The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization
Open accessAbstract
Complementary DNA clones encoding the human kidney epidermal growth factor (EGF) precursor have been isolated and sequenced. They predict the sequence of a 1,207 amino acid protein which contains EGF flanked by polypeptide segments of 970 and 184 residues at its NH2- and COOH-termini, respectively. The structural organization of the human EGF precursor is similar to that previously described for the mouse protein and there is 66% identity between the two sequences. Transfection of COS-7 cells with the human EGF precursor cDNA linked to the SV40 early promoter indicate that it can be synthesized as a membrane protein with its NH2-terminus external to the cell surface. The human EGF precursor gene is approximately 110 kilobase pairs and has 24 exons. Its exon-intron organization revealed that various domains of the EGF precursor are encoded by individual exons. Moreover, 15 of the 24 exons encode protein segments that are homologous to sequences in other proteins. Exon duplication and shuffling appear to have played an important role in determining the present structure of this protein.
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Cites
Ny, T., Elgh, F., & Lund, B. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.17.5355 · Cited by 299
Cited by
Arriza, J. L., Weinberger, C., Cerelli, G., Glaser, T. M., Handelin, B. L., Housman, D. E., & Evans, R. M. (1987) · Science · doi:10.1126/science.3037703 · Cited by 1,946
Sinha, A., Nightingale, J. M. D., West, K. P., Berlanga-Acosta, J., & Playford, R. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013136 · Cited by 303
Rutledge, B. J., Zhang, K., Bier, E., Jan, Y. N., & Perrimon, N. (1992) · Genes & Development · doi:10.1101/gad.6.8.1503 · Cited by 274
Primary structure of the human follistatin precursor and its genomic organization
Shimasaki, S., Koga, M., Esch, F., Cooksey, K., Mercado, M., Koba, A., Ueno, N., Ying, S. Y., Ling, N., & Guillemin, R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4218 · Cited by 232
Periplasmic chaperones used to enhance functional secretion of proteins in E. coli
Schlapschy, M., & Skerra, A. (2011) · Methods in Molecular Biology · doi:10.1007/978-1-61737-967-3_12 · Cited by 40
Metadata
- Authors
- Bell, G. I., Fong, N. M., Stempien, M. M., Wormsted, M. A., Caput, D., Ku, L., Urdea, M. S., Rall, L. B., & Sanchez-Pescador, R.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1986
- Volume
- 14
- Issue
- 21
- Pages
- 8427-8446
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W1993797874
- Cited by
- 317
- References
- 1
- FWCI
- 11.19
- Type
- journal article
- Language
- en
- Open access
- green
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