Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH2-terminal nucleotide binding domain

Journal of General Physiology

Volumn 116, Issue 2, 2000, Pages 163-180

  Chan, K W ^a   Csanady, L ^a   Seto Young, D ^a   Nairn, A C ^a   Gadsby, D C ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Adenosine triphosphate binding cassette transporter; Chloride channel; Coimmunoprecipitation; Domain structure; Gating kinetics

Indexed keywords

CALCIUM CHANNEL; CHLORIDE CHANNEL; TRANSMEMBRANE CONDUCTANCE REGULATOR;

AMINO ACID SEQUENCE; ARTICLE; CHANNEL GATING; CYSTIC FIBROSIS; HUMAN; MEMBRANE CONDUCTANCE; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE;

ADENOSINE MONOPHOSPHATE; ANIMALS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; ENDOPLASMIC RETICULUM; EPITOPES; FEMALE; GENE DELETION; GENE EXPRESSION; ION CHANNEL GATING; KINETICS; MEMBRANE POTENTIALS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OOCYTES; PATCH-CLAMP TECHNIQUES; PEPTIDE FRAGMENTS; PEPTIDES; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFECTION; XENOPUS LAEVIS;

EID: 0033886092     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.116.2.163     Document Type: Article

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