The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.
The Proteasome in Modern Drug Discovery: Second Life of a Highly Valuable Drug Target
Open accessAbstract
As the central figure of the cellular protein degradation machinery, the proteasome is critical for cell survival. Having been extensively targeted for inhibition, the constitutive proteasome has proven its role as a highly valuable drug target. However, recent advances in the protein homeostasis field suggest that additional chapters can be added to this successful story. For example, selective immunoproteasome inhibition promises high clinical efficacy for autoimmune disorders and inflammation, and proteasome inhibitors might serve as novel therapeutics for malaria or other microorganisms. Furthermore, utilizing the destructive force of the proteasome for selective degradation of essential drivers of human disorders has opened up a new and exciting area of drug discovery. Thus, the field of proteasome drug discovery still holds exciting questions to be answered and does not simply end with inhibiting the constitutive proteasome.
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“The effect of bortezomib comes from the boronic acid covalently binding to the hydroxy group of the β5 subunit N-terminal threonine of the 20S proteasome, leading to inhibition of the proteasome’s chymotrypsin-like activity125.”
From Advances in covalent drug discovery (2022) · cites this paper as [125]
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Cites
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
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 2,438
Nasir, O. (2013) · Kidney & Blood Pressure Research · doi:10.1159/000350152 · Cited by 2,331
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 2,265
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
Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution
Löwe, J., Stock, D., Jap, B. K., Zwickl, P., Baumeister, W. P., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,540
Ubiquitin: structures, functions, mechanisms
Pickart, C. M., & Eddins, M. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.019 · Cited by 1,491
Induced protein degradation: an emerging drug discovery paradigm
Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486
Self-citationThe proteasome: a suitable antineoplastic target
Adams, J. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1361 · Cited by 1,214
The increasing complexity of the ubiquitin code
Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054
Cited by
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Advances in covalent drug discovery
Boike, L., Henning, N. J., & Nomura, D. K. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00542-z · Cited by 823
Gehringer, M., & Laufer, S. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01153 · Cited by 772
Targeting the ubiquitin-proteasome pathway to overcome anti-cancer drug resistance
Narayanan, S., Cai, C.-Y., Assaraf, Y. G., Guo, H.-Q., Cui, Q., Wei, L., Huang, J.-J., Ashby, C. R., & Chen, Z.-S. (2020) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100663 · Cited by 332
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 243
From Discovery to Bedside: Targeting the Ubiquitin System
Wertz, I. E., & Wang, X. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.10.022 · Cited by 162
Metadata
- Authors
- Cromm, P. M., & Crews, C. M.
- Affiliations
- Yale University (US)
- Corresponding author
- Cromm, Philipp M.
- Crews, Craig M.
- Venue
- ACS Central Science
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-08-07
- Volume
- 3
- Issue
- 8
- Pages
- 830-838
- ISSN
- 2374-7943 (ISSN-L)
- 2374-7951
- PMC
- PMC5571462
- OpenAlex
- W2744284720
- Cited by
- 136
- References
- 85
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 12 · 2023: 18 · 2022: 13 · 2021: 18 · 2020: 27 · 2019: 16 · 2018: 14 · 2017: 2
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Licence
- Locations
- ACS Central Science (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Cancer Institute (R35 CA197589)
- Alexander von Humboldt-Stiftung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- proteasome, proteasome inhibitors, therapeutic target, proteostasis, selective protein degradation, autoimmune disease, inflammation, malaria, antimicrobial agents
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