The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Cupins: the most functionally diverse protein superfamily?
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Citations
Cites
Semidwarf ( sd-1 ), “green revolution” rice, contains a defective gibberellin 20-oxidase gene
Spielmeyer, W., Ellis, M. H., & Chandler, P. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132266399 · Cited by 920
Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T., & Sedgwick, B. (2002) · Nature · doi:10.1038/nature00908 · Cited by 762
Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y.-M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200273200 · Cited by 719
Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
Aas, P. A., Otterlei, M., Falnes, P. Ø., Vågbø, C. B., Skorpen, F., Akbari, M., Sundheim, O., Bjørås, M., Slupphaug, G., Seeberg, E., et al. (2003) · Nature · doi:10.1038/nature01363 · Cited by 638
AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
Falnes, P. Ø., Johansen, R. F., & Seeberg, E. (2002) · Nature · doi:10.1038/nature01048 · Cited by 616
Monna, L. (2002) · DNA Research · doi:10.1093/dnares/9.1.11 · Cited by 570
Aravind, L., & Koonin, E. V. (2001) · Genome Biology · doi:10.1186/gb-2001-2-3-research0007 · Cited by 539
Structure and Mechanism of Anthocyanidin Synthase from Arabidopsis thaliana
Wilmouth, R. C., Turnbull, J. J., Welford, R. W. D., Clifton, I. J., Prescott, A. G., & Schofield, C. J. (2002) · Structure · doi:10.1016/s0969-2126(01)00695-5 · Cited by 359
Evolution of functional diversity in the cupin superfamily
Dunwell, J. M., Culham, A., Carter, C. E., Sosa-Aguirre, C. R., & Goodenough, P. W. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01981-8 · Cited by 341
Self-citationDunwell, J. M., Khuri, S., & Gane, P. J. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.1.153-179.2000 · Cited by 335
Self-citation
Cited by
Panel), E. P. O. G. M. O. (. (2010) · EFSA Journal · doi:10.2903/j.efsa.2010.1700 · Cited by 608
Trace metal metabolism in plants
Andresen, E., Peiter, E., & Küpper, H. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/erx465 · Cited by 431
β‐Rolls, β‐Helices, and Other β‐Solenoid Proteins
Kajava, A. V., & Steven, A. C. (2006) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(06)73003-0 · Cited by 149
Allergenicity of Peanut Allergens and Its Dependence on the Structure
Geng, Q., Zhang, Y., Song, M., Zhou, X., Tang, Y., Wu, Z., & Chen, H. (2023) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13101 · Cited by 41
Architecture of the spinach plastid-encoded RNA polymerase
Wang, T., Wang, G.-L., Fang, Y., Zhang, Y., Peng, W., Zhou, Y., Zhang, A., Yu, L.-J., & Lu, C. (2024) · Nature Communications · doi:10.1038/s41467-024-54266-2 · Cited by 17
Metadata
- Authors
- Dunwell, J. M., Purvis, A., & Khuri, S.
- Venue
- Phytochemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 65
- Issue
- 1
- Pages
- 7-17
- ISSN
- 0031-9422 (ISSN-L)
- OpenAlex
- W2078336779
- Cited by
- 559
- References
- 32
- FWCI
- 8.48
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Cupins: the most functionally diverse protein superfamily? https://app.cochat.ai/papers/10.1016/j.phytochem.2003.08.016
- The paper
- Dunwell, J. M., Purvis, A., & Khuri, S. (2004). Cupins: the most functionally diverse protein superfamily? Phytochemistry. https://doi.org/10.1016/j.phytochem.2003.08.016
Data sources
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.
