Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs

@article{March1985CloningSA,
  title={Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs},
  author={Carl J. March and Bruce Mosley and Alf D. Larsen and Douglas Pat Cerretti and Gary Braedt and Virginia L. Price and Steven Gillis and Christopher S. Henney and Shirley R. Kronheim and Kenneth H. Grabstein and Paul J. Conlon and Thomas P Hopp and David J. Cosman},
  journal={Nature},
  year={1985},
  volume={315},
  pages={641-647}
}
Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-lα and IL-1β), were isolated from a macrophage cDNA library. The primary translation products of the genes are 271 and 269 amino acids long, although expression in Escherichia coli of the carboxy-terminal 159 and 153 amino acids produces IL-1 biological activity. 
Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist
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cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.
TLDR
A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells and the product of the cloned complementary DNA binds bothIL-1 alpha and IL-2 beta in a manner indistinguishable from that of the native T cell IL- 1 receptor.
Molecular cloning of the interleukin-1 beta converting enzyme.
Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA
Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1).
TLDR
The CSF-1 appears to be encoded by a single-copy gene, but its expression results in the synthesis of several messenger RNA species, ranging in size from about 1.5 to 4.5 kilobases.
Cloning and Characterization of an Alternatively Processed Human Type II Interleukin-1 Receptor mRNA*
TLDR
The purification and characterization of a soluble IL- 1 receptor expressed by COS1 cells and the cloning of an alternatively processed type II IL-1 receptor mRNA from both human and COS 1 cells are reported.
A chicken homolog of mammalian interleukin-1 beta: cDNA cloning and purification of active recombinant protein.
TLDR
Sequence homology and structural features indicate that this protein is the chicken homolog of mammalian interleukin-1beta (ChIL-1 beta), and northern blot analysis showed that ChIL- 1 beta RNA is quickly induced in blood monocyte-derived macrophages reaching maximal levels within one hour after onset of LPS treatment.
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  • Biology
    The Journal of experimental medicine
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TLDR
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