References
- Topper Y. J., Freeman C. J. Multiple hormone interactions in the developmental biology of the mammary gland. Physiol. Rev. 1980; 16: 1049–1106
- Djiane J., Houdebine L. M., Kelly P. A. Prolactin like activity of anti prolactin receptor antibodies on casein and DNA synthesis in the mammary gland. Proc. Natl. Acad. Sci. USA 1981; 11: 7445–7448
- Katoh M., Djiane J., Kelly P. A. Prolactin binding components in rabbit mammary gland: characterization by partial purification and affinity Labelling. Endocrinology 1985; 116: 2612–2620
- Dusanter‐Fourt I., Djiane J., Houdebine L. M., Kelly P. A. In vivo lactogenic effects of anti‐prolactin receptor antibodies in pseudopregnant rabbits. Life Sci. 1983; 32: 407–412
- Katoh M., Djiane J., Kelly P. A. Monoclonal antibodies against rabbit mammary prolactin receptors. J. Biol. Chem. 1985; 260: 11422–11429
- Djiane J., Dusanter‐Fourt I., Katoh M., Kelly P. A. Biological activities of binding site specific monoclonal antibodies to prolactin receptors of rabbit mammary gland. J. Biol. Chem. 1985; 260: 11430–11436
- Gullick W. J., Tzartos J., Lindstrom J. Monoclonal antibodies as probes of acetylcholine receptor structure. Biochemistry 1981; 20: 2173–2180
- Reichman M. E., Foster C. M., Eisen L. P., Eisen H. J., Torain B. F., Simons S. S. Limited Proteolysis of Covalently Labeled Glucocorticoid Receptors as a Probe of Receptor Structure. Biochemistry 1984; 23: 5376–5384
- Chinkerst M., Brugge J. S. Characterization of structural domains of the human epidermal growth factor receptor obtained by partial proteolysis. J. Biol. Chem. 1984; 259: 11534–11542
- Hunter W. M., Greewood F. C. Preparation of iodine 131 labelled human growth hormone of high specific activity. Nature 1962; 194: 495–496
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
- Dusanter‐Fourt I., Kelly P. A., Djiane J. Immunological recognition of the prolactin receptor: identification of a single binding unit of M.W. 42,000. Biochimie 1987; 69: 639–646
- Pilcht P. F., Axelrod J. D., Colello J., Czech M. P. Unimpaired signal transduction by the adipocyte insulin receptor following its partial proteolytic fragmentation. J. Biol. Chem. 1981; 256: 1570–1575
- Fuchs S. Molecular aspects of experimental autoimmune myasteria gravis. J. Supramol. Struct. Suppl. 1980; 4: 117
- Hootman S. R., Picado‐Leonard T. M. Effect of proteolytic cleavage on functional properties of muscarinic acetylcholine receptors in rat pancreatic and parotid acinar cells. Biochem. J. 1985; 231: 617–622
- Strulovici B., Lefkowitz R. J. Activation, desensitization and recycling of frog erythrocyte b‐adrenergic receptors. J. Biol. Chem. 1984; 259: 4389–4395
- Seals J. R., Czech M. P. Evidence that insulin activates an intrinsic plasma membrane protease in generating a secondary chemical mediator. J. Biol. Chem. 1980; 255: 6529–6531
- Eisen L. P., Reichman M. E., Tompson E. B., Gametchu B., Harrison R. W., Eisen H. J. Monoclonal antibody to the rat glucocorticoid receptor. Relationship between the immunoreactive and DNA‐Binding domain. J. Biol. Chem. 1985; 260: 11805–11810
- Hubbard J. R., Barrett A. J., Kalimi M. Tosyl‐Lysyl chloromethane alters glucocorticoid‐receptor complex nuclear binding and physical properties. Endocrinology 1984; 155: 65–72
- Puca G. A., Abbondanza C., Nigro V., Armetta N. M., Medici N., Molinari A. M. Estradiol receptor has proteolytic activity that is responsible for its own transformation. Proc. Natl. Acad. Sci. 1986; 83: 5367–5371
- Boutin J. M., Jolicoeur C., Okamura H., Gagnon J., Edery M., Shirota M., Banville D., Dusanter‐Fourt I., Djiane J., Kelly P. A. Cloning and expression of the rat prolactin receptor, a member of the growth hormone/prolactin receptor gene family. Cell 1988; 53: 69–77
- Edery M., Jolicoeur C., Levi‐Meyrueis C., Dusanter‐Fourt I., Petridou B., Boutin J. M., Lesueur L., Kelly P. A., Djiane J. Identification and sequence analysis of a second form of prolactin receptor by molecular cloning of complementary DNA from rabbit mammary gland. Proc. Natl. Acad. Sci. USA 1989; 86: 2112–2116