Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM051172-11
Application #
2189504
Study Section
Physiology Study Section (PHY)
Project Start
1986-09-01
Project End
1997-11-30
Budget Start
1996-09-01
Budget End
1997-11-30
Support Year
11
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Yale University
Department
Pharmacology
Type
Schools of Medicine
DUNS #
082359691
City
New Haven
State
CT
Country
United States
Zip Code
06520
Huang, Chien-Jung; Schild, Laurent; Moczydlowski, Edward G (2012) Use-dependent block of the voltage-gated Na(+) channel by tetrodotoxin and saxitoxin: effect of pore mutations that change ionic selectivity. J Gen Physiol 140:435-54
Bian, S; Favre, I; Moczydlowski, E (2001) Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation. Proc Natl Acad Sci U S A 98:4776-81
Krishnan, G; Morabito, M A; Moczydlowski, E (2001) Expression and characterization of Flag-epitope- and hexahistidine-tagged derivatives of saxiphilin for use in detection and assay of saxitoxin. Toxicon 39:291-301
Huang, C J; Moczydlowski, E (2001) Cytoplasmic polyamines as permeant blockers and modulators of the voltage-gated sodium channel. Biophys J 80:1262-79
Favre, I; Moss, G W; Goldenberg, D P et al. (2000) Structure-activity relationships for the interaction of bovine pancreatic trypsin inhibitor with an intracellular site on a large conductance Ca(2+)-activated K(+) channel. Biochemistry 39:2001-12
Huang, C J; Favre, I; Moczydlowski, E (2000) Permeation of large tetra-alkylammonium cations through mutant and wild-type voltage-gated sodium channels as revealed by relief of block at high voltage. J Gen Physiol 115:435-54
Lenarcic, B; Krishnan, G; Borukhovich, R et al. (2000) Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases. J Biol Chem 275:15572-7
Favre, I; Moczydlowski, E (1999) Simultaneous binding of basic peptides at intracellular sites on a large conductance Ca2+-activated K+ channel. Equilibrium and kinetic basis of negatively coupled ligand interactions. J Gen Physiol 113:295-320
Favre, I; Sun, Y M; Moczydlowski, E (1999) Reconstitution of native and cloned channels into planar bilayers. Methods Enzymol 294:287-304
Moczydlowski, E (1998) Chemical basis for alkali cation selectivity in potassium-channel proteins. Chem Biol 5:R291-301

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