The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death
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Proceedings of the National Academy of Sciences (PNAS), a peer reviewed journal of the National Academy of Sciences (NAS) - an authoritative source of high-impact, original research that broadly spans the biological, physical, and social sciences.
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Citations
Cites
STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,487
Structure of 20S proteasome from yeast at 2.4Å resolution
Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,257
The ubiquitin-proteasome proteolytic pathway
Ciechanover, A. (1994) · Cell · doi:10.1016/0092-8674(94)90396-4 · Cited by 1,791
Self-citationUBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,692
Mahajan, R., Delphin, C., Guan, T., Gerace, L., & Melchior, F. (1997) · Cell · doi:10.1016/s0092-8674(00)81862-0 · Cited by 1,256
Varshavsky, A. (1992) · Cell · doi:10.1016/0092-8674(92)90285-k · Cited by 467
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
Lam, Y. A., Xu, W., DeMartino, G. N., & Cohen, R. E. (1997) · Nature · doi:10.1038/385737a0 · Cited by 455
Ma, C. P., Slaughter, C. A., & DeMartino, G. N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50047-3 · Cited by 439
Nocker, S. V., Sadis, S., Rubin, D. M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., & Vierstra, R. D. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6020 · Cited by 388
Purification of an 11 S regulator of the multicatalytic protease.
Dubiel, W., Pratt, G., Ferrell, K., & Rechsteiner, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41681-x · Cited by 378
Cited by
Jiang, Y.-H., Armstrong, D., Albrecht, U., Atkins, C. M., Noebels, J. L., Eichele, G., Sweatt, J. D., & Beaudet, A. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)80596-6 · Cited by 852
Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724
Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets
Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563
“The UPS and UBL conjugation pathways have multiple essential biological roles and it is not surprising that their function, and often malfunction, are important factors in various human disease”
BackgroundMendenhall, M. D., & Hodge, A. E. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.4.1191-1243.1998 · Cited by 429
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395
Metadata
- Authors
- Ciechanover, A., & Schwartz, A. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-03-17
- Volume
- 95
- Issue
- 6
- Pages
- 2727-2730
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2087092058
- Cited by
- 507
- References
- 24
- FWCI
- 8.67
- Type
- journal article
- Language
- en
- Open access
- green
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- Ciechanover, A., & Schwartz, A. L. (1998). The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.6.2727
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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.
