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  Eubacterial proteasomes

Lupas, A., Zühl, F., Tamura, T., Wolf, S., Nagy, I., Demot, R., et al. (1997). Eubacterial proteasomes. Molecular Biology Reports, 24(1-2), 125-131.

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Lupas, A.1, Author              
Zühl, F.1, Author              
Tamura, T., Author
Wolf, S.1, Author              
Nagy, I.1, Author              
Demot, R., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Proteasome; Hslvu; Clp; Multicatalytic protease; Atp-dependent proteolysis; Rhodococcus erythropolis.; Multicatalytic proteinase; Thermoplasma-acidophilum; Structural features; Electron-microscopy; Escherichia-coli; 20s proteasome; Complex dimer; 26-s protease; 26s protease; Subunit.; Molecular biology & genetics.
 Abstract: Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependentpathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure. [References: 50]

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 Dates: 1997-03
 Publication Status: Published in print
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 Identifiers: eDoc: 318360
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Title: Molecular Biology Reports
Source Genre: Journal
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Pages: - Volume / Issue: 24 (1-2) Sequence Number: - Start / End Page: 125 - 131 Identifier: -