Addition of an N-terminal dimerization domain promotes assembly of hCG analogs: Implications for subunit combination and structure-function analysis

Molecular and Cellular Endocrinology

Volumn 152, Issue 1-2, 1999, Pages 91-98

  Lin, Win ^a   Ransom, Mark X ^a   Myers, Rebecca V ^a   Bernard, Michael P ^a   Moyle, William R ^a  

^a UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

Author keywords

Dimerization domain; FSH receptor; Glycoprotein hormone; hCG analogs; LH receptor; Subunit combination

Indexed keywords

AMINO ACID; CHORIONIC GONADOTROPIN; FOLLITROPIN; FOLLITROPIN RECEPTOR; LUTEINIZING HORMONE; LUTEINIZING HORMONE RECEPTOR;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CHIMERA; DIMERIZATION; ENZYME IMMUNOASSAY; GENE MUTATION; HORMONE ACTION; HORMONE STRUCTURE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; CHORIONIC GONADOTROPIN; DIMERIZATION; FEMALE; HUMANS; MOLECULAR SEQUENCE DATA; PREGNANCY; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, LH; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0033603467     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(99)00056-8     Document Type: Article

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