The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Cloning and expression of the human erythropoietin gene.
Open accessAbstract
The human erythropoietin gene has been isolated from a genomic phage library by using mixed 20-mer and 17-mer oligonucleotide probes. The entire coding region of the gene is contained in a 5.4-kilobase HindIII-BamHI fragment. The gene contains four intervening sequences (1562 base pairs) and five exons (582 base pairs). It encodes a 27-amino acid signal peptide and a 166-amino acid mature protein with a calculated Mr of 18,399. The erythropoietin gene, when introduced into Chinese hamster ovary cells, produces erythropoietin that is biologically active in vitro and in vivo.
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Citations
Cites
The liver as a source of extrarenal erythropoietin production
Fried, W. (1972) · Blood · doi:10.1182/blood.v40.5.671.671 · Cited by 235
Cited by
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Semenza, G. L., Nejfelt, M. K., Chi, S. M., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5680 · Cited by 990
Eschbach, J. W., Abdulhadi, M. H., Browne, J. K., Delano, B. G., Downing, M. R., Egrie, J. C., Evans, R. W., Friedman, E. A., Graber, S. E., Haley, N. R., et al. (1989) · Annals of Internal Medicine · doi:10.7326/0003-4819-111-12-992 · Cited by 795
Self-citationPost-transcriptional Regulation of Vascular Endothelial Growth Factor by Hypoxia
Levy, A. P., Levy, N. S., & Goldberg, M. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2746 · Cited by 629
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Hypoxic regulation of erythropoiesis and iron metabolism
Haase, V. H. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00174.2010 · Cited by 347
Oxygen-dependent and tissue-specific regulation of erythropoietin gene expression
Fandrey, J. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00577.2003 · Cited by 243
Bunn, H. F. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011619 · Cited by 234
Blanchard, K. L., Acquaviva, A. M., Galson, D. L., & Bunn, H. F. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5373 · Cited by 215
The HIF pathway and erythrocytosis
Lee, F. S., & Percy, M. J. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130321 · Cited by 177
Development of spirulina for the manufacture and oral delivery of protein therapeutics
Jester, B. W., Zhao, H., Gewe, M., Adame, T., Perruzza, L., Bolick, D. T., Agosti, J., Khuong, N., Kuestner, R., Gamble, C., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01249-7 · Cited by 130
Cheung, W. K., Goon, B. L., Guilfoyle, M. C., & Wacholtz, M. C. (1998) · Clinical Pharmacology & Therapeutics · doi:10.1016/s0009-9236(98)90072-8 · Cited by 112
Structural analysis of the glycosylation of gene-activated erythropoietin (epoetin delta, Dynepo)
Llop, E., Gutiérrez-Gallego, R., Segura, J., Mallorquí, J., & Pascual, J. A. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.08.027 · Cited by 79
Goh, J. S. Y., Liu, Y., Liu, H., Chan, K. F., Wan, C., Teo, G., Zhou, X., Xie, F., Zhang, P., Zhang, Y., et al. (2014) · Biotechnology Journal · doi:10.1002/biot.201300301 · Cited by 22
Thahsin, N., Khan, K. I., Sarwar, A. N. M. R., Sakib, M. N., & Rahman, M. S. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2024.100029 · Cited by 2
Metadata
- Authors
- Lin, F. K., Suggs, S., Lin, C. H., Browne, J. K., Smalling, R., Egrie, J. C., Chen, K. K., Fox, G. M., Martin, F., & Stabinsky, Z.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-11
- Volume
- 82
- Issue
- 22
- Pages
- 7580-7584
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2019289959
- Cited by
- 1,134
- References
- 1
- FWCI
- 18.36
- 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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