The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Structure and function of epidermal growth factor‐like regions in proteins
Open accessAbstract
A sequence about 40 amino acid residues long which has a significant homology to epidermal growth factor (EGF) has been found in many different proteins in single or multiple copies.The homologies per se and available functional data suggest that these domains share some common functional features.One can consider the prototype sequence as that of EGF, a 53-residue peptide, which is derived from a much longer precursor containing nine other copies of EGF-like units.EGF causes pleiotropic proliferative and developmental effects which are mediated by a specific surface receptor endowed with tyrosine kinase activity [1,2].Certain shorter synthetic peptides compete with authentic EGF for receptor binding and mimic some of the functions of EGF, indicating that the minimal receptor binding sequence lies within residues 20-31 [3]; however, addition of the amino-flanking sequences dramatically improves its affinity for the receptor [4].Several proteins which have significant sequence homology with EGF, or that contain one or more EGF-homologous repeats [e.g., urokinase (uPA), laminin Bl and low density lipoprotein receptor (LDL receptor)], are also involved in receptorligand interactions, and the sequences required for
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Human transforming growth factor-α: Precursor structure and expression in E. coli
Derynck, R., Roberts, A. B., Winkler, M. E., Chen, E. Y., & Goeddel, D. V. (1984) · Cell · doi:10.1016/0092-8674(84)90550-6 · Cited by 877
Growth factors: Mechanism of action and relation to oncogenes
Heldin, C.-H., & Westermark, B. (1984) · Cell · doi:10.1016/0092-8674(84)90296-4 · Cited by 854
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Complete nucleotide sequences of the gene for human factor IX (antihemophilic factor B)
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Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors
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Self-citationAppella, E., Robinson, E. A., Ullrich, S. J., Stoppelli, M. P., Corti, A., Cassani, G., & Blasi, F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61211-6 · Cited by 475
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Cited by
Understanding Adipocyte Differentiation
GREGOIRE, F. M., SMAS, C. M., & SUL, H. S. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.3.783 · Cited by 2,376
Proteolytic processing regulates receptor specificity and activity of VEGF-C
Joukov, V., Sorsa, T., Kumar, V., Jeltsch, M., Claesson-Welsh, L., Cao, Y., Saksela, O., Kalkkinen, N., & Alitalo, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3898 · Cited by 773
Tenascin: cDNA cloning and induction by TGF-beta.
Pearson, C. A., Pearson, D., Shibahara, S., Hofsteenge, J., & Chiquet-Ehrismann, R. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03160.x · Cited by 451
Thrombospondins: structure and regulation of expression
Bornstein, P. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.14.1426766 · Cited by 349
An eight cysteine-containing CFEM domain unique to a group of fungal membrane proteins
Kulkarni, R. D., Kelkar, H. S., & Dean, R. A. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00025-2 · Cited by 294
Metadata
- Authors
- Appella, E., Weber, I. T., & Blasi, F.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1988-04-11
- Volume
- 231
- Issue
- 1
- Pages
- 1-4
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2088854697
- Cited by
- 309
- References
- 23
- FWCI
- 8.13
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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