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  Self-compartmentalizing proteases

Lupas, A., Flanagan, J. M., Tamura, T., & Baumeister, W. (1997). Self-compartmentalizing proteases. Trends in Biochemical Sciences, 22(10), 399-404.

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Lupas, A.1, Author              
Flanagan, J. M., Author
Tamura, T., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Escherichia-coli; Saccharomyces-cerevisiae; Crystal-structure; 20s proteasome; Thermoplasma-acidophilum; Molecular chaperone; Protein-degradation; Proteolytic system; Tricorn protease; Complex.; Biochemistry & biophysics.
 Abstract: Among the hundreds of proteases characterized so far, most of which are monomeric or dimeric, there is a small group that form compartments through self-association and that segregate their proteolytic active sites to the interior of these compartments, Although few in number, they represent the main agents of intracellular protein breakdown. They belong to different hydrolase families but have converged towards the same barrel-shaped architecture. Frequently, they are coupled to chaperone-like ATPases of similar quaternary structure that regulate the access to the proteolytic compartments and appear to have been recruited from the same branch of P-loop NTPases. [References: 58]

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 Dates: 1997-10
 Publication Status: Published in print
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 Identifiers: eDoc: 318421
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Title: Trends in Biochemical Sciences
Source Genre: Journal
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Pages: - Volume / Issue: 22 (10) Sequence Number: - Start / End Page: 399 - 404 Identifier: -