Allowed N-glycosylation sites on the Kv1.2 potassium channel S1-S2 linker: Implications for linker secondary structure and the glycosylation effect on channel function

Biochemical Journal

Volumn 375, Issue 3, 2003, Pages 769-775

  Zhu, Jing ^a   Watanabe, Itaru ^a   Poholek, Amanda ^a   Koss, Matthew ^a   Gomez, Barbara ^a   Yan, Chaowen ^a   Recio Pinto, Esperanza ^b   Thornhill, William B ^a  

^a FORDHAM UNIVERSITY   (United States)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Endoplasmic reticulum; Extracellular linker; N glycosylation; Voltage gated potassium channel

Indexed keywords

AMINO ACIDS; CARBOHYDRATES; CELL MEMBRANES; CONFORMATIONS; ENZYMES; ION EXCHANGE MEMBRANES; MUTAGENESIS;

ENDOPLASMIC RETICULUM; GLYCOSYLATION;

BIOCHEMISTRY;

CARBOHYDRATE; ION CHANNEL; MEMBRANE PROTEIN; POTASSIUM; VOLTAGE GATED POTASSIUM CHANNEL;

ANIMAL CELL; AQUEOUS SOLUTION; ARTICLE; BIOASSAY; BIOENGINEERING; CONFORMATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GLYCOSYLATION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BRAIN; CELL MEMBRANE; CHO CELLS; CRICETINAE; ENDOPLASMIC RETICULUM; GLYCOSYLATION; IMMUNOBLOTTING; KV1.1 POTASSIUM CHANNEL; KV1.2 POTASSIUM CHANNEL; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEIN STRUCTURE, SECONDARY; RATS;

ANIMALIA;

EID: 0242637036     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030517     Document Type: Article

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