Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
5R01NS023294-12
Application #
2264772
Study Section
General Medicine B Study Section (GMB)
Project Start
1992-07-01
Project End
1999-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Stanford University
Department
Biology
Type
Schools of Medicine
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
Brenner, R; Jegla, T J; Wickenden, A et al. (2000) Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4. J Biol Chem 275:6453-61
Middendorf, T R; Aldrich, R W; Baylor, D A (2000) Modification of cyclic nucleotide-gated ion channels by ultraviolet light. J Gen Physiol 116:227-52
Middendorf, T R; Aldrich, R W (2000) Effects of ultraviolet modification on the gating energetics of cyclic nucleotide-gated channels. J Gen Physiol 116:253-82
Horrigan, F T; Aldrich, R W (1999) Allosteric voltage gating of potassium channels II. Mslo channel gating charge movement in the absence of Ca(2+). J Gen Physiol 114:305-36
Kanevsky, M; Aldrich, R W (1999) Determinants of voltage-dependent gating and open-state stability in the S5 segment of Shaker potassium channels. J Gen Physiol 114:215-42
Ledwell, J L; Aldrich, R W (1999) Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J Gen Physiol 113:389-414
Ogielska, E M; Aldrich, R W (1999) Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation. J Gen Physiol 113:347-58
Horrigan, F T; Cui, J; Aldrich, R W (1999) Allosteric voltage gating of potassium channels I. Mslo ionic currents in the absence of Ca(2+). J Gen Physiol 114:277-304
Smith-Maxwell, C J; Ledwell, J L; Aldrich, R W (1998) Uncharged S4 residues and cooperativity in voltage-dependent potassium channel activation. J Gen Physiol 111:421-39
Ogielska, E M; Aldrich, R W (1998) A mutation in S6 of Shaker potassium channels decreases the K+ affinity of an ion binding site revealing ion-ion interactions in the pore. J Gen Physiol 112:243-57

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