Glycosylation within the Cystein loop and six residues near conserved Cys192/Cys193 are determinants of neuronal bungarotoxin sensitivity on the neuronal nicotinic receptor α3 subunit

Molecular Pharmacology

Volumn 53, Issue 6, 1998, Pages 1112-1119

  Luetje, Charles W ^a   Maddox, Floyd N ^a   Harvey, Scott C ^a,b  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^b ELI LILLY AND COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BUNGAROTOXIN; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT; RECEPTOR SUBUNIT; CYSTEINE;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; GLYCOSYLATION; NEUROTRANSMISSION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; XENOPUS LAEVIS; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; DRUG EFFECT; FEMALE; MOLECULAR GENETICS; NERVE CELL; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; BUNGAROTOXINS; CYSTEINE; FEMALE; GLYCOSYLATION; MOLECULAR SEQUENCE DATA; NEURONS; RECEPTORS, NICOTINIC; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS LAEVIS;

EID: 0031595989     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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