUNS #
044387793
City
Durham
State
NC
Country
United States
Zip Code
27705
Chapman, Mark L; Blanke, Marie L; Krovetz, Howard S et al. (2006) Allosteric effects of external K+ ions mediated by the aspartate of the GYGD signature sequence in the Kv2.1 K+ channel. Pflugers Arch 451:776-92
Grigston, Jeffrey C; VanDongen, Hendrika M A; McNamara 3rd, James O et al. (2005) Translation of an integral membrane protein in distal dendrites of hippocampal neurons. Eur J Neurosci 21:1457-68
Chapman, Mark L; VanDongen, Antonius M J (2005) K channel subconductance levels result from heteromeric pore conformations. J Gen Physiol 126:87-103
VanDongen, Antonius M J (2004) Idealization and simulation of single ion channel data. Methods Enzymol 383:229-44
Kalbaugh, Trisha L; VanDongen, Hendrika M A; VanDongen, Antonius M J (2004) Ligand-binding residues integrate affinity and efficacy in the NMDA receptor. Mol Pharmacol 66:209-19
VanDongen, Antonius M J (2004) K channel gating by an affinity-switching selectivity filter. Proc Natl Acad Sci U S A 101:3248-52
McNamara 2nd, James O; Grigston, Jeffrey C; VanDongen, Hendrika M A et al. (2004) Rapid dendritic transport of TGN38, a putative cargo receptor. Brain Res Mol Brain Res 127:68-78
Jones, Kevin S; VanDongen, Hendrika M A; VanDongen, Antonius M J (2002) The NMDA receptor M3 segment is a conserved transduction element coupling ligand binding to channel opening. J Neurosci 22:2044-53
Chapman, M L; Krovetz, H S; VanDongen, A M (2001) GYGD pore motifs in neighbouring potassium channel subunits interact to determine ion selectivity. J Physiol 530:21-33
Wood, M W; VanDongen, H M; VanDongen, A M (1999) A mutation in the glycine binding pocket of the N-methyl-D-aspartate receptor NR1 subunit alters agonist efficacy. Brain Res Mol Brain Res 73:189-92

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