The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins
Abstract
We present the cDNA and amino acid sequences of a cytoskeletal keratin from human epidermis (Mr = 56K) that belongs to one of the two classes of keratins (Type I and Type II) present in all vertebrates. In these two types of keratins the central approximately 300 residue long regions share approximately 30% homology both with one another and with the sequences of other IF proteins. Within this region, all IF proteins are predicted to contain four helical domains demarcated from one another by three regions of beta-turns. The amino and carboxy termini of the Type II keratin are very different from those of microfibrillar keratins and other nonkeratin IF proteins. However, they contain unusual glycine-rich tandem repeats similar to the amino terminus of the Type I keratin. Thus the size heterogeneity among keratins appears to be a result of differences in the length of the terminal ends rather than the structurally conserved central region.
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Cites
Moll, R., Franke, W. W., Schiller, D. L., Geiger, B., & Krepler, R. (1982) · Cell · doi:10.1016/0092-8674(82)90400-7 · Cited by 5,247
Garnier, J., Osguthorpe, D. J., & Robson, B. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90297-8 · Cited by 4,523
Prediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Prediction of the Secondary Structure of Proteins from their Amino Acid Sequence
Chou, P. Y., & Fasman, G. D. (1979) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470122921.ch2 · Cited by 2,915
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
Intermediate Filaments: A Chemically Heterogeneous, Developmentally Regulated Class of Proteins
Lazarides, E. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.001251 · Cited by 1,010
The sequence 5′-AAUAAA-3′ forms part of the recognition site for polyadenylation of late SV40 mRNAs
Fitzgerald, M. (1981) · Cell · doi:10.1016/0092-8674(81)90521-3 · Cited by 776
Keratin cytoskeletons in epithelial cells of internal organs
Sun, T.-T., Shih, C., & Green, H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.6.2813 · Cited by 484
Compound Helical Configurations of Polypeptide Chains: Structure of Proteins of the α-Keratin Type
PAULING, L., & COREY, R. B. (1953) · Nature · doi:10.1038/171059a0 · Cited by 433
Geisler, N., & Weber, K. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01368.x · Cited by 428
Cited by
Yuspa, S. H., Kilkenny, A. E., Steinert, P. M., & Roop, D. R. (1989) · The Journal of cell biology · doi:10.1083/jcb.109.3.1207 · Cited by 572
The molecular biology of intermediate filaments
Steinert, P. M., Steven, A. C., & Roop, D. R. (1985) · Cell · doi:10.1016/0092-8674(85)90098-4 · Cited by 473
Antibody markers of basal cells in complex epithelia
Purkis, P. E., Steel, J. B., Mackenzie, I. C., Nathrath, W. B. J., Leigh, I. M., & Lane, E. B. (1990) · Journal of Cell Science · doi:10.1242/jcs.97.1.39 · Cited by 379
Metadata
- Authors
- Hanukoglu, I., & Fuchs, E.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1983-07
- Volume
- 33
- Issue
- 3
- Pages
- 915-924
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2071761976
- Cited by
- 323
- References
- 30
- FWCI
- 18.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hanukoglu, I., & Fuchs, E. (1983). The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell. https://doi.org/10.1016/0092-8674(83)90034-x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
