The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Proposed acquisition of an animal protein domain by bacteria.
Open accessAbstract
A systematic screen of a protein sequence data base confirms that the fibronectin type III (Fn3) domain is widely distributed among animal proteins and occurs also in several bacterial carbohydrate-splitting enzymes. The motif has yet to be identified in proteins from plants or fungi. All indications are that the bacterial sequences are much too similar to the animal type to be the result of conventional vertical descent. Rather, it is likely that the bacterial units were initially acquired from an animal source and are being spread further by horizontal transfers between distantly related bacteria.
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Cites
Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex
de Vos, A. M., Ultsch, M., & Kossiakoff, A. A. (1992) · Science · doi:10.1126/science.1549776 · Cited by 2,239
Structural design and molecular evolution of a cytokine receptor superfamily.
Bazan, J. F. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.6934 · Cited by 2,069
Progressive sequence alignment as a prerequisitetto correct phylogenetic trees
Feng, D.-F., & Doolittle, R. F. (1987) · Journal of Molecular Evolution · doi:10.1007/bf02603120 · Cited by 1,883
Self-citationDatabase of homology‐derived protein structures and the structural meaning of sequence alignment
Sander, C., & Schneider, R. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340090107 · Cited by 1,639
Distinguishing Homologous from Analogous Proteins
Fitch, W. M. (1970) · Systematic Zoology · doi:10.2307/2412448 · Cited by 1,503
Profile analysis: detection of distantly related proteins.
Gribskov, M., McLachlan, A. D., & Eisenberg, D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.13.4355 · Cited by 1,325
Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families
Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., & Warren, R. A. J. (1991) · Microbiological Reviews · doi:10.1128/mmbr.55.2.303-315.1991 · Cited by 961
Bork, P., Sander, C., & Valencia, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7290 · Cited by 811
Self-citationCrystal structure of an HIV-binding recombinant fragment of human CD4
Ryu, S.-E., Kwong, P. D., Truneh, A., Porter, T. G., Arthos, J. A., Rosenberg, M. J., Dai, X., Xuong, N., Axel, R., Sweet, R. W., et al. (1990) · Nature · doi:10.1038/348419a0 · Cited by 552
Cited by
Leahy, D. J., Aukhil, I., & Erickson, H. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81002-8 · Cited by 640
Irisin Mediates Effects on Bone and Fat via αV Integrin Receptors
Kim, H., Wrann, C. D., Jedrychowski, M., Vidoni, S., Kitase, Y., Nagano, K., Zhou, C., Chou, J., Parkman, V.-J. A., Novick, S. J., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.025 · Cited by 638
“FNIII domains in polypeptides are quite common, with over 200 polypeptides having these motifs (Bork and Doolittle, 1992; Potts and Campbell, 1994).”
The fibronectin type III domain as a scaffold for novel binding proteins
Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585
Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., & Pabo, C. O. (1994) · Cell · doi:10.1016/0092-8674(94)90231-3 · Cited by 506
Bork, P. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170405 · Cited by 508
Self-citation
Metadata
- Authors
- Bork, P., & Doolittle, R. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-10
- Volume
- 89
- Issue
- 19
- Pages
- 8990-8994
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2060888437
- Cited by
- 255
- References
- 25
- FWCI
- 6.36
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
