The DOI matches its Crossref record; 98 of the 98 references it cites were found in a registry or an index.
ClpXP, an ATP-powered unfolding and protein-degradation machine
Open accessAbstract
ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies.
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Cites
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Self-citationAAA+ Proteases: ATP-Fueled Machines of Protein Destruction
Sauer, R. T., & Baker, T. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-172623 · Cited by 762
Self-citationEVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS
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Self-citationThe Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
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Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
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Varnaitė, R., & MacNeill, S. A. (2016) · PROTEOMICS · doi:10.1002/pmic.201600123 · Cited by 173
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Metadata
- Authors
- Baker, T. A., & Sauer, R. T.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-01
- Volume
- 1823
- Issue
- 1
- Pages
- 15-28
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2213968760
- Cited by
- 468
- References
- 98
- FWCI
- 8.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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