Charged residues in the M2 region of α-hENaC play a role in channel conductance

American Journal of Physiology - Cell Physiology

Volumn 278, Issue 2 47-2, 2000, Pages

  Langloh, Anne Lynn B ^a   Berdiev, Bakhrom ^a   Ji, Hong Long ^a   Keyser, Kent ^b   Stanton, Bruce A ^c   Benos, Dale J ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^c DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

Biotinylation; Channel pore; Confocal microscopy; Dual electrode voltage clamp; Green fluorescent protein; Planar lipid bilayers; Site directed mutagenesis; Xenopus oocytes

Indexed keywords

AMILORIDE; COMPLEMENTARY DNA; GREEN FLUORESCENT PROTEIN; RNA; SODIUM ION;

ANIMAL CELL; ARTICLE; BIOTINYLATION; CONFOCAL LASER MICROSCOPY; ELECTRODE; LIPID BILAYER; MEMBRANE CHANNEL; MEMBRANE CONDUCTANCE; NONHUMAN; OOCYTE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; VOLTAGE CLAMP; XENOPUS LAEVIS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0034055926     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.2000.278.2.c277     Document Type: Article

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