Asn-linked glycosylation contributes to surface expression and voltage-dependent gating of Cav1.2 Ca2+ channel

Journal of Microbiology and Biotechnology

Volumn 25, Issue 8, 2015, Pages 1371-1379

  Park, Hyun Jee ^a   Min, Se Hong ^a   Won, Yu Jin ^a   Lee, Jung Ha ^a  

^a Sogang University   (South Korea)

Author keywords

Cav1.2 Ca2+ channel; N glycosylation; Point mutation; Voltage clamping; Xenopus oocyte

Indexed keywords

ASPARAGINE; CALCIUM CHANNEL; CALCIUM CHANNEL CAV1.2; TUNICAMYCIN; UNCLASSIFIED DRUG; CALCIUM CHANNEL L TYPE; L-TYPE CALCIUM CHANNEL ALPHA(1C);

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CALCIUM CURRENT; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; GLYCOSYLATION; MUTATIONAL ANALYSIS; NONHUMAN; OOCYTE; POINT MUTATION; PROTEIN EXPRESSION; SURFACE PROPERTY; XENOPUS; ANIMAL; BIOPHYSICS; DNA MUTATIONAL ANALYSIS; GENETICS; METABOLISM; MISSENSE MUTATION; PROTEIN PROCESSING; RABBIT;

ORYCTOLAGUS CUNICULUS;

ANIMALS; BIOPHYSICAL PHENOMENA; CALCIUM CHANNELS, L-TYPE; DNA MUTATIONAL ANALYSIS; GLYCOSYLATION; MUTATION, MISSENSE; POINT MUTATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RABBITS; XENOPUS;

EID: 84940186847     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1501.01066     Document Type: Article

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