Alternatively spliced forms in the cytoplasmic domain of the human Growth Hormone (GH) receptor regulate its ability to generate a soluble GH-binding protein

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 20, 1996, Pages 10723-10728

  Dastot, Florence ^a   Sobrier, Marie Laure ^a   Duquesnoy, Philippe ^a   Duriez, Bénédicte ^a   Goossens, Michel ^a   Amselem, Serge ^a  

^a HENRI MONDOR HOSPITAL   (France)

Author keywords

Cytokine receptor; Shedding

Indexed keywords

BINDING PROTEIN; COMPLEMENTARY DNA; CYTOKINE RECEPTOR; GROWTH HORMONE BINDING PROTEIN; GROWTH HORMONE RECEPTOR; MESSENGER RNA;

ALTERNATIVE RNA SPLICING; ANIMAL CELL; ARTICLE; CYTOPLASM; GENE EXPRESSION REGULATION; HUMAN; HUMAN TISSUE; NONHUMAN; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SPECIES DIFFERENCE;

ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CARRIER PROTEINS; CERCOPITHECUS AETHIOPS; COS CELLS; HUMANS; MEMBRANE PROTEINS; MICE; MOLECULAR SEQUENCE DATA; RABBITS; RATS; RECEPTORS, SOMATOTROPIN; RNA, MESSENGER; SOLUBILITY; TISSUE DISTRIBUTION;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0029780688     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.20.10723     Document Type: Article

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