Cystine knot mutations affect the folding of the glycoprotein hormone α-subunit. Differential secretion and assembly of partially folded intermediates

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 15413-15421

  Darling, Ryan J ^a   Ruddon, Raymond W ^a,b,c   Perini, Fulvio ^a   Bedows, Elliott ^a,b  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^c 986805 Nebraska Medical Center ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CHORIONIC GONADOTROPIN BETA SUBUNIT; CYSTEINE; CYSTINE;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; HORMONE RELEASE; HORMONE STRUCTURE; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

ALANINE; AMINO ACID SUBSTITUTION; CELL LINE; CYSTEINE; CYSTINE; DISULFIDES; DITHIOTHREITOL; GLYCOPROTEIN HORMONES, ALPHA SUBUNIT; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; TRANSFECTION;

ANIMALIA;

EID: 0034686019     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.20.15413     Document Type: Article

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