Asparagine rearrangements in two isoforms of erythropoietin receptor

Techniques in Protein Chemistry

Volumn 7, Issue C, 1996, Pages 109-119

  Derby, Patricia L ^a   Aoki, Kennneth H ^a   Katta, Viswanatham ^a   Rohde, Michael F ^a  

^a AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 33845475409     PISSN: 10808914     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1080-8914(96)80015-9     Document Type: Article

References (8)

1. Mayeaux P., Pallu S., Gobert S., Lacombe C., and Gisselbrecht S. Structure of the erythropoietin receptor. Proc. Soc. Exp. Biol. Med. 206 (1994) 200-204
2. Youssoufian H., Longmore G., Neumann D., Yoshimura A., and Lodish H.F. Structure, function, and activation of the erythropoietin receptor. Blood 81 (1993) 2223-2236
3. Longmore G.D., Watowich S.S., Hilson D.J., and Lodish H.F. The erythropoietin receptor: Its role in hematopoiesis and myeloproliferative diseases. J. Cell Biol 123 (1993) 1305-1308
4. Mayeaux P., Billat C., and Jacquot R. The erythropoietin receptor of the rat erythroid progenitor cells: Characterization and affinity cross-linking. J. Biol. Chem. 262 (1987) 13985-13990
5. D'Andrea A.D., Lodish H.F., and Wong G.G. Expression cloning of the erythropoietin receptor. Cell 52 (1989) 277-285
6. Stephenson R.C., and Clarke S. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 262 (1989) 6164-6170
7. Kwong M.Y., and Harris R.J. Identification of succinimide sites in proteins by N-terminal sequences analysis after alkaline hydroxylamine cleavage. Protein Sci. 3 (1994) 147-149
8. Tyler-Cross R., and Schirch V. Effects of amino acid sequence, buffers and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J. Biol. Chem. 266 (1991) 22549-22556