The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HslV by a new class of inhibitors
Open accessAbstract
The proteasome is a multicatalytic protease complex that plays a key role in diverse cellular functions. The peptide vinyl sulfone, carboxybenzyl-leucyl-leucyl-leucine vinyl sulfone (Z-L 3 VS) covalently inhibits the trypsin-like, chymotrypsin-like and, unlike lactacystin, also the peptidylglutamyl peptidase activity in isolated proteasomes, and blocks their function in living cells. Although described as a class of mechanism-based inhibitors for cysteine proteases, the peptide vinyl sulfone Z-L 3 VS and a 125 I-labeled nitrophenol derivative (125 I-NIP-L 3 VS) covalently modify the active site threonine of the catalytic β subunits of the proteasome. Modification of Thermoplasma proteasomes demonstrates the requirement for a hydroxyl amino acid (threonine, serine) as nucleophile at the β subunit’s NH 2 terminus.125 I-NIP-L 3 VS covalently modifies the HslV subunit of the Escherichia coli protease complex HslV/HslU, a reaction that requires ATP, and supports a catalytic mechanism shared with that of the eukaryotic proteasome.
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Self-citationSTRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
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Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution
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Cited by
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
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Self-citationThe proteasome: a suitable antineoplastic target
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Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
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Metadata
- Authors
- Bogyo, M., McMaster, J. S., Gaczynska, M., Tortorella, D., Goldberg, A. L., & Ploegh, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-06-24
- Volume
- 94
- Issue
- 13
- Pages
- 6629-6634
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1968330653
- Cited by
- 447
- References
- 23
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HslV by a new class of inhibitors. https://app.cochat.ai/papers/10.1073/pnas.94.13.6629
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- Bogyo, M., McMaster, J. S., Gaczynska, M., Tortorella, D., Goldberg, A. L., & Ploegh, H. (1997). Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.13.6629
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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