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Cited by 500

The DOI matches its OpenAlex record; 1 of the 1 references it cites were found in a registry or an index.

Regulation by proteolysis: energy-dependent proteases and their targets

Open access
Susan Gottesman, Michael R. Maurizi·1992·Microbiological Reviews

Abstract

A number of critical regulatory proteins in both prokaryotic and eukaryotic cells are subject to rapid, energy-dependent proteolysis. Rapid degradation combined with control over biosynthesis provides a mechanism by which the availability of a protein can be limited both temporally and spatially. Highly unstable regulatory proteins are involved in numerous biological functions, particularly at the commitment steps in developmental pathways and in emergency responses. The proteases involved in energy-dependent proteolysis are large proteins with the ability to use ATP to scan for appropriate targets and degrade complete proteins in a processive manner. These cytoplasmic proteases are also able to degrade many abnormal proteins in the cell.

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OpenAlex · 10.1128/mmbr.56.4.592-621.1992

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Metadata

Authors
Gottesman, S., & Maurizi, M. R.
Venue
Microbiological Reviews
Publisher
American Society for Microbiology
Published
1992-01-01
Volume
56
Issue
4
Pages
592-621
ISSN
0146-0749 (ISSN-L)
OpenAlex
W1897176773
Cited by
500
References
1
FWCI
12.72
Type
journal article
Language
en
Open access
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CoChat. (2026). Citation check: Regulation by proteolysis: energy-dependent proteases and their targets. https://app.cochat.ai/papers/10.1128/mmbr.56.4.592-621.1992
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Gottesman, S., & Maurizi, M. R. (1992). Regulation by proteolysis: energy-dependent proteases and their targets. Microbiological Reviews. https://doi.org/10.1128/mmbr.56.4.592-621.1992

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.