The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
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Citations
Cites
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Cited by
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764
Self-citationRegulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.082307.091526 · Cited by 1,396
The proteasome: overview of structure and functions
TANAKA, K. (2009) · Proceedings of the Japan Academy, Series B · doi:10.2183/pjab.85.12 · Cited by 862
Complete subunit architecture of the proteasome regulatory particle
Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
Molecular mechanisms of proteasome assembly
Murata, S., Yashiroda, H., & Tanaka, K. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2630 · Cited by 546
Metadata
- Authors
- Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K. J., & Groll, M.
- Venue
- Nature
- Published
- 2008-05
- Volume
- 453
- Issue
- 7194
- Pages
- 548-552
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2162263177
- Cited by
- 343
- References
- 1
- FWCI
- 11.91
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K. J., & Groll, M. (2008). Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. https://doi.org/10.1038/nature06924
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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.