The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Primary structures of human alpha-fetoprotein and its mRNA.
Open accessAbstract
DNA complementary to human alpha-fetoprotein (AFP)mRNA was cloned in the plasmid pBR322. Analysis of three overlapping cDNA clones revealed most of the nucleotide sequence of AFP mRNA, and the remaining nucleotides at the 5' end of the mRNA were elucidated from a cloned genomic DNA fragment. The amino acid sequence was deduced from the nucleotide sequence, which revealed 19 amino acids in the signal sequence and 590 amino acids in mature AFP. There are 15 regularly spaced disulfide bridges, which generate a folding structure having three repeating domains. There is one potential N-glycosylation site, Asn-Phe-Thr, in the amino acid sequence. In comparison with mouse AFP, 66% of the amino acid sequence was conserved, with the highest identity (72%) in domain 3, followed by domain 2 (67%) and domain 1 (59%). In comparison with human albumin, a 39% conservation of primary structure was found. Again, the similarity was the highest in domain 3 and the lowest in domain 1. Human AFP and human albumin are similar in overall structure, but certain parts of the molecules differ significantly in their predicted secondary structure.
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The sequence of human serum albumin cDNA and its expression in E. coli
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Cited by
Hong, H., Branham, W. S., Dial, S. L., Moland, C. L., Fang, H., Shen, J., Perkins, R., Sheehan, D., & Tong, W. (2012) · Chemical Research in Toxicology · doi:10.1021/tx3003406 · Cited by 37
Metadata
- Authors
- Morinaga, T., Sakai, M., Wegmann, T. G., & Tamaoki, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1983-08
- Volume
- 80
- Issue
- 15
- Pages
- 4604-4608
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2047386852
- Cited by
- 262
- References
- 18
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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